메뉴 건너뛰기




Volumn 352, Issue 1, 2013, Pages 5-20

Arrivals and departures at the plasma membrane: Direct and indirect transport routes

Author keywords

Exosome; Golgi bypass pathway; mRNA transport; Pre Golgi intermediate compartment; Unconventional secretion

Indexed keywords

BREFELDIN A; CD45 ANTIGEN; COAT PROTEIN COMPLEX II; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; CYTOPLASM PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90; LIPOCORTIN 2; MESSENGER RNA; PROTEOGLYCAN; RIBONUCLEOPROTEIN;

EID: 84875275175     PISSN: 0302766X     EISSN: 14320878     Source Type: Journal    
DOI: 10.1007/s00441-012-1409-5     Document Type: Review
Times cited : (29)

References (233)
  • 1
    • 77149131806 scopus 로고    scopus 로고
    • Plant secretome: Unlocking secrets of the secreted proteins
    • 19953550 1:CAS:528:DC%2BC3cXis1ektbg%3D
    • Agrawal GK, Jwa NS, Lebrun MH, Job D, Rakwal R (2010) Plant secretome: unlocking secrets of the secreted proteins. Proteomics 10:799-827
    • (2010) Proteomics , vol.10 , pp. 799-827
    • Agrawal, G.K.1    Jwa, N.S.2    Lebrun, M.H.3    Job, D.4    Rakwal, R.5
  • 2
    • 30044440555 scopus 로고    scopus 로고
    • A novel type of detergent-resistant membranes may contribute to an early protein sorting event in epithelial cells
    • 16230359 1:CAS:528:DC%2BD2MXhtlCmsLjE
    • Alfalah M, Wetzel G, Fischer I, Busche R, Sterchi EE, Zimmer KP, Sallmann HP, Naim HY (2005) A novel type of detergent-resistant membranes may contribute to an early protein sorting event in epithelial cells. J Biol Chem 280:42636-42643
    • (2005) J Biol Chem , vol.280 , pp. 42636-42643
    • Alfalah, M.1    Wetzel, G.2    Fischer, I.3    Busche, R.4    Sterchi, E.E.5    Zimmer, K.P.6    Sallmann, H.P.7    Naim, H.Y.8
  • 3
    • 8544232810 scopus 로고    scopus 로고
    • TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway
    • 15319436 1:CAS:528:DC%2BD2cXovVCntLc%3D
    • Amzallag N, Passer BJ, Allanic D, Segura E, Thery C, Goud B, Amson R, Telerman A (2004) TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway. J Biol Chem 279:46104-46112
    • (2004) J Biol Chem , vol.279 , pp. 46104-46112
    • Amzallag, N.1    Passer, B.J.2    Allanic, D.3    Segura, E.4    Thery, C.5    Goud, B.6    Amson, R.7    Telerman, A.8
  • 4
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
    • 10233156 1:CAS:528:DyaK1MXjsFSit7s%3D
    • Andrei C, Dazzi C, Lotti L, Torrisi MR, Chimini G, Rubartelli A (1999) The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles. Mol Biol Cell 10:1463-1475
    • (1999) Mol Biol Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1    Dazzi, C.2    Lotti, L.3    Torrisi, M.R.4    Chimini, G.5    Rubartelli, A.6
  • 5
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • 15534004 1:CAS:528:DC%2BD2cXpvVCns74%3D
    • Ang AL, Taguchi T, Francis S, Folsch H, Murrells LJ, Pypaert M, Warren G, Mellman I (2004) Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J Cell Biol 167:531-543
    • (2004) J Cell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Folsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 6
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function
    • 16723730 1:CAS:528:DC%2BD28Xms1Gju7k%3D
    • Appenzeller-Herzog C, Hauri HP (2006) The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci 119:2173-2183
    • (2006) J Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 7
    • 34247642111 scopus 로고    scopus 로고
    • MRNAs encoding polarity and exocytosis factors are cotransported with the cortical endoplasmic reticulum to the incipient bud in Saccharomyces cerevisiae
    • 17339339 1:CAS:528:DC%2BD2sXltFCksb4%3D
    • Aronov S, Gelin-Licht R, Zipor G, Haim L, Safran E, Gerst JE (2007) mRNAs encoding polarity and exocytosis factors are cotransported with the cortical endoplasmic reticulum to the incipient bud in Saccharomyces cerevisiae. Mol Cell Biol 27:3441-3455
    • (2007) Mol Cell Biol , vol.27 , pp. 3441-3455
    • Aronov, S.1    Gelin-Licht, R.2    Zipor, G.3    Haim, L.4    Safran, E.5    Gerst, J.E.6
  • 8
    • 0037184948 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase CD45 reaches the cell surface via golgi-dependent and -independent pathways
    • 12386161 1:CAS:528:DC%2BD38Xps12nsrk%3D
    • Baldwin TA, Ostergaard HL (2002) The protein-tyrosine phosphatase CD45 reaches the cell surface via Golgi-dependent and -independent pathways. J Biol Chem 277:50333-50340
    • (2002) J Biol Chem , vol.277 , pp. 50333-50340
    • Baldwin, T.A.1    Ostergaard, H.L.2
  • 9
    • 0034328820 scopus 로고    scopus 로고
    • Traffic pattern of cystic fibrosis transmembrane regulator through the early exocytic pathway
    • 11208075 1:CAS:528:DC%2BD3cXoslWrtrY%3D
    • Bannykh SI, Bannykh GI, Fish KN, Moyer BD, Riordan JR, Balch WE (2000) Traffic pattern of cystic fibrosis transmembrane regulator through the early exocytic pathway. Traffic 1:852-870
    • (2000) Traffic , vol.1 , pp. 852-870
    • Bannykh, S.I.1    Bannykh, G.I.2    Fish, K.N.3    Moyer, B.D.4    Riordan, J.R.5    Balch, W.E.6
  • 10
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • 9346242 1:CAS:528:DyaK2sXntVyiu7c%3D
    • Barr FA, Puype M, Vandekerckhove J, Warren G (1997) GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91:253-262
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 11
    • 77449102731 scopus 로고    scopus 로고
    • Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages
    • 19903899 1:CAS:528:DC%2BC3cXhsFegsbk%3D
    • Barres C, Blanc L, Bette-Bobillo P, Andre S, Mamoun R, Gabius HJ, Vidal M (2010) Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood 115:696-705
    • (2010) Blood , vol.115 , pp. 696-705
    • Barres, C.1    Blanc, L.2    Bette-Bobillo, P.3    Andre, S.4    Mamoun, R.5    Gabius, H.J.6    Vidal, M.7
  • 13
    • 35348913641 scopus 로고    scopus 로고
    • Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA
    • 17698811 1:CAS:528:DC%2BD2sXpvVGjurw%3D
    • Bi J, Tsai NP, Lu HY, Loh HH, Wei LN (2007) Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA. Proc Natl Acad Sci U S A 104:13810-13815
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13810-13815
    • Bi, J.1    Tsai, N.P.2    Lu, H.Y.3    Loh, H.H.4    Wei, L.N.5
  • 14
    • 77951488197 scopus 로고    scopus 로고
    • Reticulocyte membrane remodeling: Contribution of the exosome pathway
    • 20173636 1:CAS:528:DC%2BC3cXkvVymsbg%3D
    • Blanc L, Vidal M (2010) Reticulocyte membrane remodeling: contribution of the exosome pathway. Curr Opin Hematol 17:177-183
    • (2010) Curr Opin Hematol , vol.17 , pp. 177-183
    • Blanc, L.1    Vidal, M.2
  • 17
    • 0344081339 scopus 로고    scopus 로고
    • The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway
    • 12972410 1:CAS:528:DC%2BD3sXpt1Gjt7w%3D
    • Bonnon C, Goutebroze L, Denisenko-Nehrbass N, Girault JA, Faivre-Sarrailh C (2003) The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway. J Biol Chem 278:48339-48347
    • (2003) J Biol Chem , vol.278 , pp. 48339-48347
    • Bonnon, C.1    Goutebroze, L.2    Denisenko-Nehrbass, N.3    Girault, J.A.4    Faivre-Sarrailh, C.5
  • 18
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • 2510935 1:CAS:528:DyaK3cXjtlyisQ%3D%3D
    • Booth C, Koch GL (1989) Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59:729-737
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.2
  • 19
    • 79851511792 scopus 로고    scopus 로고
    • Targeting pathways of C-tail-anchored proteins
    • 20646998 1:CAS:528:DC%2BC3MXhvFentbs%3D
    • Borgese N, Fasana E (2011) Targeting pathways of C-tail-anchored proteins. Biochim Biophys Acta 1808:937-946
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 937-946
    • Borgese, N.1    Fasana, E.2
  • 20
    • 33748273867 scopus 로고    scopus 로고
    • Genetic screen for signal peptides in Hydra reveals novel secreted proteins and evidence for non-classical protein secretion
    • 16814424
    • Bottger A, Strasser D, Alexandrova O, Levin A, Fischer S, Lasi M, Rudd S, David CN (2006) Genetic screen for signal peptides in Hydra reveals novel secreted proteins and evidence for non-classical protein secretion. Eur J Cell Biol 85:1107-1117
    • (2006) Eur J Cell Biol , vol.85 , pp. 1107-1117
    • Bottger, A.1    Strasser, D.2    Alexandrova, O.3    Levin, A.4    Fischer, S.5    Lasi, M.6    Rudd, S.7    David, C.N.8
  • 21
    • 0024437936 scopus 로고
    • A restricted set of apical proteins recycle through the trans-Golgi network in MDCK cells
    • 2510995 1:STN:280:DyaK3c%2FlvF2isg%3D%3D
    • Brandli AW, Simons K (1989) A restricted set of apical proteins recycle through the trans-Golgi network in MDCK cells. EMBO J 8:3207-3213
    • (1989) EMBO J , vol.8 , pp. 3207-3213
    • Brandli, A.W.1    Simons, K.2
  • 22
    • 70450225048 scopus 로고    scopus 로고
    • ER exit sites - Localization and control of COPII vesicle formation
    • 19850039 1:CAS:528:DC%2BD1MXhsFSht7fE
    • Budnik A, Stephens DJ (2009) ER exit sites - localization and control of COPII vesicle formation. FEBS Lett 583:3796-3803
    • (2009) FEBS Lett , vol.583 , pp. 3796-3803
    • Budnik, A.1    Stephens, D.J.2
  • 23
    • 69949122067 scopus 로고    scopus 로고
    • Unconventional secretion of tubby and tubby-like protein 1
    • 19695251 1:CAS:528:DC%2BD1MXhtFajsbrJ
    • Caberoy NB, Li W (2009) Unconventional secretion of tubby and tubby-like protein 1. FEBS Lett 583:3057-3062
    • (2009) FEBS Lett , vol.583 , pp. 3057-3062
    • Caberoy, N.B.1    Li, W.2
  • 25
    • 33748135979 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent exocytosis of interleukin-1beta- containing secretory lysosomes: Role of microtubules
    • 16684958 1:CAS:528:DC%2BD28Xpt1Sltbw%3D
    • Carta S, Tassi S, Semino C, Fossati G, Mascagni P, Dinarello CA, Rubartelli A (2006) Histone deacetylase inhibitors prevent exocytosis of interleukin-1beta-containing secretory lysosomes: role of microtubules. Blood 108:1618-1626
    • (2006) Blood , vol.108 , pp. 1618-1626
    • Carta, S.1    Tassi, S.2    Semino, C.3    Fossati, G.4    Mascagni, P.5    Dinarello, C.A.6    Rubartelli, A.7
  • 26
    • 33646417688 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 induces the non-classical secretion of peroxiredoxin-I in A549 cells
    • 16677601 1:CAS:528:DC%2BD28XkslSnt7k%3D
    • Chang JW, Lee SH, Lu Y, Yoo YJ (2006) Transforming growth factor-beta1 induces the non-classical secretion of peroxiredoxin-I in A549 cells. Biochem Biophys Res Commun 345:118-123
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 118-123
    • Chang, J.W.1    Lee, S.H.2    Lu, Y.3    Yoo, Y.J.4
  • 27
    • 0037372244 scopus 로고    scopus 로고
    • Evidence for a role of the adenosine 5'-triphosphate-binding cassette transporter A1 in the externalization of annexin i from pituitary folliculo-stellate cells
    • 12586783 1:CAS:528:DC%2BD3sXhslCqtrk%3D
    • Chapman LP, Epton MJ, Buckingham JC, Morris JF, Christian HC (2003) Evidence for a role of the adenosine 5'-triphosphate-binding cassette transporter A1 in the externalization of annexin I from pituitary folliculo-stellate cells. Endocrinology 144:1062-1073
    • (2003) Endocrinology , vol.144 , pp. 1062-1073
    • Chapman, L.P.1    Epton, M.J.2    Buckingham, J.C.3    Morris, J.F.4    Christian, H.C.5
  • 28
    • 0027078625 scopus 로고
    • Isolation and characterization of a brefeldin A-resistant mutant of monkey kidney Vero cells
    • 1459197 1:CAS:528:DyaK3sXhtl2gtro%3D
    • Chen CH, Kuwazuru Y, Yoshida T, Nambiar M, Wu HC (1992) Isolation and characterization of a brefeldin A-resistant mutant of monkey kidney Vero cells. Exp Cell Res 203:321-328
    • (1992) Exp Cell Res , vol.203 , pp. 321-328
    • Chen, C.H.1    Kuwazuru, Y.2    Yoshida, T.3    Nambiar, M.4    Wu, H.C.5
  • 29
    • 0025740387 scopus 로고
    • Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland
    • 1824943 1:CAS:528:DyaK3MXpvV2juw%3D%3D
    • Christmas P, Callaway J, Fallon J, Jones J, Haigler HT (1991) Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland. J Biol Chem 266:2499-2507
    • (1991) J Biol Chem , vol.266 , pp. 2499-2507
    • Christmas, P.1    Callaway, J.2    Fallon, J.3    Jones, J.4    Haigler, H.T.5
  • 30
    • 0026506801 scopus 로고
    • Segregation of secretory material in all elements of the Golgi apparatus in principal epithelial cells of the rat seminal vesicle
    • 1543259 1:STN:280:DyaK387otV2ktw%3D%3D
    • Clermont Y, Rambourg A, Hermo L (1992) Segregation of secretory material in all elements of the Golgi apparatus in principal epithelial cells of the rat seminal vesicle. Anat Rec 232:349-358
    • (1992) Anat Rec , vol.232 , pp. 349-358
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 31
    • 55049087015 scopus 로고    scopus 로고
    • The regulated exocytosis of enlargeosomes is mediated by a SNARE machinery that includes VAMP4
    • 18713833 1:CAS:528:DC%2BD1cXhtlWntLrF
    • Cocucci E, Racchetti G, Rupnik M, Meldolesi J (2008) The regulated exocytosis of enlargeosomes is mediated by a SNARE machinery that includes VAMP4. J Cell Sci 121:2983-2991
    • (2008) J Cell Sci , vol.121 , pp. 2983-2991
    • Cocucci, E.1    Racchetti, G.2    Rupnik, M.3    Meldolesi, J.4
  • 32
    • 59249089695 scopus 로고    scopus 로고
    • Shedding microvesicles: Artefacts no more
    • 19144520 1:CAS:528:DC%2BD1MXhs1amt7Y%3D
    • Cocucci E, Racchetti G, Meldolesi J (2009) Shedding microvesicles: artefacts no more. Trends Cell Biol 19:43-51
    • (2009) Trends Cell Biol , vol.19 , pp. 43-51
    • Cocucci, E.1    Racchetti, G.2    Meldolesi, J.3
  • 33
    • 13544276472 scopus 로고    scopus 로고
    • The role of membranes and membrane trafficking in RNA localization
    • 15601254 1:CAS:528:DC%2BD2MXhtlSrtL4%3D
    • Cohen RS (2005) The role of membranes and membrane trafficking in RNA localization. Biol Cell 97:5-18
    • (2005) Biol Cell , vol.97 , pp. 5-18
    • Cohen, R.S.1
  • 34
    • 13544257399 scopus 로고    scopus 로고
    • How and why does beta-actin mRNA target?
    • 15601261 1:CAS:528:DC%2BD2MXhtlSrtLk%3D
    • Condeelis J, Singer RH (2005) How and why does beta-actin mRNA target? Biol Cell 97:97-110
    • (2005) Biol Cell , vol.97 , pp. 97-110
    • Condeelis, J.1    Singer, R.H.2
  • 35
    • 77949395187 scopus 로고    scopus 로고
    • Association of coagulation factor XIII-A with Golgi proteins within monocyte-macrophages: Implications for subcellular trafficking and secretion
    • 20086247 1:CAS:528:DC%2BC3cXksFOhsLo%3D
    • Cordell PA, Kile BT, Standeven KF, Josefsson EC, Pease RJ, Grant PJ (2010) Association of coagulation factor XIII-A with Golgi proteins within monocyte-macrophages: implications for subcellular trafficking and secretion. Blood 115:2674-2681
    • (2010) Blood , vol.115 , pp. 2674-2681
    • Cordell, P.A.1    Kile, B.T.2    Standeven, K.F.3    Josefsson, E.C.4    Pease, R.J.5    Grant, P.J.6
  • 36
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • 12535523 1:CAS:528:DC%2BD3sXhtFahu7g%3D
    • Daniels R, Kurowski B, Johnson AE, Hebert DN (2003) N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell 11:79-90
    • (2003) Mol Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 37
    • 0347481133 scopus 로고    scopus 로고
    • Nonclassical secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane
    • 14661980 1:CAS:528:DC%2BD3sXovFOgs7k%3D
    • Danielsen EM, van Deurs B, Hansen GH (2003) Nonclassical secretion of annexin A2 to the lumenal side of the enterocyte brush border membrane. Biochemistry 42:14670-14676
    • (2003) Biochemistry , vol.42 , pp. 14670-14676
    • Danielsen, E.M.1    Van Deurs, B.2    Hansen, G.H.3
  • 40
    • 4344672352 scopus 로고    scopus 로고
    • Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in furin-negative colon carcinoma LoVo cells
    • 15260832 1:CAS:528:DC%2BD2cXms1ekt74%3D
    • Deryugina EI, Ratnikov BI, Yu Q, Baciu PC, Rozanov DV, Strongin AY (2004) Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in furin-negative colon carcinoma LoVo cells. Traffic 5:627-641
    • (2004) Traffic , vol.5 , pp. 627-641
    • Deryugina, E.I.1    Ratnikov, B.I.2    Yu, Q.3    Baciu, P.C.4    Rozanov, D.V.5    Strongin, A.Y.6
  • 42
    • 79551493048 scopus 로고    scopus 로고
    • Conditioned media from cell lines: A complementary model to clinical specimens for the discovery of disease-specific biomarkers
    • 21229588 1:CAS:528:DC%2BC3MXhsVSnu7Y%3D
    • Dowling P, Clynes M (2011) Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers. Proteomics 11:794-804
    • (2011) Proteomics , vol.11 , pp. 794-804
    • Dowling, P.1    Clynes, M.2
  • 43
    • 34247872880 scopus 로고    scopus 로고
    • Identification of a signal peptide for unconventional secretion
    • 17242404 1:CAS:528:DC%2BD2sXivV2mtro%3D
    • Dupont E, Prochiantz A, Joliot A (2007) Identification of a signal peptide for unconventional secretion. J Biol Chem 282:8994-9000
    • (2007) J Biol Chem , vol.282 , pp. 8994-9000
    • Dupont, E.1    Prochiantz, A.2    Joliot, A.3
  • 44
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta
    • 22068051 1:CAS:528:DC%2BC3MXhsVejsr%2FF
    • Dupont N, Jiang S, Pilli M, Ornatowski W, Bhattacharya D, Deretic V (2011) Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta. EMBO J 30:4701-4711
    • (2011) EMBO J , vol.30 , pp. 4701-4711
    • Dupont, N.1    Jiang, S.2    Pilli, M.3    Ornatowski, W.4    Bhattacharya, D.5    Deretic, V.6
  • 45
    • 77149155386 scopus 로고    scopus 로고
    • Unconventional secretion of Acb1 is mediated by autophagosomes
    • 20156967 1:CAS:528:DC%2BC3cXislWgsrs%3D
    • Duran JM, Anjard C, Stefan C, Loomis WF, Malhotra V (2010) Unconventional secretion of Acb1 is mediated by autophagosomes. J Cell Biol 188:527-536
    • (2010) J Cell Biol , vol.188 , pp. 527-536
    • Duran, J.M.1    Anjard, C.2    Stefan, C.3    Loomis, W.F.4    Malhotra, V.5
  • 46
    • 53249142239 scopus 로고    scopus 로고
    • CD45 glycosylation controls T-cell life and death
    • 18607388 1:CAS:528:DC%2BD1cXhtF2jsrzJ
    • Earl LA, Baum LG (2008) CD45 glycosylation controls T-cell life and death. Immunol Cell Biol 86:608-615
    • (2008) Immunol Cell Biol , vol.86 , pp. 608-615
    • Earl, L.A.1    Baum, L.G.2
  • 47
    • 68649102975 scopus 로고    scopus 로고
    • Mechanisms of interleukin-1beta release
    • 19250700 1:CAS:528:DC%2BD1MXotFKisrg%3D
    • Eder C (2009) Mechanisms of interleukin-1beta release. Immunobiology 214:543-553
    • (2009) Immunobiology , vol.214 , pp. 543-553
    • Eder, C.1
  • 49
    • 70649107057 scopus 로고    scopus 로고
    • A conserved, lipid-mediated sorting mechanism of yeast Ist2 and mammalian STIM proteins to the peripheral ER
    • 19845919 1:CAS:528:DC%2BD1MXhsFajsbvN
    • Ercan E, Momburg F, Engel U, Temmerman K, Nickel W, Seedorf M (2009) A conserved, lipid-mediated sorting mechanism of yeast Ist2 and mammalian STIM proteins to the peripheral ER. Traffic 10:1802-1818
    • (2009) Traffic , vol.10 , pp. 1802-1818
    • Ercan, E.1    Momburg, F.2    Engel, U.3    Temmerman, K.4    Nickel, W.5    Seedorf, M.6
  • 50
    • 3242693560 scopus 로고    scopus 로고
    • Mini-review: The nuclear protein HMGB1 as a proinflammatory mediator
    • 15162419 1:CAS:528:DC%2BD2cXltFKrtbc%3D
    • Erlandsson Harris H, Andersson U (2004) Mini-review: the nuclear protein HMGB1 as a proinflammatory mediator. Eur J Immunol 34:1503-1512
    • (2004) Eur J Immunol , vol.34 , pp. 1503-1512
    • Erlandsson Harris, H.1    Andersson, U.2
  • 51
    • 0035918223 scopus 로고    scopus 로고
    • Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase i times the proteasomal degradation of unassembled immunoglobulin subunits
    • 11278527 1:CAS:528:DC%2BD3MXjtFynu7o%3D
    • Fagioli C, Sitia R (2001) Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase I times the proteasomal degradation of unassembled immunoglobulin subunits. J Biol Chem 276:12885-12892
    • (2001) J Biol Chem , vol.276 , pp. 12885-12892
    • Fagioli, C.1    Sitia, R.2
  • 52
    • 73249134381 scopus 로고    scopus 로고
    • A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus
    • 19933202 1:CAS:528:DC%2BC3cXovVWquw%3D%3D
    • Faso C, Chen YN, Tamura K, Held M, Zemelis S, Marti L, Saravanan R, Hummel E, Kung L, Miller E, Hawes C, Brandizzi F (2009) A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus. Plant Cell 21:3655-3671
    • (2009) Plant Cell , vol.21 , pp. 3655-3671
    • Faso, C.1    Chen, Y.N.2    Tamura, K.3    Held, M.4    Zemelis, S.5    Marti, L.6    Saravanan, R.7    Hummel, E.8    Kung, L.9    Miller, E.10    Hawes, C.11    Brandizzi, F.12
  • 53
    • 0036911086 scopus 로고    scopus 로고
    • Selective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p
    • 12475940 1:CAS:528:DC%2BD38XpsFOru74%3D
    • Fatal N, Suntio T, Makarow M (2002) Selective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p. Mol Biol Cell 13:4130-4140
    • (2002) Mol Biol Cell , vol.13 , pp. 4130-4140
    • Fatal, N.1    Suntio, T.2    Makarow, M.3
  • 54
    • 2342422041 scopus 로고    scopus 로고
    • Active and specific recruitment of a soluble cargo protein for endoplasmic reticulum exit in the absence of functional COPII component Sec24p
    • 15075228 1:CAS:528:DC%2BD2cXjvFCitLY%3D
    • Fatal N, Karhinen L, Jokitalo E, Makarow M (2004) Active and specific recruitment of a soluble cargo protein for endoplasmic reticulum exit in the absence of functional COPII component Sec24p. J Cell Sci 117:1665-1673
    • (2004) J Cell Sci , vol.117 , pp. 1665-1673
    • Fatal, N.1    Karhinen, L.2    Jokitalo, E.3    Makarow, M.4
  • 55
    • 51349095514 scopus 로고    scopus 로고
    • GRASP55 regulates Golgi ribbon formation
    • 18434598 1:CAS:528:DC%2BD1cXoslWitro%3D
    • Feinstein TN, Linstedt AD (2008) GRASP55 regulates Golgi ribbon formation. Mol Biol Cell 19:2696-2707
    • (2008) Mol Biol Cell , vol.19 , pp. 2696-2707
    • Feinstein, T.N.1    Linstedt, A.D.2
  • 57
    • 0037184006 scopus 로고    scopus 로고
    • Sulfation in the Golgi lumen of Madin-Darby canine kidney cells is inhibited by brefeldin A and depends on a factor present in the cytoplasm and on Golgi membranes
    • 12138122 1:CAS:528:DC%2BD38XnsVCjtrg%3D
    • Fjeldstad K, Pedersen ME, Vuong TT, Kolset SO, Nordstrand LM, Prydz K (2002) Sulfation in the Golgi lumen of Madin-Darby canine kidney cells is inhibited by brefeldin A and depends on a factor present in the cytoplasm and on Golgi membranes. J Biol Chem 277:36272-36279
    • (2002) J Biol Chem , vol.277 , pp. 36272-36279
    • Fjeldstad, K.1    Pedersen, M.E.2    Vuong, T.T.3    Kolset, S.O.4    Nordstrand, L.M.5    Prydz, K.6
  • 58
    • 0142070958 scopus 로고    scopus 로고
    • Regulated secretion of macrophage migration inhibitory factor is mediated by a non-classical pathway involving an ABC transporter
    • 12965208 1:CAS:528:DC%2BD3sXntVCjsLw%3D
    • Flieger O, Engling A, Bucala R, Lue H, Nickel W, Bernhagen J (2003) Regulated secretion of macrophage migration inhibitory factor is mediated by a non-classical pathway involving an ABC transporter. FEBS Lett 551:78-86
    • (2003) FEBS Lett , vol.551 , pp. 78-86
    • Flieger, O.1    Engling, A.2    Bucala, R.3    Lue, H.4    Nickel, W.5    Bernhagen, J.6
  • 59
    • 62149148157 scopus 로고    scopus 로고
    • A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KChIP1 and Kv4 potassium channels
    • 19138172 1:CAS:528:DC%2BD1MXitlWhuro%3D
    • Flowerdew SE, Burgoyne RD (2009) A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KChIP1 and Kv4 potassium channels. Biochem J 418:529-540
    • (2009) Biochem J , vol.418 , pp. 529-540
    • Flowerdew, S.E.1    Burgoyne, R.D.2
  • 60
    • 67649891328 scopus 로고    scopus 로고
    • Taking the scenic route: Biosynthetic traffic to the plasma membrane in polarized epithelial cells
    • 19453969 1:CAS:528:DC%2BD1MXovFegtr4%3D
    • Folsch H, Mattila PE, Weisz OA (2009) Taking the scenic route: biosynthetic traffic to the plasma membrane in polarized epithelial cells. Traffic 10:972-981
    • (2009) Traffic , vol.10 , pp. 972-981
    • Folsch, H.1    Mattila, P.E.2    Weisz, O.A.3
  • 61
    • 0028998505 scopus 로고
    • Recycling of a glycosylphosphatidylinositol-anchored heparan sulphate proteoglycan (glypican) in skin fibroblasts
    • 7579795 1:CAS:528:DyaK2MXntFKlsLg%3D
    • Fransson LA, Edgren G, Havsmark B, Schmidtchen A (1995) Recycling of a glycosylphosphatidylinositol-anchored heparan sulphate proteoglycan (glypican) in skin fibroblasts. Glycobiology 5:407-415
    • (1995) Glycobiology , vol.5 , pp. 407-415
    • Fransson, L.A.1    Edgren, G.2    Havsmark, B.3    Schmidtchen, A.4
  • 62
    • 79952802009 scopus 로고    scopus 로고
    • AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells
    • 21097504 1:CAS:528:DC%2BC3MXhtFKksLw%3D
    • Gangalum RK, Atanasov IC, Zhou ZH, Bhat SP (2011) AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells. J Biol Chem 286:3261-3269
    • (2011) J Biol Chem , vol.286 , pp. 3261-3269
    • Gangalum, R.K.1    Atanasov, I.C.2    Zhou, Z.H.3    Bhat, S.P.4
  • 63
    • 0036775236 scopus 로고    scopus 로고
    • The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway
    • 12231511 1:CAS:528:DC%2BD38Xpt1KgtL4%3D
    • Gardella S, Andrei C, Ferrera D, Lotti LV, Torrisi MR, Bianchi ME, Rubartelli A (2002) The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Rep 3:995-1001
    • (2002) EMBO Rep , vol.3 , pp. 995-1001
    • Gardella, S.1    Andrei, C.2    Ferrera, D.3    Lotti, L.V.4    Torrisi, M.R.5    Bianchi, M.E.6    Rubartelli, A.7
  • 64
    • 80052277733 scopus 로고    scopus 로고
    • Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway
    • 21884936 1:CAS:528:DC%2BC3MXhtFakur3N
    • Gee HY, Noh SH, Tang BL, Kim KH, Lee MG (2011) Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway. Cell 146:746-760
    • (2011) Cell , vol.146 , pp. 746-760
    • Gee, H.Y.1    Noh, S.H.2    Tang, B.L.3    Kim, K.H.4    Lee, M.G.5
  • 65
    • 39149111232 scopus 로고    scopus 로고
    • Message on the web: MRNA and ER co-trafficking
    • 18215524 1:CAS:528:DC%2BD1cXitVGhsbw%3D
    • Gerst JE (2008) Message on the web: mRNA and ER co-trafficking. Trends Cell Biol 18:68-76
    • (2008) Trends Cell Biol , vol.18 , pp. 68-76
    • Gerst, J.E.1
  • 66
    • 0032919043 scopus 로고    scopus 로고
    • Chicken erythroid AE1 anion exchangers associate with the cytoskeleton during recycling to the Golgi
    • 9950688 1:CAS:528:DyaK1MXitFGgtbc%3D
    • Ghosh S, Cox KH, Cox JV (1999) Chicken erythroid AE1 anion exchangers associate with the cytoskeleton during recycling to the Golgi. Mol Biol Cell 10:455-469
    • (1999) Mol Biol Cell , vol.10 , pp. 455-469
    • Ghosh, S.1    Cox, K.H.2    Cox, J.V.3
  • 67
    • 69949117622 scopus 로고    scopus 로고
    • Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity
    • 19684575 1:CAS:528:DC%2BD1MXhtVKrsbnJ
    • Gibbings DJ, Ciaudo C, Erhardt M, Voinnet O (2009) Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity. Nat Cell Biol 11:1143-1149
    • (2009) Nat Cell Biol , vol.11 , pp. 1143-1149
    • Gibbings, D.J.1    Ciaudo, C.2    Erhardt, M.3    Voinnet, O.4
  • 69
    • 79960745991 scopus 로고    scopus 로고
    • Unconventional secretion: A stress on GRASP
    • 21571519 1:CAS:528:DC%2BC3MXps1ejtbc%3D
    • Giuliani F, Grieve A, Rabouille C (2011) Unconventional secretion: a stress on GRASP. Curr Opin Cell Biol 23:498-504
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 498-504
    • Giuliani, F.1    Grieve, A.2    Rabouille, C.3
  • 70
    • 84862492324 scopus 로고    scopus 로고
    • Models for Golgi traffic: A critical assessment
    • Glick BS, Luini A (2011) Models for Golgi traffic: a critical assessment. Cold Spring Harb Perspect Biol 3(11):a005215
    • (2011) Spring Harb Perspect Biol , vol.3 , Issue.11 , pp. 005215
    • Glick, B.S.1    Luini, A.2
  • 72
    • 84863866336 scopus 로고    scopus 로고
    • Golgi bypass: Skirting around the heart of classical secretion
    • 4. pii
    • Grieve AG, Rabouille C (2011) Golgi bypass: skirting around the heart of classical secretion. Cold Spring Harb Perspect Biol 3(4. pii):a005298
    • (2011) Spring Harb Perspect Biol , vol.3 , pp. 005298
    • Grieve, A.G.1    Rabouille, C.2
  • 73
    • 0022975133 scopus 로고
    • The trans Golgi network: Sorting at the exit site of the Golgi complex
    • 2945253 1:CAS:528:DyaL2sXjtFyn
    • Griffiths G, Simons K (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234:438-443
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 74
    • 57149087260 scopus 로고    scopus 로고
    • Secretion of active membrane type 1 matrix metalloproteinase (MMP-14) into extracellular space in microvesicular exosomes
    • 18802920 1:CAS:528:DC%2BD1cXhsFWgt77L
    • Hakulinen J, Sankkila L, Sugiyama N, Lehti K, Keski-Oja J (2008) Secretion of active membrane type 1 matrix metalloproteinase (MMP-14) into extracellular space in microvesicular exosomes. J Cell Biochem 105:1211-1218
    • (2008) J Cell Biochem , vol.105 , pp. 1211-1218
    • Hakulinen, J.1    Sankkila, L.2    Sugiyama, N.3    Lehti, K.4    Keski-Oja, J.5
  • 75
    • 49749105225 scopus 로고    scopus 로고
    • Secretory outposts for the local processing of membrane cargo in neuronal dendrites
    • 18532987 1:CAS:528:DC%2BD1cXhtVyksb3P
    • Hanus C, Ehlers MD (2008) Secretory outposts for the local processing of membrane cargo in neuronal dendrites. Traffic 9:1437-1445
    • (2008) Traffic , vol.9 , pp. 1437-1445
    • Hanus, C.1    Ehlers, M.D.2
  • 76
    • 27744482336 scopus 로고    scopus 로고
    • Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway
    • 16260497 1:CAS:528:DC%2BD2MXht1ShsrbP
    • Hasdemir B, Fitzgerald DJ, Prior IA, Tepikin AV, Burgoyne RD (2005) Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway. J Cell Biol 171:459-469
    • (2005) J Cell Biol , vol.171 , pp. 459-469
    • Hasdemir, B.1    Fitzgerald, D.J.2    Prior, I.A.3    Tepikin, A.V.4    Burgoyne, R.D.5
  • 77
    • 0015950295 scopus 로고
    • The action mechanism of brefeldin A. I. Growth recovery of Candida albicans by lipids from the action of brefeldin A
    • 1:CAS:528:DyaE2cXhsVWntrY%3D
    • Hayashi T, Takatsuki A, Tamura G (1974) The action mechanism of brefeldin A. I. Growth recovery of Candida albicans by lipids from the action of brefeldin A. J Antibiot (Tokyo) 27:65-72
    • (1974) J Antibiot (Tokyo) , vol.27 , pp. 65-72
    • Hayashi, T.1    Takatsuki, A.2    Tamura, G.3
  • 78
    • 58149091543 scopus 로고    scopus 로고
    • Syndecan-1 ectodomain shedding is regulated by the small GTPase Rab5
    • 18957427 1:CAS:528:DC%2BD1cXhsVylsrrN
    • Hayashida K, Stahl PD, Park PW (2008) Syndecan-1 ectodomain shedding is regulated by the small GTPase Rab5. J Biol Chem 283:35435-35444
    • (2008) J Biol Chem , vol.283 , pp. 35435-35444
    • Hayashida, K.1    Stahl, P.D.2    Park, P.W.3
  • 79
    • 3142518032 scopus 로고    scopus 로고
    • Secretory protein trafficking in Giardia intestinalis
    • 15225300 1:CAS:528:DC%2BD2cXlvFensbo%3D
    • Hehl AB, Marti M (2004) Secretory protein trafficking in Giardia intestinalis. Mol Microbiol 53:19-28
    • (2004) Mol Microbiol , vol.53 , pp. 19-28
    • Hehl, A.B.1    Marti, M.2
  • 80
    • 9444272907 scopus 로고    scopus 로고
    • MRNA localization and ER-based protein sorting mechanisms dictate the use of tER-Golgi units involved in Gurken transport in Drosophila oocytes
    • 15385627 1:CAS:528:DC%2BD2cXhtVGlsLvK
    • Herpers B, Rabouille C (2004) mRNA localization and ER-based protein sorting mechanisms dictate the use of tER-Golgi units involved in Gurken transport in Drosophila oocytes. Mol Biol Cell 15:5306-5317
    • (2004) Mol Biol Cell , vol.15 , pp. 5306-5317
    • Herpers, B.1    Rabouille, C.2
  • 81
    • 70849088746 scopus 로고    scopus 로고
    • Subcellular mRNA localization in animal cells and why it matters
    • 19965463 1:CAS:528:DC%2BD1MXhsVKhur7E
    • Holt CE, Bullock SL (2009) Subcellular mRNA localization in animal cells and why it matters. Science 326:1212-1216
    • (2009) Science , vol.326 , pp. 1212-1216
    • Holt, C.E.1    Bullock, S.L.2
  • 82
    • 0037113095 scopus 로고    scopus 로고
    • Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC)
    • 12376558 1:CAS:528:DC%2BD38XpsVyjsro%3D
    • Horstmann H, Ng CP, Tang BL, Hong W (2002) Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC). J Cell Sci 115:4263-4273
    • (2002) J Cell Sci , vol.115 , pp. 4263-4273
    • Horstmann, H.1    Ng, C.P.2    Tang, B.L.3    Hong, W.4
  • 83
    • 84858336834 scopus 로고    scopus 로고
    • The formation, function and fate of protein storage compartments in seeds
    • Ibl V, Stoger E (2012) The formation, function and fate of protein storage compartments in seeds. Protoplasma 249(2):379-392
    • (2012) Protoplasma , vol.249 , Issue.2 , pp. 379-392
    • Ibi, V.1    Stoger, E.2
  • 84
    • 64849104544 scopus 로고    scopus 로고
    • Mechanisms of transport through the Golgi complex
    • 19193869 1:CAS:528:DC%2BD1MXjs1Wls70%3D
    • Jackson CL (2009) Mechanisms of transport through the Golgi complex. J Cell Sci 122:443-452
    • (2009) J Cell Sci , vol.122 , pp. 443-452
    • Jackson, C.L.1
  • 85
    • 77951885732 scopus 로고    scopus 로고
    • Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions
    • 20345754 1:CAS:528:DC%2BC3cXnt1Gnsbo%3D
    • Jang A, Lee HJ, Suk JE, Jung JW, Kim KP, Lee SJ (2010) Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions. J Neurochem 113:1263-1274
    • (2010) J Neurochem , vol.113 , pp. 1263-1274
    • Jang, A.1    Lee, H.J.2    Suk, J.E.3    Jung, J.W.4    Kim, K.P.5    Lee, S.J.6
  • 87
    • 0032537741 scopus 로고    scopus 로고
    • Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein
    • 9705930 1:CAS:528:DyaK1cXks1Ghtbc%3D
    • Joliot A, Maizel A, Rosenberg D, Trembleau A, Dupas S, Volovitch M, Prochiantz A (1998) Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein. Curr Biol 8:856-863
    • (1998) Curr Biol , vol.8 , pp. 856-863
    • Joliot, A.1    Maizel, A.2    Rosenberg, D.3    Trembleau, A.4    Dupas, S.5    Volovitch, M.6    Prochiantz, A.7
  • 88
    • 0027465514 scopus 로고
    • Expression of mutant ELH prohormones in AtT-20 cells: The relationship between prohormone processing and sorting
    • 8458863 1:CAS:528:DyaK3sXitlSmsL8%3D
    • Jung LJ, Kreiner T, Scheller RH (1993) Expression of mutant ELH prohormones in AtT-20 cells: the relationship between prohormone processing and sorting. J Cell Biol 121:11-21
    • (1993) J Cell Biol , vol.121 , pp. 11-21
    • Jung, L.J.1    Kreiner, T.2    Scheller, R.H.3
  • 89
    • 1842589369 scopus 로고    scopus 로고
    • A novel transport pathway for a yeast plasma membrane protein encoded by a localized mRNA
    • 15028216 1:CAS:528:DC%2BD2cXisVektr4%3D
    • Juschke C, Ferring D, Jansen RP, Seedorf M (2004) A novel transport pathway for a yeast plasma membrane protein encoded by a localized mRNA. Curr Biol 14:406-411
    • (2004) Curr Biol , vol.14 , pp. 406-411
    • Juschke, C.1    Ferring, D.2    Jansen, R.P.3    Seedorf, M.4
  • 90
    • 22044445588 scopus 로고    scopus 로고
    • SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane
    • 15911878
    • Juschke C, Wachter A, Schwappach B, Seedorf M (2005) SEC18/NSF- independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. J Cell Biol 169:613-622
    • (2005) J Cell Biol , vol.169 , pp. 613-622
    • Juschke, C.1    Wachter, A.2    Schwappach, B.3    Seedorf, M.4
  • 91
    • 73949133327 scopus 로고    scopus 로고
    • SPRED: A machine learning approach for the identification of classical and non-classical secretory proteins in mammalian genomes
    • 19995554 1:CAS:528:DC%2BC3cXot1yiug%3D%3D
    • Kandaswamy KK, Pugalenthi G, Hartmann E, Kalies KU, Moller S, Suganthan PN, Martinetz T (2010) SPRED: a machine learning approach for the identification of classical and non-classical secretory proteins in mammalian genomes. Biochem Biophys Res Commun 391:1306-1311
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1306-1311
    • Kandaswamy, K.K.1    Pugalenthi, G.2    Hartmann, E.3    Kalies, K.U.4    Moller, S.5    Suganthan, P.N.6    Martinetz, T.7
  • 92
    • 21044454345 scopus 로고    scopus 로고
    • Endoplasmic reticulum exit of a secretory glycoprotein in the absence of sec24p family proteins in yeast
    • 15941408 1:CAS:528:DC%2BD2MXlsFWhtrY%3D
    • Karhinen L, Bastos RN, Jokitalo E, Makarow M (2005) Endoplasmic reticulum exit of a secretory glycoprotein in the absence of sec24p family proteins in yeast. Traffic 6:562-574
    • (2005) Traffic , vol.6 , pp. 562-574
    • Karhinen, L.1    Bastos, R.N.2    Jokitalo, E.3    Makarow, M.4
  • 93
    • 33751199883 scopus 로고    scopus 로고
    • Exosomes: From biogenesis and secretion to biological function
    • 17067686 1:CAS:528:DC%2BD28Xht1eqsrjL
    • Keller S, Sanderson MP, Stoeck A, Altevogt P (2006) Exosomes: from biogenesis and secretion to biological function. Immunol Lett 107:102-108
    • (2006) Immunol Lett , vol.107 , pp. 102-108
    • Keller, S.1    Sanderson, M.P.2    Stoeck, A.3    Altevogt, P.4
  • 94
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • 18329368 1:CAS:528:DC%2BD1cXjs1ait74%3D
    • Keller M, Ruegg A, Werner S, Beer HD (2008) Active caspase-1 is a regulator of unconventional protein secretion. Cell 132:818-831
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 95
    • 34547604776 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP is required for unconventional protein secretion during development
    • 17655921 1:CAS:528:DC%2BD2sXptlynuro%3D
    • Kinseth MA, Anjard C, Fuller D, Guizzunti G, Loomis WF, Malhotra V (2007) The Golgi-associated protein GRASP is required for unconventional protein secretion during development. Cell 130:524-534
    • (2007) Cell , vol.130 , pp. 524-534
    • Kinseth, M.A.1    Anjard, C.2    Fuller, D.3    Guizzunti, G.4    Loomis, W.F.5    Malhotra, V.6
  • 96
    • 0033938963 scopus 로고    scopus 로고
    • Transport between ER and Golgi
    • 10873822 1:CAS:528:DC%2BD3cXlt1Srtbc%3D
    • Klumperman J (2000) Transport between ER and Golgi. Curr Opin Cell Biol 12:445-449
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 445-449
    • Klumperman, J.1
  • 97
    • 70450223327 scopus 로고    scopus 로고
    • The Golgi apparatus: Lessons from Drosophila
    • 19800333 1:CAS:528:DC%2BD1MXhsFShtL7O
    • Kondylis V, Rabouille C (2009) The Golgi apparatus: lessons from Drosophila. FEBS Lett 583:3827-3838
    • (2009) FEBS Lett , vol.583 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 98
    • 79952034405 scopus 로고    scopus 로고
    • Identification of ER proteins involved in the functional organisation of the early secretory pathway in Drosophila cells by a targeted RNAi screen
    • 21383842 1:CAS:528:DC%2BC3MXivFGgs70%3D
    • Kondylis V, Tang Y, Fuchs F, Boutros M, Rabouille C (2011) Identification of ER proteins involved in the functional organisation of the early secretory pathway in Drosophila cells by a targeted RNAi screen. PLoS One 6:e17173
    • (2011) PLoS One , vol.6 , pp. 17173
    • Kondylis, V.1    Tang, Y.2    Fuchs, F.3    Boutros, M.4    Rabouille, C.5
  • 99
    • 79960376333 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in alpha-synuclein and UCH-L1 inhibit the unconventional secretion of UCH-L1
    • 21693148 1:CAS:528:DC%2BC3MXptVOmt7g%3D
    • Konya C, Hatanaka Y, Fujiwara Y, Uchida K, Nagai Y, Wada K, Kabuta T (2011) Parkinson's disease-associated mutations in alpha-synuclein and UCH-L1 inhibit the unconventional secretion of UCH-L1. Neurochem Int 59:251-258
    • (2011) Neurochem Int , vol.59 , pp. 251-258
    • Konya, C.1    Hatanaka, Y.2    Fujiwara, Y.3    Uchida, K.4    Nagai, Y.5    Wada, K.6    Kabuta, T.7
  • 100
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • 3896128 1:STN:280:DyaL2M3nvVSjsA%3D%3D
    • Kornfeld R, Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631-664
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 101
    • 0025919701 scopus 로고
    • PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A
    • 1710224 1:CAS:528:DyaK3MXisVGitr4%3D
    • Ktistakis NT, Roth MG, Bloom GS (1991) PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A. J Cell Biol 113:1009-1023
    • (1991) J Cell Biol , vol.113 , pp. 1009-1023
    • Ktistakis, N.T.1    Roth, M.G.2    Bloom, G.S.3
  • 102
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the normal rat kidney cell
    • 10087259 1:CAS:528:DyaK1MXitVKjtLk%3D
    • Ladinsky MS, Mastronarde DN, McIntosh JR, Howell KE, Staehelin LA (1999) Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J Cell Biol 144:1135-1149
    • (1999) J Cell Biol , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 103
    • 0021676811 scopus 로고
    • Lysosomal enzyme phosphorylation. Recognition of a protein-dependent determinant allows specific phosphorylation of oligosaccharides present on lysosomal enzymes
    • 6094568 1:STN:280:DyaL2M%2FlsV2msg%3D%3D
    • Lang L, Reitman M, Tang J, Roberts RM, Kornfeld S (1984) Lysosomal enzyme phosphorylation. Recognition of a protein-dependent determinant allows specific phosphorylation of oligosaccharides present on lysosomal enzymes. J Biol Chem 259:14663-14671
    • (1984) J Biol Chem , vol.259 , pp. 14663-14671
    • Lang, L.1    Reitman, M.2    Tang, J.3    Roberts, R.M.4    Kornfeld, S.5
  • 104
    • 77951084351 scopus 로고    scopus 로고
    • Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes
    • 20351264 1:CAS:528:DC%2BC3cXltVKkt7k%3D
    • Lavieu G, Orci L, Shi L, Geiling M, Ravazzola M, Wieland F, Cosson P, Rothman JE (2010) Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes. Proc Natl Acad Sci U S A 107:6876-6881
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 6876-6881
    • Lavieu, G.1    Orci, L.2    Shi, L.3    Geiling, M.4    Ravazzola, M.5    Wieland, F.6    Cosson, P.7    Rothman, J.E.8
  • 105
    • 0033880710 scopus 로고    scopus 로고
    • Different properties of two isoforms of annexin XIII in MDCK cells
    • 10862718 1:CAS:528:DC%2BD3cXlslyktLo%3D
    • Lecat S, Verkade P, Thiele C, Fiedler K, Simons K, Lafont F (2000) Different properties of two isoforms of annexin XIII in MDCK cells. J Cell Sci 113:2607-2618
    • (2000) J Cell Sci , vol.113 , pp. 2607-2618
    • Lecat, S.1    Verkade, P.2    Thiele, C.3    Fiedler, K.4    Simons, K.5    Lafont, F.6
  • 107
    • 22044433038 scopus 로고    scopus 로고
    • Endoplasmic reticulum: One continuous network compartmentalized by extrinsic cues
    • 15975783 1:CAS:528:DC%2BD2MXmt1Srur4%3D
    • Levine T, Rabouille C (2005) Endoplasmic reticulum: one continuous network compartmentalized by extrinsic cues. Curr Opin Cell Biol 17:362-368
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 362-368
    • Levine, T.1    Rabouille, C.2
  • 108
    • 0027212532 scopus 로고
    • Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells. Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway
    • 8505302 1:CAS:528:DyaK3sXks1yktbc%3D
    • Lindstedt R, Apodaca G, Barondes SH, Mostov KE, Leffler H (1993) Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells. Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway. J Biol Chem 268:11750-11757
    • (1993) J Biol Chem , vol.268 , pp. 11750-11757
    • Lindstedt, R.1    Apodaca, G.2    Barondes, S.H.3    Mostov, K.E.4    Leffler, H.5
  • 109
    • 0026079731 scopus 로고
    • Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells
    • 1917917 1:CAS:528:DyaK3MXltlakt7w%3D
    • Low SH, Wong SH, Tang BL, Tan P, Subramaniam VN, Hong W (1991) Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells. J Biol Chem 266:17729-17732
    • (1991) J Biol Chem , vol.266 , pp. 17729-17732
    • Low, S.H.1    Wong, S.H.2    Tang, B.L.3    Tan, P.4    Subramaniam, V.N.5    Hong, W.6
  • 110
    • 0026703819 scopus 로고
    • Selective inhibition of protein targeting to the apical domain of MDCK cells by brefeldin A
    • 1352300 1:CAS:528:DyaK38Xks1Ont7c%3D
    • Low SH, Tang BL, Wong SH, Hong W (1992) Selective inhibition of protein targeting to the apical domain of MDCK cells by brefeldin A. J Cell Biol 118:51-62
    • (1992) J Cell Biol , vol.118 , pp. 51-62
    • Low, S.H.1    Tang, B.L.2    Wong, S.H.3    Hong, W.4
  • 111
    • 79951558394 scopus 로고    scopus 로고
    • Structural organization of the Golgi apparatus
    • 21071196 1:CAS:528:DC%2BC3MXit12ju7o%3D
    • Lowe M (2011) Structural organization of the Golgi apparatus. Curr Opin Cell Biol 23:85-93
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 85-93
    • Lowe, M.1
  • 112
    • 0032516893 scopus 로고    scopus 로고
    • Regulation of membrane traffic in animal cells by COPI
    • 9714733 1:CAS:528:DyaK1cXltFWksbk%3D
    • Lowe M, Kreis TE (1998) Regulation of membrane traffic in animal cells by COPI. Biochim Biophys Acta 1404:53-66
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 53-66
    • Lowe, M.1    Kreis, T.E.2
  • 113
    • 79960761117 scopus 로고    scopus 로고
    • Aldo-keto reductase family 1, member B10 is secreted through a lysosome-mediated non-classical pathway
    • 21585341 1:CAS:528:DC%2BC3MXpsVajsLs%3D
    • Luo DX, Huang MC, Ma J, Gao Z, Liao DF, Cao D (2011) Aldo-keto reductase family 1, member B10 is secreted through a lysosome-mediated non-classical pathway. Biochem J 438:71-80
    • (2011) Biochem J , vol.438 , pp. 71-80
    • Luo, D.X.1    Huang, M.C.2    Ma, J.3    Gao, Z.4    Liao, D.F.5    Cao, D.6
  • 115
    • 80052226774 scopus 로고    scopus 로고
    • Protein export at the ER: Loading big collagens into COPII carriers
    • 21878990 1:CAS:528:DC%2BC3MXhtFSltb3E
    • Malhotra V, Erlmann P (2011) Protein export at the ER: loading big collagens into COPII carriers. EMBO J 30:3475-3480
    • (2011) EMBO J , vol.30 , pp. 3475-3480
    • Malhotra, V.1    Erlmann, P.2
  • 116
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • 17114456 1:CAS:528:DC%2BD28Xht1WrsL3J
    • Mambula SS, Calderwood SK (2006) Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J Immunol 177:7849-7857
    • (2006) J Immunol , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 117
    • 77149152566 scopus 로고    scopus 로고
    • Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
    • 20156962 1:CAS:528:DC%2BC3cXislWgsrg%3D
    • Manjithaya R, Anjard C, Loomis WF, Subramani S (2010) Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation. J Cell Biol 188:537-546
    • (2010) J Cell Biol , vol.188 , pp. 537-546
    • Manjithaya, R.1    Anjard, C.2    Loomis, W.F.3    Subramani, S.4
  • 118
    • 52549093192 scopus 로고    scopus 로고
    • Take the 'A' train: On fast tracks to the cell surface
    • 18726174 1:CAS:528:DC%2BD1cXhtFCqsr3N
    • Marie M, Sannerud R, Avsnes Dale H, Saraste J (2008) Take the 'A' train: on fast tracks to the cell surface. Cell Mol Life Sci 65:2859-2874
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2859-2874
    • Marie, M.1    Sannerud, R.2    Avsnes Dale, H.3    Saraste, J.4
  • 119
    • 70350120449 scopus 로고    scopus 로고
    • The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome
    • 19710425 1:CAS:528:DC%2BD1MXhsVSksL3O
    • Marie M, Dale HA, Sannerud R, Saraste J (2009) The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome. Mol Biol Cell 20:4458-4470
    • (2009) Mol Biol Cell , vol.20 , pp. 4458-4470
    • Marie, M.1    Dale, H.A.2    Sannerud, R.3    Saraste, J.4
  • 120
    • 60149086205 scopus 로고    scopus 로고
    • MRNA localization: Gene expression in the spatial dimension
    • 19239891 1:CAS:528:DC%2BD1MXkvFGksbY%3D
    • Martin KC, Ephrussi A (2009) mRNA localization: gene expression in the spatial dimension. Cell 136:719-730
    • (2009) Cell , vol.136 , pp. 719-730
    • Martin, K.C.1    Ephrussi, A.2
  • 121
    • 0035188530 scopus 로고    scopus 로고
    • Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels
    • 11719551 1:CAS:528:DC%2BD3MXosl2rtbY%3D
    • Martin PE, Blundell G, Ahmad S, Errington RJ, Evans WH (2001) Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels. J Cell Sci 114:3845-3855
    • (2001) J Cell Sci , vol.114 , pp. 3845-3855
    • Martin, P.E.1    Blundell, G.2    Ahmad, S.3    Errington, R.J.4    Evans, W.H.5
  • 122
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • 10412983 1:CAS:528:DyaK1MXks1Kktrw%3D
    • Martinez-Menarguez JA, Geuze HJ, Slot JW, Klumperman J (1999) Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98:81-90
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 124
    • 61849129278 scopus 로고    scopus 로고
    • Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells
    • 19029439 1:CAS:528:DC%2BD1MXisV2hsrw%3D
    • Maxson JE, Enns CA, Zhang AS (2009) Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells. Blood 113:1786-1793
    • (2009) Blood , vol.113 , pp. 1786-1793
    • Maxson, J.E.1    Enns, C.A.2    Zhang, A.S.3
  • 125
    • 77953481684 scopus 로고    scopus 로고
    • Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: A role for plasminogen activation
    • 20553606
    • McCready J, Sims JD, Chan D, Jay DG (2010) Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation. BMC Cancer 10:294
    • (2010) BMC Cancer , vol.10 , pp. 294
    • McCready, J.1    Sims, J.D.2    Chan, D.3    Jay, D.G.4
  • 126
    • 33744947804 scopus 로고    scopus 로고
    • Fas-ligand is stored in secretory lysosomes of ocular barrier epithelia and released with microvesicles
    • 16563377 1:CAS:528:DC%2BD28Xls1Gqsbc%3D
    • McKechnie NM, King BC, Fletcher E, Braun G (2006) Fas-ligand is stored in secretory lysosomes of ocular barrier epithelia and released with microvesicles. Exp Eye Res 83:304-314
    • (2006) Exp Eye Res , vol.83 , pp. 304-314
    • McKechnie, N.M.1    King, B.C.2    Fletcher, E.3    Braun, G.4
  • 128
    • 0028575371 scopus 로고
    • Analysis of transport and targeting of syndecan-1: Effect of cytoplasmic tail deletions
    • 7696713 1:CAS:528:DyaK2MXivVygsLo%3D
    • Miettinen HM, Edwards SN, Jalkanen M (1994) Analysis of transport and targeting of syndecan-1: effect of cytoplasmic tail deletions. Mol Biol Cell 5:1325-1339
    • (1994) Mol Biol Cell , vol.5 , pp. 1325-1339
    • Miettinen, H.M.1    Edwards, S.N.2    Jalkanen, M.3
  • 129
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • 12941277 1:CAS:528:DC%2BD3sXmvFahtbc%3D
    • Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, Orci L, Schekman R (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114:497-509
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 131
    • 0037403872 scopus 로고    scopus 로고
    • The architecture of microtubular network and Golgi orientation in osteoclasts-major differences between avian and mammalian species
    • 12706117 1:CAS:528:DC%2BD3sXivFektLo%3D
    • Mulari MT, Patrikainen L, Kaisto T, Metsikko K, Salo JJ, Vaananen HK (2003) The architecture of microtubular network and Golgi orientation in osteoclasts-major differences between avian and mammalian species. Exp Cell Res 285:221-235
    • (2003) Exp Cell Res , vol.285 , pp. 221-235
    • Mulari, M.T.1    Patrikainen, L.2    Kaisto, T.3    Metsikko, K.4    Salo, J.J.5    Vaananen, H.K.6
  • 132
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • 11207371 1:CAS:528:DC%2BD3MXis1Klsro%3D
    • Muniz M, Morsomme P, Riezman H (2001) Protein sorting upon exit from the endoplasmic reticulum. Cell 104:313-320
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 134
    • 77957700450 scopus 로고    scopus 로고
    • Mobile ER-to-Golgi but not post-Golgi membrane transport carriers disappear during the terminal myogenic differentiation
    • 20848131
    • Nevalainen M, Kaisto T, Metsikko K (2010) Mobile ER-to-Golgi but not post-Golgi membrane transport carriers disappear during the terminal myogenic differentiation. Cell Tissue Res 342:107-116
    • (2010) Cell Tissue Res , vol.342 , pp. 107-116
    • Nevalainen, M.1    Kaisto, T.2    Metsikko, K.3
  • 135
    • 79951537603 scopus 로고    scopus 로고
    • Beyond the endoplasmic reticulum: Atypical GRP78 in cell viability, signalling and therapeutic targeting
    • 21309747 1:CAS:528:DC%2BC3MXhvVCns7Y%3D
    • Ni M, Zhang Y, Lee AS (2011) Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting. Biochem J 434:181-188
    • (2011) Biochem J , vol.434 , pp. 181-188
    • Ni, M.1    Zhang, Y.2    Lee, A.S.3
  • 136
    • 21844468743 scopus 로고    scopus 로고
    • Unconventional secretory routes: Direct protein export across the plasma membrane of mammalian cells
    • 15998317 1:CAS:528:DC%2BD2MXmsVeitbY%3D
    • Nickel W (2005) Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells. Traffic 6:607-614
    • (2005) Traffic , vol.6 , pp. 607-614
    • Nickel, W.1
  • 137
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • 19122676 1:CAS:528:DC%2BD1MXhtVyisg%3D%3D
    • Nickel W, Rabouille C (2009) Mechanisms of regulated unconventional protein secretion. Nat Rev Mol Cell Biol 10:148-155
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 138
    • 55849145075 scopus 로고    scopus 로고
    • Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells
    • 18590485 1:CAS:528:DC%2BD1cXhtlOgtbbJ
    • Nickel W, Seedorf M (2008) Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu Rev Cell Dev Biol 24:287-308
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 287-308
    • Nickel, W.1    Seedorf, M.2
  • 139
    • 0028939322 scopus 로고
    • Ceramide reverses brefeldin A (BFA) resistance in BFA-resistant cell lines
    • 7876158 1:CAS:528:DyaK2MXjvVyrtbs%3D
    • Oda T, Chen CH, Wu HC (1995) Ceramide reverses brefeldin A (BFA) resistance in BFA-resistant cell lines. J Biol Chem 270:4088-4092
    • (1995) J Biol Chem , vol.270 , pp. 4088-4092
    • Oda, T.1    Chen, C.H.2    Wu, H.C.3
  • 140
    • 10344260159 scopus 로고    scopus 로고
    • Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles
    • 15516922 1:CAS:528:DC%2BD2cXhtVarsL%2FE
    • Otte S, Barlowe C (2004) Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles. Nat Cell Biol 6:1189-1194
    • (2004) Nat Cell Biol , vol.6 , pp. 1189-1194
    • Otte, S.1    Barlowe, C.2
  • 141
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • 17812524 1:STN:280:DC%2BC3cvktVaqug%3D%3D
    • Palade G (1975) Intracellular aspects of the process of protein synthesis. Science 189:867
    • (1975) Science , vol.189 , pp. 867
    • Palade, G.1
  • 142
    • 44849128559 scopus 로고    scopus 로고
    • Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system
    • 18555781 1:CAS:528:DC%2BD1cXnsF2gtbY%3D
    • Patterson GH, Hirschberg K, Polishchuk RS, Gerlich D, Phair RD, Lippincott-Schwartz J (2008) Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system. Cell 133:1055-1067
    • (2008) Cell , vol.133 , pp. 1055-1067
    • Patterson, G.H.1    Hirschberg, K.2    Polishchuk, R.S.3    Gerlich, D.4    Phair, R.D.5    Lippincott-Schwartz, J.6
  • 144
    • 0032549069 scopus 로고    scopus 로고
    • Blockade of the classical pathway of protein secretion does not affect the cellular exportation of lipocortin 1
    • 9533818 1:CAS:528:DyaK1cXhtVWksbg%3D
    • Philip JG, Flower RJ, Buckingham JC (1998) Blockade of the classical pathway of protein secretion does not affect the cellular exportation of lipocortin 1. Regul Pept 73:133-139
    • (1998) Regul Pept , vol.73 , pp. 133-139
    • Philip, J.G.1    Flower, R.J.2    Buckingham, J.C.3
  • 145
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • 15326289 1:CAS:528:DC%2BD2cXnvFemsLo%3D
    • Pisitkun T, Shen RF, Knepper MA (2004) Identification and proteomic profiling of exosomes in human urine. Proc Natl Acad Sci U S A 101:13368-13373
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 146
  • 148
    • 0034618102 scopus 로고    scopus 로고
    • Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae
    • 10931860 1:CAS:528:DC%2BD3cXlsFygsLc%3D
    • Prinz WA, Grzyb L, Veenhuis M, Kahana JA, Silver PA, Rapoport TA (2000) Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J Cell Biol 150:461-474
    • (2000) J Cell Biol , vol.150 , pp. 461-474
    • Prinz, W.A.1    Grzyb, L.2    Veenhuis, M.3    Kahana, J.A.4    Silver, P.A.5    Rapoport, T.A.6
  • 150
    • 0033975514 scopus 로고    scopus 로고
    • Synthesis and sorting of proteoglycans
    • 10633071 1:CAS:528:DC%2BD3cXht1ynt7k%3D
    • Prydz K, Dalen KT (2000) Synthesis and sorting of proteoglycans. J Cell Sci 113(Pt 2):193-205
    • (2000) J Cell Sci , vol.113 , Issue.PART 2 , pp. 193-205
    • Prydz, K.1    Dalen, K.T.2
  • 151
    • 0026779146 scopus 로고
    • Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells
    • 1400572 1:CAS:528:DyaK38XlvV2ju7g%3D
    • Prydz K, Hansen SH, Sandvig K, van Deurs B (1992) Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells. J Cell Biol 119:259-272
    • (1992) J Cell Biol , vol.119 , pp. 259-272
    • Prydz, K.1    Hansen, S.H.2    Sandvig, K.3    Van Deurs, B.4
  • 152
    • 38849131487 scopus 로고    scopus 로고
    • How many ways through the Golgi maze?
    • 18088319 1:CAS:528:DC%2BD1cXisVaktbk%3D
    • Prydz K, Dick G, Tveit H (2008) How many ways through the Golgi maze? Traffic 9:299-304
    • (2008) Traffic , vol.9 , pp. 299-304
    • Prydz, K.1    Dick, G.2    Tveit, H.3
  • 153
    • 33644756640 scopus 로고    scopus 로고
    • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution
    • 16489344 1:CAS:528:DC%2BD28XhvVKhtL4%3D
    • Puthenveedu MA, Bachert C, Puri S, Lanni F, Linstedt AD (2006) GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat Cell Biol 8:238-248
    • (2006) Nat Cell Biol , vol.8 , pp. 238-248
    • Puthenveedu, M.A.1    Bachert, C.2    Puri, S.3    Lanni, F.4    Linstedt, A.D.5
  • 154
    • 67349108796 scopus 로고    scopus 로고
    • P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways
    • 19189228 1:CAS:528:DC%2BD1MXmtlOrur0%3D
    • Qu Y, Dubyak GR (2009) P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways. Purinergic Signal 5:163-173
    • (2009) Purinergic Signal , vol.5 , pp. 163-173
    • Qu, Y.1    Dubyak, G.R.2
  • 155
    • 67349209224 scopus 로고    scopus 로고
    • The role of the cytoskeleton in the formation of gap junctions by Connexin 30
    • 19285977 1:CAS:528:DC%2BD1MXlslWit7o%3D
    • Qu C, Gardner P, Schrijver I (2009) The role of the cytoskeleton in the formation of gap junctions by Connexin 30. Exp Cell Res 315:1683-1692
    • (2009) Exp Cell Res , vol.315 , pp. 1683-1692
    • Qu, C.1    Gardner, P.2    Schrijver, I.3
  • 157
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • 19325624 1:CAS:528:DC%2BD1MXjs1Klurs%3D
    • Raiborg C, Stenmark H (2009) The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458:445-452
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 158
    • 79953161238 scopus 로고    scopus 로고
    • The endoplasmic reticulum and protein trafficking in dendrites and axons
    • 21215635 1:CAS:528:DC%2BC3MXkt1Gnt74%3D
    • Ramirez OA, Couve A (2011) The endoplasmic reticulum and protein trafficking in dendrites and axons. Trends Cell Biol 21:219-227
    • (2011) Trends Cell Biol , vol.21 , pp. 219-227
    • Ramirez, O.A.1    Couve, A.2
  • 159
    • 77953934642 scopus 로고    scopus 로고
    • HIV-1 Tat is unconventionally secreted through the plasma membrane
    • 19995346 1:CAS:528:DC%2BC3cXjtlahsL4%3D
    • Rayne F, Debaisieux S, Bonhoure A, Beaumelle B (2010) HIV-1 Tat is unconventionally secreted through the plasma membrane. Cell Biol Int 34:409-413
    • (2010) Cell Biol Int , vol.34 , pp. 409-413
    • Rayne, F.1    Debaisieux, S.2    Bonhoure, A.3    Beaumelle, B.4
  • 160
    • 38149097035 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator trafficking is mediated by the COPI coat in epithelial cells
    • 17932045 1:CAS:528:DC%2BD1cXhsFeitw%3D%3D
    • Rennolds J, Tower C, Musgrove L, Fan L, Maloney K, Clancy JP, Kirk KL, Sztul E, Cormet-Boyaka E (2008) Cystic fibrosis transmembrane conductance regulator trafficking is mediated by the COPI coat in epithelial cells. J Biol Chem 283:833-839
    • (2008) J Biol Chem , vol.283 , pp. 833-839
    • Rennolds, J.1    Tower, C.2    Musgrove, L.3    Fan, L.4    Maloney, K.5    Clancy, J.P.6    Kirk, K.L.7    Sztul, E.8    Cormet-Boyaka, E.9
  • 162
    • 0032145308 scopus 로고    scopus 로고
    • Secretion of plasminogen activator inhibitor 2 by human peripheral blood monocytes occurs via an endoplasmic reticulum-Golgi-independent pathway
    • 9683531 1:CAS:528:DyaK1cXltFGmu7s%3D
    • Ritchie H, Booth NA (1998) Secretion of plasminogen activator inhibitor 2 by human peripheral blood monocytes occurs via an endoplasmic reticulum-Golgi-independent pathway. Exp Cell Res 242:439-450
    • (1998) Exp Cell Res , vol.242 , pp. 439-450
    • Ritchie, H.1    Booth, N.A.2
  • 163
    • 20544431747 scopus 로고    scopus 로고
    • Protein sorting in the Golgi complex: Shifting paradigms
    • 15927284 1:CAS:528:DC%2BD2MXlsVCjurg%3D
    • Rodriguez-Boulan E, Musch A (2005) Protein sorting in the Golgi complex: shifting paradigms. Biochim Biophys Acta 1744:455-464
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 455-464
    • Rodriguez-Boulan, E.1    Musch, A.2
  • 164
    • 42049097236 scopus 로고    scopus 로고
    • Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum
    • 18391072 1:CAS:528:DC%2BD1cXks1Gku74%3D
    • Ronchi P, Colombo S, Francolini M, Borgese N (2008) Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum. J Cell Biol 181:105-118
    • (2008) J Cell Biol , vol.181 , pp. 105-118
    • Ronchi, P.1    Colombo, S.2    Francolini, M.3    Borgese, N.4
  • 166
    • 78951472912 scopus 로고    scopus 로고
    • The proprotein convertase PC7: Unique zymogen activation and trafficking pathways
    • 21075846 1:CAS:528:DC%2BC3MXosVamug%3D%3D
    • Rousselet E, Benjannet S, Hamelin J, Canuel M, Seidah NG (2011) The proprotein convertase PC7: unique zymogen activation and trafficking pathways. J Biol Chem 286:2728-2738
    • (2011) J Biol Chem , vol.286 , pp. 2728-2738
    • Rousselet, E.1    Benjannet, S.2    Hamelin, J.3    Canuel, M.4    Seidah, N.G.5
  • 167
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
    • 2328723 1:CAS:528:DyaK3cXkt1Wqtbo%3D
    • Rubartelli A, Cozzolino F, Talio M, Sitia R (1990) A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. EMBO J 9:1503-1510
    • (1990) EMBO J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 168
    • 0026353711 scopus 로고
    • Ricin transport in brefeldin A-treated cells: Correlation between Golgi structure and toxic effect
    • 1955466 1:CAS:528:DyaK3MXmsFSjsb8%3D
    • Sandvig K, Prydz K, Hansen SH, van Deurs B (1991) Ricin transport in brefeldin A-treated cells: correlation between Golgi structure and toxic effect. J Cell Biol 115:971-981
    • (1991) J Cell Biol , vol.115 , pp. 971-981
    • Sandvig, K.1    Prydz, K.2    Hansen, S.H.3    Van Deurs, B.4
  • 169
    • 0026684124 scopus 로고
    • Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
    • 1641040 1:CAS:528:DyaK38Xls1Glur0%3D
    • Sandvig K, Garred O, Prydz K, Kozlov JV, Hansen SH, van Deurs B (1992) Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature 358:510-512
    • (1992) Nature , vol.358 , pp. 510-512
    • Sandvig, K.1    Garred, O.2    Prydz, K.3    Kozlov, J.V.4    Hansen, S.H.5    Van Deurs, B.6
  • 170
    • 33745421381 scopus 로고    scopus 로고
    • Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery
    • 16421253 1:CAS:528:DC%2BD28XltlSqu74%3D
    • Sannerud R, Marie M, Nizak C, Dale HA, Pernet-Gallay K, Perez F, Goud B, Saraste J (2006) Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery. Mol Biol Cell 17:1514-1526
    • (2006) Mol Biol Cell , vol.17 , pp. 1514-1526
    • Sannerud, R.1    Marie, M.2    Nizak, C.3    Dale, H.A.4    Pernet-Gallay, K.5    Perez, F.6    Goud, B.7    Saraste, J.8
  • 171
    • 84866558510 scopus 로고    scopus 로고
    • Nitric oxide regulates non-classical secretion of tissue transglutaminase
    • 22046470 1:CAS:528:DC%2BC3MXhtlWjs7nN
    • Santhanam L, Berkowitz DE, Belkin AM (2011) Nitric oxide regulates non-classical secretion of tissue transglutaminase. Commun Integr Biol 4:584-586
    • (2011) Commun Integr Biol , vol.4 , pp. 584-586
    • Santhanam, L.1    Berkowitz, D.E.2    Belkin, A.M.3
  • 172
    • 34247282758 scopus 로고    scopus 로고
    • Functional symmetry of endomembranes
    • 17267686 1:CAS:528:DC%2BD2sXktVSmtb0%3D
    • Saraste J, Goud B (2007) Functional symmetry of endomembranes. Mol Biol Cell 18:1430-1436
    • (2007) Mol Biol Cell , vol.18 , pp. 1430-1436
    • Saraste, J.1    Goud, B.2
  • 173
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulm and the Golgi complex
    • 1457777 1:STN:280:DyaK3s%2FptFWquw%3D%3D
    • Saraste J, Kuismanen E (1992) Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulm and the Golgi complex. Semin Cell Biol 3:343-355
    • (1992) Semin Cell Biol , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 174
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • 1808196 1:CAS:528:DyaK38Xjs1ektg%3D%3D
    • Saraste J, Svensson K (1991) Distribution of the intermediate elements operating in ER to Golgi transport. J Cell Sci 100:415-430
    • (1991) J Cell Sci , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 175
    • 70450221903 scopus 로고    scopus 로고
    • Emerging new roles of the pre-Golgi intermediate compartment in biosynthetic-secretory trafficking
    • 19887068 1:CAS:528:DC%2BD1MXhsFSht7fF
    • Saraste J, Dale HA, Bazzocco S, Marie M (2009) Emerging new roles of the pre-Golgi intermediate compartment in biosynthetic-secretory trafficking. FEBS Lett 583:3804-3810
    • (2009) FEBS Lett , vol.583 , pp. 3804-3810
    • Saraste, J.1    Dale, H.A.2    Bazzocco, S.3    Marie, M.4
  • 176
    • 14944360626 scopus 로고    scopus 로고
    • COPII coat assembly and selective export from the endoplasmic reticulum
    • 15671485 1:CAS:528:DC%2BD2MXisleht7s%3D
    • Sato K (2004) COPII coat assembly and selective export from the endoplasmic reticulum. J Biochem 136:755-760
    • (2004) J Biochem , vol.136 , pp. 755-760
    • Sato, K.1
  • 177
    • 0037096162 scopus 로고    scopus 로고
    • The exosome pathway in K562 cells is regulated by Rab11
    • 12045221 1:CAS:528:DC%2BD38XlsVCqur4%3D
    • Savina A, Vidal M, Colombo MI (2002) The exosome pathway in K562 cells is regulated by Rab11. J Cell Sci 115:2505-2515
    • (2002) J Cell Sci , vol.115 , pp. 2505-2515
    • Savina, A.1    Vidal, M.2    Colombo, M.I.3
  • 178
    • 79960104144 scopus 로고    scopus 로고
    • MicroRNAs in development and disease
    • 21742789 1:CAS:528:DC%2BC3MXhtFyjur%2FK
    • Sayed D, Abdellatif M (2011) MicroRNAs in development and disease. Physiol Rev 91:827-887
    • (2011) Physiol Rev , vol.91 , pp. 827-887
    • Sayed, D.1    Abdellatif, M.2
  • 179
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • 9323141 1:CAS:528:DyaK2sXmtlOlsbo%3D
    • Scales SJ, Pepperkok R, Kreis TE (1997) Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90:1137-1148
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 180
    • 85027957912 scopus 로고    scopus 로고
    • Microvesicles are messengers
    • 21590325
    • Schifferli JA (2011) Microvesicles are messengers. Semin Immunopathol 33:393-394
    • (2011) Semin Immunopathol , vol.33 , pp. 393-394
    • Schifferli, J.A.1
  • 181
    • 33746546711 scopus 로고    scopus 로고
    • Coordination of endoplasmic reticulum and mRNA localization to the yeast bud
    • 16890529 1:CAS:528:DC%2BD28XotFWlsLc%3D
    • Schmid M, Jaedicke A, Du TG, Jansen RP (2006) Coordination of endoplasmic reticulum and mRNA localization to the yeast bud. Curr Biol 16:1538-1543
    • (2006) Curr Biol , vol.16 , pp. 1538-1543
    • Schmid, M.1    Jaedicke, A.2    Du, T.G.3    Jansen, R.P.4
  • 182
    • 38849095347 scopus 로고    scopus 로고
    • DGRASP-mediated noncanonical integrin secretion is required for Drosophila epithelial remodeling
    • 18267086 1:CAS:528:DC%2BD1cXit1Ojs74%3D
    • Schotman H, Karhinen L, Rabouille C (2008) dGRASP-mediated noncanonical integrin secretion is required for Drosophila epithelial remodeling. Dev Cell 14:171-182
    • (2008) Dev Cell , vol.14 , pp. 171-182
    • Schotman, H.1    Karhinen, L.2    Rabouille, C.3
  • 184
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • 21978957 1:CAS:528:DC%2BC3MXht12rtbvF
    • Schwarz F, Aebi M (2011) Mechanisms and principles of N-linked protein glycosylation. Curr Opin Struct Biol 21:576-582
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 185
    • 78649351677 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum domains in determining secretion routes
    • 21173840
    • Seedorf M (2010) Role of endoplasmic reticulum domains in determining secretion routes. F1000 Biol Rep 2:77
    • (2010) F1000 Biol Rep , vol.2 , pp. 77
    • Seedorf, M.1
  • 186
    • 27544483286 scopus 로고    scopus 로고
    • Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1
    • 16247033 1:CAS:528:DC%2BD2MXhtFGktbnJ
    • Seelenmeyer C, Wegehingel S, Tews I, Kunzler M, Aebi M, Nickel W (2005) Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1. J Cell Biol 171:373-381
    • (2005) J Cell Biol , vol.171 , pp. 373-381
    • Seelenmeyer, C.1    Wegehingel, S.2    Tews, I.3    Kunzler, M.4    Aebi, M.5    Nickel, W.6
  • 187
    • 36949012954 scopus 로고    scopus 로고
    • The role of annexin II in angiogenesis and tumor progression: A potential therapeutic target
    • 18220793 1:CAS:528:DC%2BD1cXnsVOhtw%3D%3D
    • Sharma MC, Sharma M (2007) The role of annexin II in angiogenesis and tumor progression: a potential therapeutic target. Curr Pharm Des 13:3568-3575
    • (2007) Curr Pharm des , vol.13 , pp. 3568-3575
    • Sharma, M.C.1    Sharma, M.2
  • 188
  • 189
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • 16901774 1:CAS:528:DC%2BD28XosFGjtLg%3D
    • Shibata Y, Voeltz GK, Rapoport TA (2006) Rough sheets and smooth tubules. Cell 126:435-439
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 190
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • 10487747 1:CAS:528:DyaK1MXms1ajsLY%3D
    • Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, Barr FA (1999) GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J 18:4949-4960
    • (1999) EMBO J , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 191
    • 78650265541 scopus 로고    scopus 로고
    • Exosomes and other microvesicles in infection biology: Organelles with unanticipated phenotypes
    • 21040357 1:CAS:528:DC%2BC3MXivVWhs7o%3D
    • Silverman JM, Reiner NE (2011) Exosomes and other microvesicles in infection biology: organelles with unanticipated phenotypes. Cell Microbiol 13:1-9
    • (2011) Cell Microbiol , vol.13 , pp. 1-9
    • Silverman, J.M.1    Reiner, N.E.2
  • 193
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes - Vesicular carriers for intercellular communication
    • 19442504 1:CAS:528:DC%2BD1MXps1Cltbc%3D
    • Simons M, Raposo G (2009) Exosomes - vesicular carriers for intercellular communication. Curr Opin Cell Biol 21:575-581
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 194
    • 31944449219 scopus 로고    scopus 로고
    • Biogenesis of tubular ER-to-Golgi transport intermediates
    • 16314391 1:CAS:528:DC%2BD28XhtlWrurY%3D
    • Simpson JC, Nilsson T, Pepperkok R (2006) Biogenesis of tubular ER-to-Golgi transport intermediates. Mol Biol Cell 17:723-737
    • (2006) Mol Biol Cell , vol.17 , pp. 723-737
    • Simpson, J.C.1    Nilsson, T.2    Pepperkok, R.3
  • 195
    • 55749112807 scopus 로고    scopus 로고
    • Proteomic profiling of exosomes: Current perspectives
    • 18780348 1:CAS:528:DC%2BD1cXht1Kgur7P
    • Simpson RJ, Jensen SS, Lim JW (2008) Proteomic profiling of exosomes: current perspectives. Proteomics 8:4083-4099
    • (2008) Proteomics , vol.8 , pp. 4083-4099
    • Simpson, R.J.1    Jensen, S.S.2    Lim, J.W.3
  • 197
    • 78149342808 scopus 로고    scopus 로고
    • A novel mRNA affinity purification technique for the identification of interacting proteins and transcripts in ribonucleoprotein complexes
    • 20876833 1:CAS:528:DC%2BC3cXhsVGhsLzJ
    • Slobodin B, Gerst JE (2010) A novel mRNA affinity purification technique for the identification of interacting proteins and transcripts in ribonucleoprotein complexes. RNA 16:2277-2290
    • (2010) RNA , vol.16 , pp. 2277-2290
    • Slobodin, B.1    Gerst, J.E.2
  • 198
    • 0021955354 scopus 로고
    • Intracellular movement of cell surface receptors after endocytosis: Resialylation of asialo-transferrin receptor in human erythroleukemia cells
    • 2982885 1:CAS:528:DyaL2MXht12gu70%3D
    • Snider MD, Rogers OC (1985) Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells. J Cell Biol 100:826-834
    • (1985) J Cell Biol , vol.100 , pp. 826-834
    • Snider, M.D.1    Rogers, O.C.2
  • 199
    • 0022538605 scopus 로고
    • Membrane traffic in animal cells: Cellular glycoproteins return to the site of Golgi mannosidase i
    • 3013899 1:CAS:528:DyaL28XksFyntr4%3D
    • Snider MD, Rogers OC (1986) Membrane traffic in animal cells: cellular glycoproteins return to the site of Golgi mannosidase I. J Cell Biol 103:265-275
    • (1986) J Cell Biol , vol.103 , pp. 265-275
    • Snider, M.D.1    Rogers, O.C.2
  • 200
    • 34447549180 scopus 로고    scopus 로고
    • Differential requirements for ts-O45-G and procollagen biosynthetic transport
    • 17547706 1:CAS:528:DC%2BD2sXovVylu70%3D
    • Starkuviene V, Pepperkok R (2007) Differential requirements for ts-O45-G and procollagen biosynthetic transport. Traffic 8:1035-1051
    • (2007) Traffic , vol.8 , pp. 1035-1051
    • Starkuviene, V.1    Pepperkok, R.2
  • 201
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • 11884515 1:CAS:528:DC%2BD38XivFGnsbc%3D
    • Stephens DJ, Pepperkok R (2002) Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J Cell Sci 115:1149-1160
    • (2002) J Cell Sci , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 202
    • 0023729781 scopus 로고
    • The pathways of endocytosed transferrin and secretory protein are connected in the trans-Golgi reticulum
    • 3260238 1:CAS:528:DyaL1cXkvFSiur0%3D
    • Stoorvogel W, Geuze HJ, Griffith JM, Strous GJ (1988) The pathways of endocytosed transferrin and secretory protein are connected in the trans-Golgi reticulum. J Cell Biol 106:1821-1829
    • (1988) J Cell Biol , vol.106 , pp. 1821-1829
    • Stoorvogel, W.1    Geuze, H.J.2    Griffith, J.M.3    Strous, G.J.4
  • 203
    • 59649103480 scopus 로고    scopus 로고
    • An inactivating mutation within the first extracellular loop of the thyrotropin receptor impedes normal posttranslational maturation of the extracellular domain
    • 18927215 1:CAS:528:DC%2BD1MXhs1Sgt70%3D
    • Sura-Trueba S, Aumas C, Carre A, Durif S, Leger J, Polak M, de Roux N (2009) An inactivating mutation within the first extracellular loop of the thyrotropin receptor impedes normal posttranslational maturation of the extracellular domain. Endocrinology 150:1043-1050
    • (2009) Endocrinology , vol.150 , pp. 1043-1050
    • Sura-Trueba, S.1    Aumas, C.2    Carre, A.3    Durif, S.4    Leger, J.5    Polak, M.6    De Roux, N.7
  • 204
    • 0034644626 scopus 로고    scopus 로고
    • Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier
    • 11030653 1:CAS:528:DC%2BD3cXnsVGitbY%3D
    • Takizawa PA, DeRisi JL, Wilhelm JE, Vale RD (2000) Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 290:341-344
    • (2000) Science , vol.290 , pp. 341-344
    • Takizawa, P.A.1    Derisi, J.L.2    Wilhelm, J.E.3    Vale, R.D.4
  • 206
    • 20544451051 scopus 로고    scopus 로고
    • COPII and exit from the endoplasmic reticulum
    • 15979503 1:CAS:528:DC%2BD2MXlsVCjtb0%3D
    • Tang BL, Wang Y, Ong YS, Hong W (2005) COPII and exit from the endoplasmic reticulum. Biochim Biophys Acta 1744:293-303
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 293-303
    • Tang, B.L.1    Wang, Y.2    Ong, Y.S.3    Hong, W.4
  • 207
    • 0036798783 scopus 로고    scopus 로고
    • Improperly folded green fluorescent protein is secreted via a non-classical pathway
    • 12235295 1:CAS:528:DC%2BD38XotFemurY%3D
    • Tanudji M, Hevi S, Chuck SL (2002) Improperly folded green fluorescent protein is secreted via a non-classical pathway. J Cell Sci 115:3849-3857
    • (2002) J Cell Sci , vol.115 , pp. 3849-3857
    • Tanudji, M.1    Hevi, S.2    Chuck, S.L.3
  • 208
    • 77953141222 scopus 로고    scopus 로고
    • Regulation of ER-Golgi intermediate compartment tubulation and mobility by COPI coats, motor proteins and microtubules
    • 20136777 1:CAS:528:DC%2BC3cXlt1Kis70%3D
    • Tomas M, Martinez-Alonso E, Ballesta J, Martinez-Menarguez JA (2010) Regulation of ER-Golgi intermediate compartment tubulation and mobility by COPI coats, motor proteins and microtubules. Traffic 11:616-625
    • (2010) Traffic , vol.11 , pp. 616-625
    • Tomas, M.1    Martinez-Alonso, E.2    Ballesta, J.3    Martinez-Menarguez, J.A.4
  • 209
    • 33845491061 scopus 로고    scopus 로고
    • Cellular localization and function of the antiviral protein, ovine Mx1 (oMx1): I. Ovine Mx1 is secreted by endometrial epithelial cells via an 'unconventional' secretory pathway
    • 17156187 1:CAS:528:DC%2BD2sXjs12ku7k%3D
    • Toyokawa K, Carling SJ, Ott TL (2007) Cellular localization and function of the antiviral protein, ovine Mx1 (oMx1): I. Ovine Mx1 is secreted by endometrial epithelial cells via an 'unconventional' secretory pathway. Am J Reprod Immunol 57:13-22
    • (2007) Am J Reprod Immunol , vol.57 , pp. 13-22
    • Toyokawa, K.1    Carling, S.J.2    Ott, T.L.3
  • 210
    • 6344225447 scopus 로고    scopus 로고
    • Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae
    • 15356266 1:CAS:528:DC%2BD2cXpslKnsLw%3D
    • Trautwein M, Dengjel J, Schirle M, Spang A (2004) Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae. Mol Biol Cell 15:5021-5037
    • (2004) Mol Biol Cell , vol.15 , pp. 5021-5037
    • Trautwein, M.1    Dengjel, J.2    Schirle, M.3    Spang, A.4
  • 211
    • 70350632412 scopus 로고    scopus 로고
    • A secretory Golgi bypass route to the apical surface domain of epithelial MDCK cells
    • 19765262 1:CAS:528:DC%2BD1MXhtlOitLbM
    • Tveit H, Akslen LK, Fagereng GL, Tranulis MA, Prydz K (2009) A secretory Golgi bypass route to the apical surface domain of epithelial MDCK cells. Traffic 10:1685-1695
    • (2009) Traffic , vol.10 , pp. 1685-1695
    • Tveit, H.1    Akslen, L.K.2    Fagereng, G.L.3    Tranulis, M.A.4    Prydz, K.5
  • 212
    • 0025142335 scopus 로고
    • Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane
    • 2153669 1:CAS:528:DyaK3cXhtlKgurY%3D
    • Urbani L, Simoni RD (1990) Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane. J Biol Chem 265:1919-1923
    • (1990) J Biol Chem , vol.265 , pp. 1919-1923
    • Urbani, L.1    Simoni, R.D.2
  • 213
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • 17486113 1:CAS:528:DC%2BD2sXmtVSmtb8%3D
    • Valadi H, Ekstrom K, Bossios A, Sjostrand M, Lee JJ, Lotvall JO (2007) Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat Cell Biol 9:654-659
    • (2007) Nat Cell Biol , vol.9 , pp. 654-659
    • Valadi, H.1    Ekstrom, K.2    Bossios, A.3    Sjostrand, M.4    Lee, J.J.5    Lotvall, J.O.6
  • 214
    • 80052187639 scopus 로고    scopus 로고
    • Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2
    • 21737841 1:CAS:528:DC%2BC3MXhtVOktL3I
    • Valapala M, Vishwanatha JK (2011) Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2. J Biol Chem 286:30911-30925
    • (2011) J Biol Chem , vol.286 , pp. 30911-30925
    • Valapala, M.1    Vishwanatha, J.K.2
  • 215
    • 33744532148 scopus 로고    scopus 로고
    • Recycling endosomes
    • 16636069
    • van Ijzendoorn SC (2006) Recycling endosomes. J Cell Sci 119:1679-1681
    • (2006) J Cell Sci , vol.119 , pp. 1679-1681
    • Van Ijzendoorn, S.C.1
  • 216
    • 5444220240 scopus 로고    scopus 로고
    • COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
    • 15479737 1:CAS:528:DC%2BD2cXosVOiu70%3D
    • Wang X, Matteson J, An Y, Moyer B, Yoo JS, Bannykh S, Wilson IA, Riordan JR, Balch WE (2004) COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code. J Cell Biol 167:65-74
    • (2004) J Cell Biol , vol.167 , pp. 65-74
    • Wang, X.1    Matteson, J.2    An, Y.3    Moyer, B.4    Yoo, J.S.5    Bannykh, S.6    Wilson, I.A.7    Riordan, J.R.8    Balch, W.E.9
  • 217
    • 33749337008 scopus 로고    scopus 로고
    • A novel recently evolved gene C19orf24 encodes a non-classical secreted protein
    • 16847563 1:CAS:528:DC%2BD28Xht1Gkur%2FO
    • Wang XR, Zhou YB, Liu F, Wang KS, Shen Y, Liu JH, Han ZG (2006) A novel recently evolved gene C19orf24 encodes a non-classical secreted protein. Cell Mol Biol Lett 11:161-170
    • (2006) Cell Mol Biol Lett , vol.11 , pp. 161-170
    • Wang, X.R.1    Zhou, Y.B.2    Liu, F.3    Wang, K.S.4    Shen, Y.5    Liu, J.H.6    Han, Z.G.7
  • 218
    • 79959973077 scopus 로고    scopus 로고
    • Comparative secretome investigation of Magnaporthe oryzae proteins responsive to nitrogen starvation
    • 21563842 1:CAS:528:DC%2BC3MXmvFSltbk%3D
    • Wang Y, Wu J, Park ZY, Kim SG, Rakwal R, Agrawal GK, Kim ST, Kang KY (2011) Comparative secretome investigation of Magnaporthe oryzae proteins responsive to nitrogen starvation. J Proteome Res 10:3136-3148
    • (2011) J Proteome Res , vol.10 , pp. 3136-3148
    • Wang, Y.1    Wu, J.2    Park, Z.Y.3    Kim, S.G.4    Rakwal, R.5    Agrawal, G.K.6    Kim, S.T.7    Kang, K.Y.8
  • 219
    • 78649460427 scopus 로고    scopus 로고
    • Unraveling the Golgi ribbon
    • 21040294
    • Wei JH, Seemann J (2010) Unraveling the Golgi ribbon. Traffic 11:1391-1400
    • (2010) Traffic , vol.11 , pp. 1391-1400
    • Wei, J.H.1    Seemann, J.2
  • 220
    • 27644538815 scopus 로고    scopus 로고
    • Efficient protein trafficking requires trailer hitch, a component of a ribonucleoprotein complex localized to the ER in Drosophila
    • 16256742 1:CAS:528:DC%2BD2MXht1alsLvO
    • Wilhelm JE, Buszczak M, Sayles S (2005) Efficient protein trafficking requires trailer hitch, a component of a ribonucleoprotein complex localized to the ER in Drosophila. Dev Cell 9:675-685
    • (2005) Dev Cell , vol.9 , pp. 675-685
    • Wilhelm, J.E.1    Buszczak, M.2    Sayles, S.3
  • 221
    • 0022508416 scopus 로고
    • Transferrin receptors recycle to cis and middle as well as trans-Golgi cisternae in Ig-secreting myeloma cells
    • 3013900 1:CAS:528:DyaL28XksFyntr8%3D
    • Woods JW, Doriaux M, Farquhar MG (1986) Transferrin receptors recycle to cis and middle as well as trans-Golgi cisternae in Ig-secreting myeloma cells. J Cell Biol 103:277-286
    • (1986) J Cell Biol , vol.103 , pp. 277-286
    • Woods, J.W.1    Doriaux, M.2    Farquhar, M.G.3
  • 222
    • 76149083892 scopus 로고    scopus 로고
    • GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
    • 20083603 1:CAS:528:DC%2BC3cXhsVyjsLw%3D
    • Xiang Y, Wang Y (2010) GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking. J Cell Biol 188:237-251
    • (2010) J Cell Biol , vol.188 , pp. 237-251
    • Xiang, Y.1    Wang, Y.2
  • 224
    • 0033730407 scopus 로고    scopus 로고
    • The p58-positive pre-Golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H+-ATPase
    • 11017878 1:CAS:528:DC%2BD3cXosVKgtbo%3D
    • Ying M, Flatmark T, Saraste J (2000) The p58-positive pre-Golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H+-ATPase. J Cell Sci 113:3623-3638
    • (2000) J Cell Sci , vol.113 , pp. 3623-3638
    • Ying, M.1    Flatmark, T.2    Saraste, J.3
  • 225
    • 0037192856 scopus 로고    scopus 로고
    • Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway
    • 11799116 1:CAS:528:DC%2BD38Xis1Kgsb8%3D
    • Yoo JS, Moyer BD, Bannykh S, Yoo HM, Riordan JR, Balch WE (2002) Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway. J Biol Chem 277:11401-11409
    • (2002) J Biol Chem , vol.277 , pp. 11401-11409
    • Yoo, J.S.1    Moyer, B.D.2    Bannykh, S.3    Yoo, H.M.4    Riordan, J.R.5    Balch, W.E.6
  • 226
    • 34248196504 scopus 로고    scopus 로고
    • A bipartite signal regulates the faithful delivery of apical domain marker podocalyxin/Gp135
    • 17332505 1:CAS:528:DC%2BD2sXlt1Ors7s%3D
    • Yu CY, Chen JY, Lin YY, Shen KF, Lin WL, Chien CL, ter Beest MB, Jou TS (2007) A bipartite signal regulates the faithful delivery of apical domain marker podocalyxin/Gp135. Mol Biol Cell 18:1710-1722
    • (2007) Mol Biol Cell , vol.18 , pp. 1710-1722
    • Yu, C.Y.1    Chen, J.Y.2    Lin, Y.Y.3    Shen, K.F.4    Lin, W.L.5    Chien, C.L.6    Ter Beest, M.B.7    Jou, T.S.8
  • 227
    • 57349191615 scopus 로고    scopus 로고
    • Single-channel analysis of functional epithelial sodium channel (ENaC) stability at the apical membrane of A6 distal kidney cells
    • 18784262 1:CAS:528:DC%2BD1cXhsVWkurzP
    • Yu L, Helms MN, Yue Q, Eaton DC (2008) Single-channel analysis of functional epithelial sodium channel (ENaC) stability at the apical membrane of A6 distal kidney cells. Am J Physiol Renal Physiol 295:F1519-F1527
    • (2008) Am J Physiol Renal Physiol , vol.295
    • Yu, L.1    Helms, M.N.2    Yue, Q.3    Eaton, D.C.4
  • 228
    • 33750299160 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2
    • 17030799 1:CAS:528:DC%2BD28XhtFCjtLjE
    • Zehe C, Engling A, Wegehingel S, Schafer T, Nickel W (2006) Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2. Proc Natl Acad Sci U S A 103:15479-15484
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15479-15484
    • Zehe, C.1    Engling, A.2    Wegehingel, S.3    Schafer, T.4    Nickel, W.5
  • 229
    • 79955692581 scopus 로고    scopus 로고
    • Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes
    • 21556374 1:CAS:528:DC%2BC3MXls1Snu7o%3D
    • Zemskov EA, Mikhailenko I, Hsia RC, Zaritskaya L, Belkin AM (2011) Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes. PLoS One 6:e19414
    • (2011) PLoS One , vol.6 , pp. 19414
    • Zemskov, E.A.1    Mikhailenko, I.2    Hsia, R.C.3    Zaritskaya, L.4    Belkin, A.M.5
  • 230
    • 33645723490 scopus 로고    scopus 로고
    • Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers
    • 16531996 1:CAS:528:DC%2BD28Xjt12qsrk%3D
    • Zeuschner D, Geerts WJ, van Donselaar E, Humbel BM, Slot JW, Koster AJ, Klumperman J (2006) Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers. Nat Cell Biol 8:377-383
    • (2006) Nat Cell Biol , vol.8 , pp. 377-383
    • Zeuschner, D.1    Geerts, W.J.2    Van Donselaar, E.3    Humbel, B.M.4    Slot, J.W.5    Koster, A.J.6    Klumperman, J.7
  • 231
    • 67949115524 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from endothelial cells by a non-classical pathway involving exosomes
    • 19555663 1:CAS:528:DC%2BD1MXps1Chtro%3D
    • Zhan R, Leng X, Liu X, Wang X, Gong J, Yan L, Wang L, Wang Y, Qian LJ (2009) Heat shock protein 70 is secreted from endothelial cells by a non-classical pathway involving exosomes. Biochem Biophys Res Commun 387:229-233
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 229-233
    • Zhan, R.1    Leng, X.2    Liu, X.3    Wang, X.4    Gong, J.5    Yan, L.6    Wang, L.7    Wang, Y.8    Qian, L.J.9
  • 232
    • 34248356819 scopus 로고    scopus 로고
    • EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites
    • 17360537 1:CAS:528:DC%2BD2sXjsFGntLc%3D
    • Zuber C, Cormier JH, Guhl B, Santimaria R, Hebert DN, Roth J (2007) EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc Natl Acad Sci U S A 104:4407-4412
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4407-4412
    • Zuber, C.1    Cormier, J.H.2    Guhl, B.3    Santimaria, R.4    Hebert, D.N.5    Roth, J.6
  • 233
    • 33846821720 scopus 로고    scopus 로고
    • Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation
    • 17164290 1:CAS:528:DC%2BD2sXht1Gmtr4%3D
    • Zuccato E, Blott EJ, Holt O, Sigismund S, Shaw M, Bossi G, Griffiths GM (2007) Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation. J Cell Sci 120:191-199
    • (2007) J Cell Sci , vol.120 , pp. 191-199
    • Zuccato, E.1    Blott, E.J.2    Holt, O.3    Sigismund, S.4    Shaw, M.5    Bossi, G.6    Griffiths, G.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.