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Volumn 270, Issue C, 2008, Pages 145-179

Chapter 4 Protein Trafficking in Polarized Cells

Author keywords

Epithelia; Membrane targetting; Polarity; Sorting determinants; Trafficking

Indexed keywords

LIPID;

EID: 57149088819     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(08)01404-4     Document Type: Review
Times cited : (29)

References (239)
  • 1
    • 30044440555 scopus 로고    scopus 로고
    • A novel type of detergent-resistant membranes may contribute to an early protein sorting event in epithelial cells
    • Alfalah M., Wetzel G., Fischer I., Busche R., Sterchi E.E., Zimmer K., Sallmann H.P., and Naim H.Y. A novel type of detergent-resistant membranes may contribute to an early protein sorting event in epithelial cells. J. Biol. Chem. 280 52 (2005) 42636-42643
    • (2005) J. Biol. Chem. , vol.280 , Issue.52 , pp. 42636-42643
    • Alfalah, M.1    Wetzel, G.2    Fischer, I.3    Busche, R.4    Sterchi, E.E.5    Zimmer, K.6    Sallmann, H.P.7    Naim, H.Y.8
  • 3
    • 0043268862 scopus 로고    scopus 로고
    • The apical compartment: Trafficking pathways, regulators and scaffolding proteins
    • Altschuler Y., Hodson C., and Milgram S.L. The apical compartment: Trafficking pathways, regulators and scaffolding proteins. Curr. Opin. Cell Biol. 15 4 (2003) 423-429
    • (2003) Curr. Opin. Cell Biol. , vol.15 , Issue.4 , pp. 423-429
    • Altschuler, Y.1    Hodson, C.2    Milgram, S.L.3
  • 4
    • 0033523770 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 and endocytosis at the apical surface of Madin-Darby canine kidney cells
    • Altschuler Y., Liu S.-H., Katz L., Tang K., Hardy S., Brodsky F., Apodaca G., and Mostov K. ADP-ribosylation factor 6 and endocytosis at the apical surface of Madin-Darby canine kidney cells. J. Cell Biol. 147 1 (1999) 7-12
    • (1999) J. Cell Biol. , vol.147 , Issue.1 , pp. 7-12
    • Altschuler, Y.1    Liu, S.-H.2    Katz, L.3    Tang, K.4    Hardy, S.5    Brodsky, F.6    Apodaca, G.7    Mostov, K.8
  • 5
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • Ang A.L., Taguchi T., Francis S., Folsch H., Murrells L.J., Pypaert M., Warren G., and Mellman I. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J. Cell Biol. 167 3 (2004) 531-543
    • (2004) J. Cell Biol. , vol.167 , Issue.3 , 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
    • 34247148026 scopus 로고    scopus 로고
    • Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells
    • Au J.S.Y., Puri C., Ihrke G., Kendrick-Jones J., and Buss F. Myosin VI is required for sorting of AP-1B-dependent cargo to the basolateral domain in polarized MDCK cells. J. Cell Biol. 177 1 (2007) 103-114
    • (2007) J. Cell Biol. , vol.177 , Issue.1 , pp. 103-114
    • Au, J.S.Y.1    Puri, C.2    Ihrke, G.3    Kendrick-Jones, J.4    Buss, F.5
  • 8
    • 1542777034 scopus 로고    scopus 로고
    • Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD
    • Baas A.F., Kuipers J., van der Wel N.N., Batlle E., Koerten H.K., Peters P.J., and Clevers H.C. Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD. Cell 116 3 (2004) 457-466
    • (2004) Cell , vol.116 , Issue.3 , pp. 457-466
    • Baas, A.F.1    Kuipers, J.2    van der Wel, N.N.3    Batlle, E.4    Koerten, H.K.5    Peters, P.J.6    Clevers, H.C.7
  • 9
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao R., Antony C., Dotti C., Karsenti E., Stelzer E.H.K., and Simons K. The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109 6I (1989) 2817-2832
    • (1989) J. Cell Biol. , vol.109 , Issue.6 I , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.K.5    Simons, K.6
  • 10
    • 10044225690 scopus 로고    scopus 로고
    • Coupling actin and membrane dynamics during calcium-regulated exocytosis: A role for Rho and ARF GTPases
    • Sp. Iss. SI
    • Bader M.F., Doussau F., Chasserot-Golaz S., Vitale N., and Gasman S. Coupling actin and membrane dynamics during calcium-regulated exocytosis: A role for Rho and ARF GTPases. Biochim. Biophys. Acta Mol. Cell Res. 1742 1-3 (2004) 37-49 Sp. Iss. SI
    • (2004) Biochim. Biophys. Acta Mol. Cell Res. , vol.1742 , Issue.1-3 , pp. 37-49
    • Bader, M.F.1    Doussau, F.2    Chasserot-Golaz, S.3    Vitale, N.4    Gasman, S.5
  • 12
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • Bard F., and Malhotra V. The formation of TGN-to-plasma-membrane transport carriers. Annu. Rev. Cell Dev. Biol. 22 (2006) 439-455
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 13
    • 12844268551 scopus 로고    scopus 로고
    • The adaptor protein AP-4 as a component of the clathrin coat machinery: A morphological study
    • Barois N., and Bakke O. The adaptor protein AP-4 as a component of the clathrin coat machinery: A morphological study. Biochem. J. 385 Part 2 (2005) 503-510
    • (2005) Biochem. J. , vol.385 , Issue.PART 2 , pp. 503-510
    • Barois, N.1    Bakke, O.2
  • 14
    • 0037139604 scopus 로고    scopus 로고
    • Genetic analyses of adaptin function from yeast to mammals
    • Boehm M., and Bonifacino J.S. Genetic analyses of adaptin function from yeast to mammals. Gene 286 2 (2002) 175-186
    • (2002) Gene , vol.286 , Issue.2 , pp. 175-186
    • Boehm, M.1    Bonifacino, J.S.2
  • 15
    • 0036668808 scopus 로고    scopus 로고
    • The μ2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and yppØ sorting signals at distinct sites
    • Boll W., Rapoport I., Brunner C., Modis Y., Prehn S., and Kirchhausen T. The μ2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and yppØ sorting signals at distinct sites. Traffic 3 8 (2002) 590-600
    • (2002) Traffic , vol.3 , Issue.8 , pp. 590-600
    • Boll, W.1    Rapoport, I.2    Brunner, C.3    Modis, Y.4    Prehn, S.5    Kirchhausen, T.6
  • 16
    • 0034036097 scopus 로고    scopus 로고
    • A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi
    • Boman A.L., Zhang C., Zhu X., and Kahn R.A. A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. Mol. Biol. Cell 11 4 (2000) 1241-1255
    • (2000) Mol. Biol. Cell , vol.11 , Issue.4 , pp. 1241-1255
    • Boman, A.L.1    Zhang, C.2    Zhu, X.3    Kahn, R.A.4
  • 17
    • 15744369263 scopus 로고    scopus 로고
    • Novel function for receptor activity-modifying proteins (RAMPs) in post-endocytic receptor trafficking
    • Bomberger J.M., Parameswaran N., Hall C.S., Aiyar N., and Spielman W.S. Novel function for receptor activity-modifying proteins (RAMPs) in post-endocytic receptor trafficking. J. Biol. Chem. 280 10 (2005) 9297-9307
    • (2005) J. Biol. Chem. , vol.280 , Issue.10 , pp. 9297-9307
    • Bomberger, J.M.1    Parameswaran, N.2    Hall, C.S.3    Aiyar, N.4    Spielman, W.S.5
  • 18
    • 0024819257 scopus 로고
    • Endocytosis in filter-grown Madin-Darby canine kidney cells
    • Bomsel M., Prydz K., Parton R.G., Gruenberg J., and Simons K. Endocytosis in filter-grown Madin-Darby canine kidney cells. J. Cell Biol. 109 6 (1989) 3243-3258
    • (1989) J. Cell Biol. , vol.109 , Issue.6 , pp. 3243-3258
    • Bomsel, M.1    Prydz, K.2    Parton, R.G.3    Gruenberg, J.4    Simons, K.5
  • 19
    • 0025029828 scopus 로고
    • Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel M., Parton R., Kuznetsov S.A., Schroer T.A., and Gruenberg J. Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell 62 4 (1990) 719-731
    • (1990) Cell , vol.62 , Issue.4 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kuznetsov, S.A.3    Schroer, T.A.4    Gruenberg, J.5
  • 20
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: Adaptors on the move
    • Bonifacino J.S. The GGA proteins: Adaptors on the move. Nat. Rev. Mol. Cell Biol. 5 1 (2004) 23-32
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , Issue.1 , pp. 23-32
    • Bonifacino, J.S.1
  • 21
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino J.S., and Dell'Angelica E.C. Molecular bases for the recognition of tyrosine-based sorting signals. J. Cell Biol. 145 5 (1999) 923-926
    • (1999) J. Cell Biol. , vol.145 , Issue.5 , pp. 923-926
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 22
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 23
    • 0025606401 scopus 로고
    • Regulation of microtubule dynamics and nucleation during polarization in MDCK-II cells
    • Bre M., Pepperkok R., Hill A., Levilliers N., Ansorge W., Stelzer E., and Karsenti E. Regulation of microtubule dynamics and nucleation during polarization in MDCK-II cells. J. Cell Biol. 111 6 (1990) 3013-3021
    • (1990) J. Cell Biol. , vol.111 , Issue.6 , pp. 3013-3021
    • Bre, M.1    Pepperkok, R.2    Hill, A.3    Levilliers, N.4    Ansorge, W.5    Stelzer, E.6    Karsenti, E.7
  • 24
    • 0025605057 scopus 로고
    • Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells
    • Breitfeld P.P., Mckinnon W.C., and Mostov K.E. Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells. J. Cell Biol. 111 6 (1990) 2365-2373
    • (1990) J. Cell Biol. , vol.111 , Issue.6 , pp. 2365-2373
    • Breitfeld, P.P.1    Mckinnon, W.C.2    Mostov, K.E.3
  • 25
    • 33845309656 scopus 로고    scopus 로고
    • Lipid rafts, detergent-resistant membranes, and raft targeting signals
    • Brown D.A. Lipid rafts, detergent-resistant membranes, and raft targeting signals. Physiology 21 (2006) 430-439
    • (2006) Physiology , vol.21 , pp. 430-439
    • Brown, D.A.1
  • 26
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., and London E. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14 (1998) 111-136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 27
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of 2 proteins in MDCK cells
    • Brown D.A., Crise B., and Rose J. Mechanism of membrane anchoring affects polarized expression of 2 proteins in MDCK cells. Science 245 4925 (1989) 1499-1501
    • (1989) Science , vol.245 , Issue.4925 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.3
  • 28
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition
    • Brugger B., Graham C., Leibrecht I., Mombelli E., Jen A., Wieland F., and Morris R. The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition. J. Biol. Chem. 279 9 (2004) 7530-7536
    • (2004) J. Biol. Chem. , vol.279 , Issue.9 , pp. 7530-7536
    • Brugger, B.1    Graham, C.2    Leibrecht, I.3    Mombelli, E.4    Jen, A.5    Wieland, F.6    Morris, R.7
  • 29
    • 33846065117 scopus 로고    scopus 로고
    • Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells
    • Capaldo C.T., and Macara I.G. Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells. Mol. Biol. Cell 18 1 (2007) 189-200
    • (2007) Mol. Biol. Cell , vol.18 , Issue.1 , pp. 189-200
    • Capaldo, C.T.1    Macara, I.G.2
  • 31
    • 57149113835 scopus 로고    scopus 로고
    • Defective coupling of apical PTH receptors to phospholipase c and loss of PTH induced internalization of NaPI-IIa in NHERF1 knock out mice
    • Capuano P., Bacic D., Roos M., Gisler S.M., Biber J., Kaissling B., Weinman E.J., Wagner C.A., and Murer H. Defective coupling of apical PTH receptors to phospholipase c and loss of PTH induced internalization of NaPI-IIa in NHERF1 knock out mice. Nephrol. Dial. Transplant. 20 Suppl. 5 (2005) V187-V188
    • (2005) Nephrol. Dial. Transplant. , vol.20 , Issue.SUPPL. 5
    • Capuano, P.1    Bacic, D.2    Roos, M.3    Gisler, S.M.4    Biber, J.5    Kaissling, B.6    Weinman, E.J.7    Wagner, C.A.8    Murer, H.9
  • 33
    • 21244439989 scopus 로고    scopus 로고
    • Myosin II regulatory light chain is required for trafficking of bile salt export protein to the apical membrane in Madin-Darby canine kidney cells
    • Chan W., Calderon G., Swift A.L., Moseley J., Li S.H., Hosoya H., Arias I.M., and Ortiz D.F. Myosin II regulatory light chain is required for trafficking of bile salt export protein to the apical membrane in Madin-Darby canine kidney cells. J. Biol. Chem. 280 25 (2005) 23741-23747
    • (2005) J. Biol. Chem. , vol.280 , Issue.25 , pp. 23741-23747
    • Chan, W.1    Calderon, G.2    Swift, A.L.3    Moseley, J.4    Li, S.H.5    Hosoya, H.6    Arias, I.M.7    Ortiz, D.F.8
  • 35
    • 14544288669 scopus 로고    scopus 로고
    • The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin
    • Chen H., and De Camilli P. The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin. Proc. Natl. Acad. Sci. USA 102 8 (2005) 2766-2771
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.8 , pp. 2766-2771
    • Chen, H.1    De Camilli, P.2
  • 36
    • 33847240063 scopus 로고    scopus 로고
    • Reconstructing the endocytotic machinery
    • Cheng Y., and Walz T. Reconstructing the endocytotic machinery. Methods Cell Biol. 79 (2007) 463-487
    • (2007) Methods Cell Biol. , vol.79 , pp. 463-487
    • Cheng, Y.1    Walz, T.2
  • 37
    • 33645292025 scopus 로고    scopus 로고
    • Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids
    • Cheng Z., Singh R.D., Marks D.L., and Pagano R.E. Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids. Mol. Membr. Biol. 23 1 (2006) 101-110
    • (2006) Mol. Membr. Biol. , vol.23 , Issue.1 , pp. 101-110
    • Cheng, Z.1    Singh, R.D.2    Marks, D.L.3    Pagano, R.E.4
  • 38
    • 0030989282 scopus 로고    scopus 로고
    • Intracellular association between UDP-glucose: Glycoprotein glucosyltransferase and an incompletely folded variant of α1-antitrypsin
    • Choudhury P., Liu Y., Bick R.J., and Sifers R.N. Intracellular association between UDP-glucose: Glycoprotein glucosyltransferase and an incompletely folded variant of α1-antitrypsin. J. Biol. Chem. 272 20 (1997) 13446-13451
    • (1997) J. Biol. Chem. , vol.272 , Issue.20 , pp. 13446-13451
    • Choudhury, P.1    Liu, Y.2    Bick, R.J.3    Sifers, R.N.4
  • 39
    • 34249704583 scopus 로고    scopus 로고
    • Post-endocytic sorting of calcitonin receptor-like receptor and receptor activity-modifying protein 1
    • Cottrell G.S., Padilla B., Pikios S., Roosterman D., Steinhoff M., Grady E.F., and Bunnett N.W. Post-endocytic sorting of calcitonin receptor-like receptor and receptor activity-modifying protein 1. J. Biol. Chem. 282 16 (2007) 12260-12271
    • (2007) J. Biol. Chem. , vol.282 , Issue.16 , pp. 12260-12271
    • Cottrell, G.S.1    Padilla, B.2    Pikios, S.3    Roosterman, D.4    Steinhoff, M.5    Grady, E.F.6    Bunnett, N.W.7
  • 40
    • 0030797573 scopus 로고    scopus 로고
    • A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric acid secretion
    • Courtois-Coutry N., Roush D., Rajendran V., McCarthy J.B., Geibel J., Kashgarian M., and Caplan M.J. A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric acid secretion. Cell 90 3 (1997) 501-510
    • (1997) Cell , vol.90 , Issue.3 , pp. 501-510
    • Courtois-Coutry, N.1    Roush, D.2    Rajendran, V.3    McCarthy, J.B.4    Geibel, J.5    Kashgarian, M.6    Caplan, M.J.7
  • 41
    • 34447264528 scopus 로고    scopus 로고
    • What is the function of neuronal AP-3?
    • Danglot L., and Galli T. What is the function of neuronal AP-3?. Mol. Biol. Cell 99 7 (2007) 349-361
    • (2007) Mol. Biol. Cell , vol.99 , Issue.7 , pp. 349-361
    • Danglot, L.1    Galli, T.2
  • 42
    • 33645311204 scopus 로고    scopus 로고
    • Lipid raft organization and function in brush borders of epithelial cells
    • Danielsen E.M., and Hansen G.H. Lipid raft organization and function in brush borders of epithelial cells. Mol. Membr. Biol. 23 1 (2006) 71-79
    • (2006) Mol. Membr. Biol. , vol.23 , Issue.1 , pp. 71-79
    • Danielsen, E.M.1    Hansen, G.H.2
  • 43
    • 0035910554 scopus 로고    scopus 로고
    • Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16
    • Daub H., Gevaert K., Vandekerckhove J., Sobel A., and Hall A. Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16. J. Biol. Chem. 276 3 (2001) 1677-1680
    • (2001) J. Biol. Chem. , vol.276 , Issue.3 , pp. 1677-1680
    • Daub, H.1    Gevaert, K.2    Vandekerckhove, J.3    Sobel, A.4    Hall, A.5
  • 44
    • 33750850353 scopus 로고    scopus 로고
    • Apical protein transport
    • Delacour D., and Jacob R. Apical protein transport. Cell. Mol. Life Sci. 63 21 (2006) 2491-2505
    • (2006) Cell. Mol. Life Sci. , vol.63 , Issue.21 , pp. 2491-2505
    • Delacour, D.1    Jacob, R.2
  • 47
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • Deora A.B., Kreitzer G., Jacovina A.T., and Hajjar K.A. An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface. J. Biol. Chem. 279 42 (2004) 43411-43418
    • (2004) J. Biol. Chem. , vol.279 , Issue.42 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 49
    • 21044448584 scopus 로고    scopus 로고
    • The cell biology of Hermansky-Pudlak syndrome: Recent advances
    • Di Pietro S.M., and Dell'Angelica E.C. The cell biology of Hermansky-Pudlak syndrome: Recent advances. Traffic 6 7 (2005) 525-533
    • (2005) Traffic , vol.6 , Issue.7 , pp. 525-533
    • Di Pietro, S.M.1    Dell'Angelica, E.C.2
  • 50
    • 31744442614 scopus 로고    scopus 로고
    • Stonin 2 is an AP-2-dependent endocytic sorting adaptor for synaptotagmin internalization and recycling
    • Diril M.K., Wienisch M., Jung N., Klingauf J., and Haucke V. Stonin 2 is an AP-2-dependent endocytic sorting adaptor for synaptotagmin internalization and recycling. Dev. Cell 10 2 (2006) 233-244
    • (2006) Dev. Cell , vol.10 , Issue.2 , pp. 233-244
    • Diril, M.K.1    Wienisch, M.2    Jung, N.3    Klingauf, J.4    Haucke, V.5
  • 51
    • 34447629085 scopus 로고    scopus 로고
    • Regulatory binding partners and complexes of NHE3
    • Donowitz M., and Li X.H. Regulatory binding partners and complexes of NHE3. Physiol. Rev. 87 3 (2007) 825-872
    • (2007) Physiol. Rev. , vol.87 , Issue.3 , pp. 825-872
    • Donowitz, M.1    Li, X.H.2
  • 52
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray B., Ghosh P., Griffith J., Geuze H.J., and Kornfeld S. Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297 5587 (2002) 1700-1703
    • (2002) Science , vol.297 , Issue.5587 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 53
    • 0346734131 scopus 로고    scopus 로고
    • The tetraspanin CD63 enhances the internalization of the H,K-ATPase beta-subunit
    • Duffield A., Kamsteeg E.J., Brown A.N., Pagel P., and Caplan M.J. The tetraspanin CD63 enhances the internalization of the H,K-ATPase beta-subunit. Proc. Natl. Acad. Sci. USA 100 26 (2003) 15560-15565
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.26 , pp. 15560-15565
    • Duffield, A.1    Kamsteeg, E.J.2    Brown, A.N.3    Pagel, P.4    Caplan, M.J.5
  • 54
    • 2942641824 scopus 로고    scopus 로고
    • Sorting of H,K-ATPase beta-subunit in MDCK and LLC-PK1 cells is independent of μ 1B adaptin expression
    • Duffield A., Folsch H., Mellman I., and Caplan M.J. Sorting of H,K-ATPase beta-subunit in MDCK and LLC-PK1 cells is independent of μ 1B adaptin expression. Traffic 5 6 (2004) 449-461
    • (2004) Traffic , vol.5 , Issue.6 , pp. 449-461
    • Duffield, A.1    Folsch, H.2    Mellman, I.3    Caplan, M.J.4
  • 55
    • 0034695917 scopus 로고    scopus 로고
    • A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase
    • Dunbar L.A., Aronson P., and Caplan M.J. A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase. J. Cell Biol. 148 4 (2000) 769-778
    • (2000) J. Cell Biol. , vol.148 , Issue.4 , pp. 769-778
    • Dunbar, L.A.1    Aronson, P.2    Caplan, M.J.3
  • 56
  • 57
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus
    • Erickson J.W., Zhang C.J., Kahn R.A., Evans T., and Cerione R.A. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem. 271 43 (1996) 26850-26854
    • (1996) J. Biol. Chem. , vol.271 , Issue.43 , pp. 26850-26854
    • Erickson, J.W.1    Zhang, C.J.2    Kahn, R.A.3    Evans, T.4    Cerione, R.A.5
  • 58
    • 37849189374 scopus 로고    scopus 로고
    • Roles of the actin cytoskeleton and myosins in the endomembrane system
    • Fath K.R. Roles of the actin cytoskeleton and myosins in the endomembrane system. Adv. Mol. Cell Biol. 37 (2006) 119-134
    • (2006) Adv. Mol. Cell Biol. , vol.37 , pp. 119-134
    • Fath, K.R.1
  • 59
    • 0035793377 scopus 로고    scopus 로고
    • Control of fusion pore during exocytosis by Munc18
    • Fisher R.J., Pevsner J., and Burgoyne R.D. Control of fusion pore during exocytosis by Munc18. Science 291 5505 (2001) 875-878
    • (2001) Science , vol.291 , Issue.5505 , pp. 875-878
    • Fisher, R.J.1    Pevsner, J.2    Burgoyne, R.D.3
  • 61
    • 16844374089 scopus 로고    scopus 로고
    • The building blocks for basolateral vesicles in polarized epithelial cells
    • Folsch H. The building blocks for basolateral vesicles in polarized epithelial cells. Trends Cell Biol. 15 4 (2005) 222-228
    • (2005) Trends Cell Biol. , vol.15 , Issue.4 , pp. 222-228
    • Folsch, H.1
  • 62
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Folsch H., Ohno H., Bonifacino J.S., and Mellman I. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99 2 (1999) 189-198
    • (1999) Cell , vol.99 , Issue.2 , pp. 189-198
    • Folsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 63
    • 2942592305 scopus 로고    scopus 로고
    • Myosin VI: A structural role in actin organization important for protein and organelle localization and trafficking
    • Frank D.J., Noguchi T., and Miller K.G. Myosin VI: A structural role in actin organization important for protein and organelle localization and trafficking. Curr. Opin. Cell Biol. 16 2 (2004) 189-194
    • (2004) Curr. Opin. Cell Biol. , vol.16 , Issue.2 , pp. 189-194
    • Frank, D.J.1    Noguchi, T.2    Miller, K.G.3
  • 64
    • 4744352147 scopus 로고    scopus 로고
    • Endocytic and transcytotic processes in villous syncytiotrophoblast: Role in nutrient transport to the human fetus
    • Fuchs R., and Ellinger I. Endocytic and transcytotic processes in villous syncytiotrophoblast: Role in nutrient transport to the human fetus. Traffic 5 10 (2004) 725-738
    • (2004) Traffic , vol.5 , Issue.10 , pp. 725-738
    • Fuchs, R.1    Ellinger, I.2
  • 66
    • 0141533034 scopus 로고    scopus 로고
    • Roles of Rho-family GTPases in cell polarisation and directional migration
    • Fukata M., Nakagawa M., and Kaibuchi K. Roles of Rho-family GTPases in cell polarisation and directional migration. Curr. Opin. Cell Biol. 15 5 (2003) 590-597
    • (2003) Curr. Opin. Cell Biol. , vol.15 , Issue.5 , pp. 590-597
    • Fukata, M.1    Nakagawa, M.2    Kaibuchi, K.3
  • 68
    • 0032482226 scopus 로고    scopus 로고
    • In polarized MDCK cells basolateral vesicles arise from clathrin-γ- adaptin-coated domains on endosomal tubules
    • Futter C.E., Gibson A., Allchin E.H., Maxwell S., Ruddock L.J., Odorizzi G., et al. In polarized MDCK cells basolateral vesicles arise from clathrin-γ- adaptin-coated domains on endosomal tubules. J. Cell Biol. 141 3 (1998) 611-623
    • (1998) J. Cell Biol. , vol.141 , Issue.3 , pp. 611-623
    • Futter, C.E.1    Gibson, A.2    Allchin, E.H.3    Maxwell, S.4    Ruddock, L.J.5    Odorizzi, G.6
  • 69
    • 0036045770 scopus 로고    scopus 로고
    • The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane
    • Gan Y.B., McGraw T.E., and Rodriguez-Boulan E. The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nat. Cell Biol. 4 8 (2002) 605-609
    • (2002) Nat. Cell Biol. , vol.4 , Issue.8 , pp. 605-609
    • Gan, Y.B.1    McGraw, T.E.2    Rodriguez-Boulan, E.3
  • 70
    • 0037022122 scopus 로고    scopus 로고
    • Assembly of epithelial tight is negatively regulated by junctions
    • Gao L., Joberty G., and Macara I.G. Assembly of epithelial tight is negatively regulated by junctions. Curr. Biol. 12 3 (2002) 221-225
    • (2002) Curr. Biol. , vol.12 , Issue.3 , pp. 221-225
    • Gao, L.1    Joberty, G.2    Macara, I.G.3
  • 71
    • 0037416217 scopus 로고    scopus 로고
    • Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein
    • Garrard S.M., Capaldo C.T., Gao L., Rosen M.K., Macara I.G., and Tomchick D.R. Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein. EMBO J. 22 5 (2003) 1125-1133
    • (2003) EMBO J. , vol.22 , Issue.5 , pp. 1125-1133
    • Garrard, S.M.1    Capaldo, C.T.2    Gao, L.3    Rosen, M.K.4    Macara, I.G.5    Tomchick, D.R.6
  • 72
    • 33748199154 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells
    • U64
    • Gassama-Diagne A., Yu W., ter Beest M., Martin-Belmonte F., Kierbel A., Engel J., and Mostov K. Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells. Nat. Cell Biol. 8 9 (2006) 963 U64
    • (2006) Nat. Cell Biol. , vol.8 , Issue.9 , pp. 963
    • Gassama-Diagne, A.1    Yu, W.2    ter Beest, M.3    Martin-Belmonte, F.4    Kierbel, A.5    Engel, J.6    Mostov, K.7
  • 73
    • 33748920372 scopus 로고    scopus 로고
    • AMPA and NMDA glutamate receptor trafficking: Multiple roads for reaching and leaving the synapse
    • Groc L., and Choquet D. AMPA and NMDA glutamate receptor trafficking: Multiple roads for reaching and leaving the synapse. Cell Tissue Res. 326 2 (2006) 423-438
    • (2006) Cell Tissue Res. , vol.326 , Issue.2 , pp. 423-438
    • Groc, L.1    Choquet, D.2
  • 74
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg J., and Stenmark H. The biogenesis of multivesicular endosomes. Nat. Rev. Mol. Cell Biol. 5 4 (2004) 317-323
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , Issue.4 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 75
    • 0034685807 scopus 로고    scopus 로고
    • Characterization of rapid membrane internalization and recycling
    • Hao M., and Maxfield F.R. Characterization of rapid membrane internalization and recycling. J. Biol. Chem. 275 20 (2000) 15279-15286
    • (2000) J. Biol. Chem. , vol.275 , Issue.20 , pp. 15279-15286
    • Hao, M.1    Maxfield, F.R.2
  • 76
    • 34047126285 scopus 로고    scopus 로고
    • Mapping the interactions between Lys48 and Lys63-linked di-ubiquitins and a ubiquitin-interacting motif of S5a
    • Haririnia A., D'Onofrio M., and Fushman D. Mapping the interactions between Lys48 and Lys63-linked di-ubiquitins and a ubiquitin-interacting motif of S5a. J. Mol. Biol. 368 3 (2007) 753-766
    • (2007) J. Mol. Biol. , vol.368 , Issue.3 , pp. 753-766
    • Haririnia, A.1    D'Onofrio, M.2    Fushman, D.3
  • 77
    • 0034740693 scopus 로고    scopus 로고
    • Mechanisma and role of PDZ domains in signaling complex assembly
    • Harris B.Z., and Lim W.A. Mechanisma and role of PDZ domains in signaling complex assembly. J. Cell Sci. 114 18 (2001) 3219-3231
    • (2001) J. Cell Sci. , vol.114 , Issue.18 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 78
    • 28844478464 scopus 로고    scopus 로고
    • Phosphoinositide regulation of clathrin-mediated endocytosis
    • Haucke V. Phosphoinositide regulation of clathrin-mediated endocytosis. Biochem. Soc. Trans. 33 6 (2005) 1285-1289
    • (2005) Biochem. Soc. Trans. , vol.33 , Issue.6 , pp. 1285-1289
    • Haucke, V.1
  • 79
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L., and Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19 (2003) 141-172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 80
    • 0037351330 scopus 로고    scopus 로고
    • Changing directions: Clathrin-mediated transport between the Golgi and endosomes
    • Hinners I., and Tooze S.A. Changing directions: Clathrin-mediated transport between the Golgi and endosomes. J. Cell Sci. 116 5 (2003) 763-771
    • (2003) J. Cell Sci. , vol.116 , Issue.5 , pp. 763-771
    • Hinners, I.1    Tooze, S.A.2
  • 82
    • 3042542722 scopus 로고    scopus 로고
    • The subapical compartment: A traffic center in membrane polarity development
    • Hoekstra D., Tyteca D., and van IJzendoorn S.C.D. The subapical compartment: A traffic center in membrane polarity development. J. Cell Sci. 117 11 (2004) 2183-2192
    • (2004) J. Cell Sci. , vol.117 , Issue.11 , pp. 2183-2192
    • Hoekstra, D.1    Tyteca, D.2    van IJzendoorn, S.C.D.3
  • 83
    • 15044339712 scopus 로고    scopus 로고
    • Compartmentalization of growth factor receptor signalling
    • Hoeller D., Volarevic S., and Dikic I. Compartmentalization of growth factor receptor signalling. Curr. Opin. Cell Biol. 17 2 (2005) 107-111
    • (2005) Curr. Opin. Cell Biol. , vol.17 , Issue.2 , pp. 107-111
    • Hoeller, D.1    Volarevic, S.2    Dikic, I.3
  • 84
    • 1642279428 scopus 로고    scopus 로고
    • Glycosphingolipid clusters as organizers of plasma membrane rafts and caveolate
    • Hoessli D.C., Semac I., Iqbal A., Nasir-ud-Din A., and Borisch B. Glycosphingolipid clusters as organizers of plasma membrane rafts and caveolate. Curr. Org. Chem. 8 5 (2004) 439-452
    • (2004) Curr. Org. Chem. , vol.8 , Issue.5 , pp. 439-452
    • Hoessli, D.C.1    Semac, I.2    Iqbal, A.3    Nasir-ud-Din, A.4    Borisch, B.5
  • 85
    • 0039252786 scopus 로고    scopus 로고
    • The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains
    • Hofmann M.W., Honing S., Rodionov D., Dobberstein B., von Figura K., and Bakke O. The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains. J. Biol. Chem. 274 51 (1999) 36153-36158
    • (1999) J. Biol. Chem. , vol.274 , Issue.51 , pp. 36153-36158
    • Hofmann, M.W.1    Honing, S.2    Rodionov, D.3    Dobberstein, B.4    von Figura, K.5    Bakke, O.6
  • 86
    • 23844556932 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. SNAREs and traffic. Biochim. Biophys. Acta 1744 3 (2005) 493-517
    • (2005) Biochim. Biophys. Acta , vol.1744 , Issue.3 , pp. 493-517
    • Hong, W.1
  • 87
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • Honing S., Sandoval I.V., and von Figura K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J. 17 5 (1998) 1304-1314
    • (1998) EMBO J. , vol.17 , Issue.5 , pp. 1304-1314
    • Honing, S.1    Sandoval, I.V.2    von Figura, K.3
  • 89
    • 0025168710 scopus 로고
    • Differential microtubule requirements for transcytosis in MDCK cells
    • Hunziker W., Male P., and Mellman I. Differential microtubule requirements for transcytosis in MDCK cells. EMBO J. 9 11 (1990) 3515-3525
    • (1990) EMBO J. , vol.9 , Issue.11 , pp. 3515-3525
    • Hunziker, W.1    Male, P.2    Mellman, I.3
  • 90
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
    • Hurd T.W., Gao L., Roh M.H., Macara I.G., and Margolis B. Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat. Cell Biol. 5 2 (2003) 137-142
    • (2003) Nat. Cell Biol. , vol.5 , Issue.2 , pp. 137-142
    • Hurd, T.W.1    Gao, L.2    Roh, M.H.3    Macara, I.G.4    Margolis, B.5
  • 91
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley J.H., and Emr S.D. The ESCRT complexes: Structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 277-298
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 92
    • 0842291430 scopus 로고    scopus 로고
    • Carboxy terminus of glucose transporter 3 contains an apical membrane targeting domain
    • Inukai K., Shewan A.M., Pascoe W.S., Katayama S., James D.E., and Oka Y. Carboxy terminus of glucose transporter 3 contains an apical membrane targeting domain. Mol. Endocrinol. 18 2 (2004) 339-349
    • (2004) Mol. Endocrinol. , vol.18 , Issue.2 , pp. 339-349
    • Inukai, K.1    Shewan, A.M.2    Pascoe, W.S.3    Katayama, S.4    James, D.E.5    Oka, Y.6
  • 93
    • 0022753927 scopus 로고
    • Modulation of p36 phosphorylation in human-cells-Studies using anti-p36 monoclonal-antibodies
    • Isacke C.M., Trowbridge I.S., and Hunter T. Modulation of p36 phosphorylation in human-cells-Studies using anti-p36 monoclonal-antibodies. Mol. Cell. Biol. 6 7 (1986) 2745-2751
    • (1986) Mol. Cell. Biol. , vol.6 , Issue.7 , pp. 2745-2751
    • Isacke, C.M.1    Trowbridge, I.S.2    Hunter, T.3
  • 94
    • 0037380088 scopus 로고    scopus 로고
    • Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells
    • Jacob R., Heine M., Alfalah M., and Naim H.Y. Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells. Curr. Biol. 13 7 (2003) 607-612
    • (2003) Curr. Biol. , vol.13 , Issue.7 , pp. 607-612
    • Jacob, R.1    Heine, M.2    Alfalah, M.3    Naim, H.Y.4
  • 96
    • 0036017680 scopus 로고    scopus 로고
    • Clathrin-dependent or not: Is it still the question?
    • Johannes L., and Lamaze C. Clathrin-dependent or not: Is it still the question?. Traffic 3 7 (2002) 443-451
    • (2002) Traffic , vol.3 , Issue.7 , pp. 443-451
    • Johannes, L.1    Lamaze, C.2
  • 97
    • 0032585530 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation
    • Jost M., Simpson F., Kavran J.M., Lemmon M.A., and Schmid S.L. Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation. Curr. Biol. 8 25 (1998) 1399-1402
    • (1998) Curr. Biol. , vol.8 , Issue.25 , pp. 1399-1402
    • Jost, M.1    Simpson, F.2    Kavran, J.M.3    Lemmon, M.A.4    Schmid, S.L.5
  • 98
    • 0033832942 scopus 로고    scopus 로고
    • RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: Involvement of the Ral pathway in receptor endocytosis
    • Jullien-Flores V., Mahe Y., Mirey G., Leprince C., Meunier-Bisceuil B., Sorkin A., and Camonis J.H. RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: Involvement of the Ral pathway in receptor endocytosis. J. Cell Sci. 113 16 (2000) 2837-2844
    • (2000) J. Cell Sci. , vol.113 , Issue.16 , pp. 2837-2844
    • Jullien-Flores, V.1    Mahe, Y.2    Mirey, G.3    Leprince, C.4    Meunier-Bisceuil, B.5    Sorkin, A.6    Camonis, J.H.7
  • 99
    • 0032544565 scopus 로고    scopus 로고
    • The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C-elegans EGF receptor LET-23 in vulval epithelial cells
    • Kaech S.M., Whitfield C.W., and Kim S.K. The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C-elegans EGF receptor LET-23 in vulval epithelial cells. Cell 94 6 (1998) 761-771
    • (1998) Cell , vol.94 , Issue.6 , pp. 761-771
    • Kaech, S.M.1    Whitfield, C.W.2    Kim, S.K.3
  • 100
    • 0037041026 scopus 로고    scopus 로고
    • Unusual structural organization of the endocytic proteins AP180 and epsin 1
    • Kalthoff C., Alves J., Urbanke C., Knorr R., and Ungewickell E.J. Unusual structural organization of the endocytic proteins AP180 and epsin 1. J. Biol. Chem. 277 10 (2002) 8209-8216
    • (2002) J. Biol. Chem. , vol.277 , Issue.10 , pp. 8209-8216
    • Kalthoff, C.1    Alves, J.2    Urbanke, C.3    Knorr, R.4    Ungewickell, E.J.5
  • 102
    • 28844501267 scopus 로고    scopus 로고
    • Analysis of ubiquitin-dependent protein sorting within the endocytic pathway in Saccharomyces cerevisiae
    • Katzmann D.J., and Wendland B. Analysis of ubiquitin-dependent protein sorting within the endocytic pathway in Saccharomyces cerevisiae. Methods Enzymol. 399 Part B (2005) 192-211
    • (2005) Methods Enzymol. , vol.399 , Issue.PART B , pp. 192-211
    • Katzmann, D.J.1    Wendland, B.2
  • 103
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann D.J., Odorizzi G., and Emr S.D. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3 12 (2002) 893-905
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , Issue.12 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 105
    • 0032432673 scopus 로고    scopus 로고
    • Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: Disorders of protein trafficking and the role of ER molecular chaperones
    • Kim P.S., and Arvan P. Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: Disorders of protein trafficking and the role of ER molecular chaperones. Endocr. Rev. 19 2 (1998) 173-202
    • (1998) Endocr. Rev. , vol.19 , Issue.2 , pp. 173-202
    • Kim, P.S.1    Arvan, P.2
  • 106
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E., and Sheng M. PDZ domain proteins of synapses. Nat. Rev. Neurosci. 5 10 (2004) 771-781
    • (2004) Nat. Rev. Neurosci. , vol.5 , Issue.10 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 109
    • 0036087626 scopus 로고    scopus 로고
    • FcRn-mediated transcytosis of immunoglobulin G in human renal proximal tubular epithelial cells
    • Kobayashi N., Suzuki Y., Tsuge T., Okumura K., Ra C., and Tomino Y. FcRn-mediated transcytosis of immunoglobulin G in human renal proximal tubular epithelial cells. Am. J. Physiol. Ren. Physiol. 282 2 51-2 (2002) F358-F365
    • (2002) Am. J. Physiol. Ren. Physiol. , vol.282 , Issue.2 51-2
    • Kobayashi, N.1    Suzuki, Y.2    Tsuge, T.3    Okumura, K.4    Ra, C.5    Tomino, Y.6
  • 110
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski R., Hall A., and Mellman I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell Biol. 1 1 (1999) 8-13
    • (1999) Nat. Cell Biol. , vol.1 , Issue.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 111
    • 33751072638 scopus 로고    scopus 로고
    • Lys63-linked polyubiquitin chains-Linking more than just ubiquitin
    • Kawadler H., and Yang X.L. Lys63-linked polyubiquitin chains-Linking more than just ubiquitin. Cancer Biol. Ther. 5 10 (2006) 1273-1274
    • (2006) Cancer Biol. Ther. , vol.5 , Issue.10 , pp. 1273-1274
    • Kawadler, H.1    Yang, X.L.2
  • 112
    • 0036704540 scopus 로고    scopus 로고
    • Clathrin-Protein interactions
    • Lafer E.M. Clathrin-Protein interactions. Traffic 3 8 (2002) 513-520
    • (2002) Traffic , vol.3 , Issue.8 , pp. 513-520
    • Lafer, E.M.1
  • 113
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney-cells
    • Lafont F., Burkhardt J.K., and Simons K. Involvement of microtubule motors in basolateral and apical transport in kidney-cells. Nature 372 6508 (1994) 801-803
    • (1994) Nature , vol.372 , Issue.6508 , pp. 801-803
    • Lafont, F.1    Burkhardt, J.K.2    Simons, K.3
  • 114
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont F., Lecat S., Verkade P., and Simons K. Annexin XIIIb associates with lipid microdomains to function in apical delivery. J. Cell Biol. 142 6 (1998) 1413-1427
    • (1998) J. Cell Biol. , vol.142 , Issue.6 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 115
    • 0033616708 scopus 로고    scopus 로고
    • Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells
    • Lafont F., Verkade P., Galli T., Wimmer C., Louvard D., and Simons K. Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells. Proc. Natl. Acad. Sci. USA 96 7 (1999) 3734-3738
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.7 , pp. 3734-3738
    • Lafont, F.1    Verkade, P.2    Galli, T.3    Wimmer, C.4    Louvard, D.5    Simons, K.6
  • 116
    • 33745594600 scopus 로고    scopus 로고
    • The distribution and targeting of neuronal voltage-gated ion channels
    • Lai H.C., and Jan L.Y. The distribution and targeting of neuronal voltage-gated ion channels. Nat. Rev. Neurosci. 7 7 (2006) 548-562
    • (2006) Nat. Rev. Neurosci. , vol.7 , Issue.7 , pp. 548-562
    • Lai, H.C.1    Jan, L.Y.2
  • 117
    • 33751084598 scopus 로고    scopus 로고
    • The emerging role of PDZ adapter proteins for regulation of intestinal ion transport
    • Lamprecht G., and Seidler U. The emerging role of PDZ adapter proteins for regulation of intestinal ion transport. Am. J. Physiol.-Gastrointest. Liver Physiol. 291 5 (2006) G766-G777
    • (2006) Am. J. Physiol.-Gastrointest. Liver Physiol. , vol.291 , Issue.5
    • Lamprecht, G.1    Seidler, U.2
  • 118
    • 27144543784 scopus 로고    scopus 로고
    • Scaffolding microdomains and beyond: The function of reggie/flotillin proteins
    • Langhorst M.F., Reuter A., and Stuermer C.A.O. Scaffolding microdomains and beyond: The function of reggie/flotillin proteins. Cell. Mol. Life Sci. 62 19-20 (2005) 2228-2240
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.19-20 , pp. 2228-2240
    • Langhorst, M.F.1    Reuter, A.2    Stuermer, C.A.O.3
  • 120
    • 2942625797 scopus 로고    scopus 로고
    • Plasma membrane microdomains: Organization, function and trafficking (review)
    • Laude A.J., and Prior I.A. Plasma membrane microdomains: Organization, function and trafficking (review). Mol. Membr. Biol. 21 3 (2004) 193-205
    • (2004) Mol. Membr. Biol. , vol.21 , Issue.3 , pp. 193-205
    • Laude, A.J.1    Prior, I.A.2
  • 122
    • 0038269099 scopus 로고    scopus 로고
    • + exchanger 3 (NHE3) activity by increasing its exocytosis by an NHE3 kinase A regulatory protein-dependent mechanism
    • + exchanger 3 (NHE3) activity by increasing its exocytosis by an NHE3 kinase A regulatory protein-dependent mechanism. J. Biol. Chem. 278 19 (2003) 16494-16501
    • (2003) J. Biol. Chem. , vol.278 , Issue.19 , pp. 16494-16501
    • Lee-Kwon, W.1    Kawano, K.2    Choi, J.W.3    Kim, J.H.4    Donowitz, M.5
  • 123
    • 0034084289 scopus 로고    scopus 로고
    • Sorting of membrane and fluid at the apical pole of polarized Madin-Darby canine kidney cells
    • Leung S.M., Ruiz W.G., and Apodaca G. Sorting of membrane and fluid at the apical pole of polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 11 6 (2000) 2131
    • (2000) Mol. Biol. Cell , vol.11 , Issue.6 , pp. 2131
    • Leung, S.M.1    Ruiz, W.G.2    Apodaca, G.3
  • 125
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial-cells
    • Lisanti M.P., Caras I.W., Davitz M.A., and Rodriguez-Boulan E. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial-cells. J. Cell Biol. 109 5 (1989) 2145-2156
    • (1989) J. Cell Biol. , vol.109 , Issue.5 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 126
    • 33846807375 scopus 로고    scopus 로고
    • Yeast P4-ATPases Drs2p and Dnf1p are essential cargos of the NPFXD/Sla1p endocytic pathway
    • Liu K., Hua Z.L., Nepute J.A., and Graham T.R. Yeast P4-ATPases Drs2p and Dnf1p are essential cargos of the NPFXD/Sla1p endocytic pathway. Mol. Biol. Cell 18 2 (2007) 487-500
    • (2007) Mol. Biol. Cell , vol.18 , Issue.2 , pp. 487-500
    • Liu, K.1    Hua, Z.L.2    Nepute, J.A.3    Graham, T.R.4
  • 127
    • 0029847075 scopus 로고    scopus 로고
    • Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • Low S.H., Chapin S.J., Weimbs T., Komuves L.G., Bennett M.K., and Mostov K.E. Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 7 12 (1996) 2007-2018
    • (1996) Mol. Biol. Cell , vol.7 , Issue.12 , pp. 2007-2018
    • Low, S.H.1    Chapin, S.J.2    Weimbs, T.3    Komuves, L.G.4    Bennett, M.K.5    Mostov, K.E.6
  • 129
    • 1542350778 scopus 로고    scopus 로고
    • Par proteins: Partners in polarization
    • Macara A.G. Par proteins: Partners in polarization. Curr. Biol. 14 4 (2004) R160-R162
    • (2004) Curr. Biol. , vol.14 , Issue.4
    • Macara, A.G.1
  • 130
    • 33748969492 scopus 로고    scopus 로고
    • Endocytic adaptors: Recruiters, coordinators and regulators
    • Maldonado-Baez L., and Wendland B. Endocytic adaptors: Recruiters, coordinators and regulators. Trends Cell Biol. 16 10 (2006) 505-513
    • (2006) Trends Cell Biol. , vol.16 , Issue.10 , pp. 505-513
    • Maldonado-Baez, L.1    Wendland, B.2
  • 131
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells-The cytoplasmic domain contains 2 tyrosine-dependent targeting determinants
    • Matter K., Hunziker W., and Mellman I. Basolateral sorting of LDL receptor in MDCK cells-The cytoplasmic domain contains 2 tyrosine-dependent targeting determinants. Cell 71 5 (1992) 741-753
    • (1992) Cell , vol.71 , Issue.5 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 133
    • 33845355027 scopus 로고    scopus 로고
    • Interaction of epithelial ion channels with the actin-based cytoskeleton
    • Mazzochi C., Benos D.J., and Smith P.R. Interaction of epithelial ion channels with the actin-based cytoskeleton. Am. J. Physiol.-Ren. Physiol. 291 6 (2006) F1113-F1122
    • (2006) Am. J. Physiol.-Ren. Physiol. , vol.291 , Issue.6
    • Mazzochi, C.1    Benos, D.J.2    Smith, P.R.3
  • 134
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride H.M., Rybin V., Murphy C., Giner A., Teasdale R., and Zerial M. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98 3 (1999) 377-386
    • (1999) Cell , vol.98 , Issue.3 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 135
    • 33748762242 scopus 로고    scopus 로고
    • Vesicle formation at the plasma membrane and trans-Golgi network: The same but different
    • McNiven M.A., and Thompson H.M. Vesicle formation at the plasma membrane and trans-Golgi network: The same but different. Science 313 5793 (2006) 1591-1594
    • (2006) Science , vol.313 , Issue.5793 , pp. 1591-1594
    • McNiven, M.A.1    Thompson, H.M.2
  • 136
    • 34347401218 scopus 로고    scopus 로고
    • Regulation of receptors and transporters by ubiquitination: New insights into surprisingly similar mechanisms
    • Miranda M., and Sorkin A. Regulation of receptors and transporters by ubiquitination: New insights into surprisingly similar mechanisms. Mol. Interv. 7 3 (2007) 157-167
    • (2007) Mol. Interv. , vol.7 , Issue.3 , pp. 157-167
    • Miranda, M.1    Sorkin, A.2
  • 137
    • 34248185949 scopus 로고    scopus 로고
    • LKB1 and AMPK maintain epithelial cell polarity under energetic stress
    • Mirouse V., Swick L.L., Kazgan N., St Johnston D., and Brenman J.E. LKB1 and AMPK maintain epithelial cell polarity under energetic stress. J. Cell Biol. 177 3 (2007) 387-392
    • (2007) J. Cell Biol. , vol.177 , Issue.3 , pp. 387-392
    • Mirouse, V.1    Swick, L.L.2    Kazgan, N.3    St Johnston, D.4    Brenman, J.E.5
  • 138
    • 0028824434 scopus 로고
    • Characterization of myosin-Ia and Myosin-Ib, 2 unconventional myosins associated with the drosophila brush-border cytoskeleton
    • Morgan N.S., Heintzelman M.B., and Mooseker M.S. Characterization of myosin-Ia and Myosin-Ib, 2 unconventional myosins associated with the drosophila brush-border cytoskeleton. Dev. Biol. 172 1 (1995) 51-71
    • (1995) Dev. Biol. , vol.172 , Issue.1 , pp. 51-71
    • Morgan, N.S.1    Heintzelman, M.B.2    Mooseker, M.S.3
  • 139
    • 0033592669 scopus 로고    scopus 로고
    • Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis
    • Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A., and Kikuchi A. Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis. Oncogene 18 43 (1999) 5915-5922
    • (1999) Oncogene , vol.18 , Issue.43 , pp. 5915-5922
    • Morinaka, K.1    Koyama, S.2    Nakashima, S.3    Hinoi, T.4    Okawa, K.5    Iwamatsu, A.6    Kikuchi, A.7
  • 141
  • 142
    • 0037383848 scopus 로고    scopus 로고
    • Polarized epithelial membrane traffic: Conservation and plasticity
    • Mostov K.E., Su T., and ter Beest M. Polarized epithelial membrane traffic: Conservation and plasticity. Nat. Cell Biol. 5 4 (2003) 287-293
    • (2003) Nat. Cell Biol. , vol.5 , Issue.4 , pp. 287-293
    • Mostov, K.E.1    Su, T.2    ter Beest, M.3
  • 143
    • 33645732101 scopus 로고    scopus 로고
    • Vesicular trafficking of tyrosine kinase receptors and associated proteins in the regulation of signaling and vascular function
    • Mukherjee S., Tessema M., and Wandinger-Ness A. Vesicular trafficking of tyrosine kinase receptors and associated proteins in the regulation of signaling and vascular function. Circ. Res. 98 6 (2006) 743-756
    • (2006) Circ. Res. , vol.98 , Issue.6 , pp. 743-756
    • Mukherjee, S.1    Tessema, M.2    Wandinger-Ness, A.3
  • 144
    • 32344453668 scopus 로고    scopus 로고
    • Analysis of hVps34/hVps15 interactions with Rab5 in vivo and in vitro
    • Murray J.T., and Backer J.M. Analysis of hVps34/hVps15 interactions with Rab5 in vivo and in vitro. Methods Enzymol. 403 (2005) 789-799
    • (2005) Methods Enzymol. , vol.403 , pp. 789-799
    • Murray, J.T.1    Backer, J.M.2
  • 145
    • 0842309131 scopus 로고    scopus 로고
    • ER-to-golgi transport and cytoskeletal interactions in animal cells
    • Murshid A., and Presley J.F. ER-to-golgi transport and cytoskeletal interactions in animal cells. Cell. Mol. Life Sci. 61 2 (2004) 133-145
    • (2004) Cell. Mol. Life Sci. , vol.61 , Issue.2 , pp. 133-145
    • Murshid, A.1    Presley, J.F.2
  • 146
    • 0042858417 scopus 로고    scopus 로고
    • Cell biology of the presynaptic terminal
    • Murthy V.N., and De Camilli P. Cell biology of the presynaptic terminal. Annu. Rev. Neurosci. 26 (2003) 701-728
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 701-728
    • Murthy, V.N.1    De Camilli, P.2
  • 147
    • 0742289586 scopus 로고    scopus 로고
    • Microtubule organization and function in epithelial cells
    • Musch A. Microtubule organization and function in epithelial cells. Traffic 5 1 (2004) 1-9
    • (2004) Traffic , vol.5 , Issue.1 , pp. 1-9
    • Musch, A.1
  • 148
    • 0035341316 scopus 로고    scopus 로고
    • cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network
    • Musch A., Cohen D., Kreitzer G., and Rodriguez-Boulan E. cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J. 20 9 (2001) 2171-2179
    • (2001) EMBO J. , vol.20 , Issue.9 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 149
    • 0032475976 scopus 로고    scopus 로고
    • Identification of sorting determinants in the C-terminal cytoplasmic tails of the gamma-aminobutyric acid transporters GAT-2 and GAT-3
    • Muth T.R., Ahn J., and Caplan M.J. Identification of sorting determinants in the C-terminal cytoplasmic tails of the gamma-aminobutyric acid transporters GAT-2 and GAT-3. J. Biol. Chem. 273 40 (1998) 25616-25627
    • (1998) J. Biol. Chem. , vol.273 , Issue.40 , pp. 25616-25627
    • Muth, T.R.1    Ahn, J.2    Caplan, M.J.3
  • 150
    • 0033580927 scopus 로고    scopus 로고
    • Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV
    • Naim H.Y., Joberty G., Alfalah M., and Jacob R. Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV. J. Biol. Chem. 274 25 (1999) 17961-17967
    • (1999) J. Biol. Chem. , vol.274 , Issue.25 , pp. 17961-17967
    • Naim, H.Y.1    Joberty, G.2    Alfalah, M.3    Jacob, R.4
  • 151
    • 3342977736 scopus 로고    scopus 로고
    • Characterization of a nonclathrin endocytic pathway: Membrane cargo and lipid requirements
    • Naslavsky N., Weigert R., and Donaldson J.G. Characterization of a nonclathrin endocytic pathway: Membrane cargo and lipid requirements. Mol. Biol. Cell 15 8 (2004) 3542-3552
    • (2004) Mol. Biol. Cell , vol.15 , Issue.8 , pp. 3542-3552
    • Naslavsky, N.1    Weigert, R.2    Donaldson, J.G.3
  • 152
    • 0033522506 scopus 로고    scopus 로고
    • Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant μ2 subunit and its effects on endocytosis
    • Nesterov A., Carter R.E., Sorkina T., Gill G.N., and Sorkin A. Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant μ2 subunit and its effects on endocytosis. EMBO J. 18 9 (1999) 2489-2499
    • (1999) EMBO J. , vol.18 , Issue.9 , pp. 2489-2499
    • Nesterov, A.1    Carter, R.E.2    Sorkina, T.3    Gill, G.N.4    Sorkin, A.5
  • 154
    • 0035494465 scopus 로고    scopus 로고
    • KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes
    • Noda Y., Okada Y., Saito N., Setou M., Xu Y., Zhang Z.Z., and Hirokawa N. KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes. J. Cell Biol. 155 1 (2001) 77-88
    • (2001) J. Cell Biol. , vol.155 , Issue.1 , pp. 77-88
    • Noda, Y.1    Okada, Y.2    Saito, N.3    Setou, M.4    Xu, Y.5    Zhang, Z.Z.6    Hirokawa, N.7
  • 155
    • 0038784499 scopus 로고    scopus 로고
    • Transcytotic efflux from early endosomes is dependent on cholesterol and glycosphingolipids in polarized hepatic cells
    • Nyasae L.K., Hubbard A.L., and Tuma P.L. Transcytotic efflux from early endosomes is dependent on cholesterol and glycosphingolipids in polarized hepatic cells. Mol. Biol. Cell 14 7 (2003) 2689-2705
    • (2003) Mol. Biol. Cell , vol.14 , Issue.7 , pp. 2689-2705
    • Nyasae, L.K.1    Hubbard, A.L.2    Tuma, P.L.3
  • 156
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh P., McIntosh D.P., and Schnitzer J.E. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141 1 (1998) 101-114
    • (1998) J. Cell Biol. , vol.141 , Issue.1 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 159
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S., Sarnataro D., Pillich R., Tivodar S., Nitsch L., and Zurzolo C. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 167 4 (2004) 699-709
    • (2004) J. Cell Biol. , vol.167 , Issue.4 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 160
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton R.G., Joggerst B., and Simons K. Regulated internalization of caveolae. J. Cell Biol. 127 5 (1994) 1199-1215
    • (1994) J. Cell Biol. , vol.127 , Issue.5 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 161
    • 0036239115 scopus 로고    scopus 로고
    • Endocytosis via caveolae
    • Pelkmans L., and Helenius A. Endocytosis via caveolae. Traffic 3 5 (2002) 311-320
    • (2002) Traffic , vol.3 , Issue.5 , pp. 311-320
    • Pelkmans, L.1    Helenius, A.2
  • 162
    • 0034717801 scopus 로고    scopus 로고
    • Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb
    • Plant P.J., Lafont F., Lecat S., Verkade P., Simons K., and Rotin D. Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb. J. Cell Biol. 149 7 (2000) 1473-1483
    • (2000) J. Cell Biol. , vol.149 , Issue.7 , pp. 1473-1483
    • Plant, P.J.1    Lafont, F.2    Lecat, S.3    Verkade, P.4    Simons, K.5    Rotin, D.6
  • 163
    • 2342599664 scopus 로고    scopus 로고
    • Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway
    • Polishchuk R., Di Pentima A., and Lippincott-Schwartz J. Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nat. Cell Biol. 6 4 (2004) 297-307
    • (2004) Nat. Cell Biol. , vol.6 , Issue.4 , pp. 297-307
    • Polishchuk, R.1    Di Pentima, A.2    Lippincott-Schwartz, J.3
  • 164
    • 0142134219 scopus 로고    scopus 로고
    • Munc18-2/syntaxin3 complexes are spatially separated from syntaxin3-containing SNARE complexes
    • Pombo I., Rivera J., and Blank U. Munc18-2/syntaxin3 complexes are spatially separated from syntaxin3-containing SNARE complexes. FEBS Lett. 550 1-3 (2003) 144-148
    • (2003) FEBS Lett. , vol.550 , Issue.1-3 , pp. 144-148
    • Pombo, I.1    Rivera, J.2    Blank, U.3
  • 165
    • 1542313963 scopus 로고    scopus 로고
    • Specific N-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol-anchored forms of endolyn in Madin-Darby canine kidney cells
    • Potter B.A., Ihrke G., Bruns J.R., Weixel K.M., and Weisz O.A. Specific N-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol-anchored forms of endolyn in Madin-Darby canine kidney cells. Mol. Biol. Cell 15 3 (2004) 1407-1416
    • (2004) Mol. Biol. Cell , vol.15 , Issue.3 , pp. 1407-1416
    • Potter, B.A.1    Ihrke, G.2    Bruns, J.R.3    Weixel, K.M.4    Weisz, O.A.5
  • 167
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells
    • Puertollano R., Martin-Belmonte F., Millan J., de Marco M.D., Albar J.P., Kremer L., and Alonso M.A. The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. J. Cell Biol. 145 1 (1999) 141-151
    • (1999) J. Cell Biol. , vol.145 , Issue.1 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    de Marco, M.D.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 168
    • 34250899749 scopus 로고    scopus 로고
    • Ubiquitin trafficking to the lysosome-Keeping the house tidy and getting rid of unwanted guests
    • Purdy G.E., and Russell D.G. Ubiquitin trafficking to the lysosome-Keeping the house tidy and getting rid of unwanted guests. Autophagy 3 4 (2007) 399-401
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 399-401
    • Purdy, G.E.1    Russell, D.G.2
  • 169
  • 170
    • 34347407665 scopus 로고    scopus 로고
    • Exogenous MAL reroutes selected hepatic apical proteins into the direct pathway in WIF-B cells
    • Ramnarayanan S.P., Cheng C.A., Bastaki M., and Tuma P.L. Exogenous MAL reroutes selected hepatic apical proteins into the direct pathway in WIF-B cells. Mol. Biol. Cell 18 7 (2007) 2707-2715
    • (2007) Mol. Biol. Cell , vol.18 , Issue.7 , pp. 2707-2715
    • Ramnarayanan, S.P.1    Cheng, C.A.2    Bastaki, M.3    Tuma, P.L.4
  • 171
    • 1542358809 scopus 로고    scopus 로고
    • Streamlined synaptic vesicle cycle in cone photoreceptor terminals
    • Rea R., Li J., Dharia A., Levitan E.S., Sterling P., and Kramer R.H. Streamlined synaptic vesicle cycle in cone photoreceptor terminals. Neuron 41 5 (2004) 755-766
    • (2004) Neuron , vol.41 , Issue.5 , pp. 755-766
    • Rea, R.1    Li, J.2    Dharia, A.3    Levitan, E.S.4    Sterling, P.5    Kramer, R.H.6
  • 172
    • 34249689155 scopus 로고    scopus 로고
    • Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
    • Rickman C., Medine C.N., Bergmann A., and Duncan R.R. Functionally and spatially distinct modes of munc18-syntaxin 1 interaction. J. Biol. Chem. 282 16 (2007) 12097-12103
    • (2007) J. Biol. Chem. , vol.282 , Issue.16 , pp. 12097-12103
    • Rickman, C.1    Medine, C.N.2    Bergmann, A.3    Duncan, R.R.4
  • 173
    • 0032513225 scopus 로고    scopus 로고
    • Medium chains of adaptor complexes AP-1 and AP-2 recognize leucine-based sorting signals from the invariant chain
    • Rodionov D.G., and Bakke O. Medium chains of adaptor complexes AP-1 and AP-2 recognize leucine-based sorting signals from the invariant chain. J. Biol. Chem. 273 11 (1998) 6005-6008
    • (1998) J. Biol. Chem. , vol.273 , Issue.11 , pp. 6005-6008
    • Rodionov, D.G.1    Bakke, O.2
  • 174
  • 176
    • 0036902323 scopus 로고    scopus 로고
    • Immunoglobulin transport across polarized epithelial cells
    • Rojas R., and Apodaca G. Immunoglobulin transport across polarized epithelial cells. Nat. Rev. Mol. Cell Biol. 3 12 (2002) 944-955
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , Issue.12 , pp. 944-955
    • Rojas, R.1    Apodaca, G.2
  • 177
    • 0032500602 scopus 로고    scopus 로고
    • Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Roush D.L., Gottardi C.J., Naim H.Y., Roth M.G., and Caplan M.J. Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells. J. Biol. Chem. 273 41 (1998) 26862-26869
    • (1998) J. Biol. Chem. , vol.273 , Issue.41 , pp. 26862-26869
    • Roush, D.L.1    Gottardi, C.J.2    Naim, H.Y.3    Roth, M.G.4    Caplan, M.J.5
  • 178
    • 33745902844 scopus 로고    scopus 로고
    • Molecular mechanisms of late endosome morphology, identity and sorting
    • Russell M.R.G., Nickerson D.P., and Odorizzi G. Molecular mechanisms of late endosome morphology, identity and sorting. Curr. Opin. Cell Biol. 18 4 (2006) 422-428
    • (2006) Curr. Opin. Cell Biol. , vol.18 , Issue.4 , pp. 422-428
    • Russell, M.R.G.1    Nickerson, D.P.2    Odorizzi, G.3
  • 179
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated clathrin-independent pinocytic pathway
    • Sabharanjak S., Sharma P., Parton R.G., and Mayor S. GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated clathrin-independent pinocytic pathway. Dev. Cell 2 4 (2002) 411-423
    • (2002) Dev. Cell , vol.2 , Issue.4 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 180
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaun C., James D.J., and Chamberlain L.H. Lipid rafts and the regulation of exocytosis. Traffic 5 4 (2004) 255-264
    • (2004) Traffic , vol.5 , Issue.4 , pp. 255-264
    • Salaun, C.1    James, D.J.2    Chamberlain, L.H.3
  • 181
    • 0024564286 scopus 로고
    • Endocytosis from coated pits of shiga toxin: A glycolipid-binding protein from shigella dysenteriae 1
    • Sandvig K., Olsnes S., Brown J.E., Petersen O.W., and Van Deurs B. Endocytosis from coated pits of shiga toxin: A glycolipid-binding protein from shigella dysenteriae 1. J. Cell Biol. 108 4 (1989) 1331-1343
    • (1989) J. Cell Biol. , vol.108 , Issue.4 , pp. 1331-1343
    • Sandvig, K.1    Olsnes, S.2    Brown, J.E.3    Petersen, O.W.4    Van Deurs, B.5
  • 182
    • 34247282758 scopus 로고    scopus 로고
    • Functional symmetry of endomembranes
    • Saraste J., and Goud B. Functional symmetry of endomembranes. Mol. Biol. Cell 18 4 (2007) 1430-1436
    • (2007) Mol. Biol. Cell , vol.18 , Issue.4 , pp. 1430-1436
    • Saraste, J.1    Goud, B.2
  • 183
    • 0034351416 scopus 로고    scopus 로고
    • Glycosylation and protein transport
    • Scheiffele P., and Fullekrug J. Glycosylation and protein transport. Mol. Trafficking 36 (2000) 27-35
    • (2000) Mol. Trafficking , vol.36 , pp. 27-35
    • Scheiffele, P.1    Fullekrug, J.2
  • 184
    • 0028810337 scopus 로고
    • N-Glycans as apical sorting signals in epithelial-cells
    • Scheiffele P., Peranen J., and Simons K. N-Glycans as apical sorting signals in epithelial-cells. Nature 378 6552 (1995) 96-98
    • (1995) Nature , vol.378 , Issue.6552 , pp. 96-98
    • Scheiffele, P.1    Peranen, J.2    Simons, K.3
  • 185
    • 33745509798 scopus 로고    scopus 로고
    • Endocytosis of the glucose transporter GLUT8 is mediated by interaction of a dileucine motif with the beta 2-adaptin subunit of the AP-2 adaptor complex
    • Schmidt U., Briese S., Leicht K., Schurmann A., Joost H.G., and Al-Hasani H. Endocytosis of the glucose transporter GLUT8 is mediated by interaction of a dileucine motif with the beta 2-adaptin subunit of the AP-2 adaptor complex. J. Cell Sci. 119 11 (2006) 2321-2331
    • (2006) J. Cell Sci. , vol.119 , Issue.11 , pp. 2321-2331
    • Schmidt, U.1    Briese, S.2    Leicht, K.3    Schurmann, A.4    Joost, H.G.5    Al-Hasani, H.6
  • 186
    • 0029014820 scopus 로고
    • Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases
    • Schnitzer J.E., Liu J., and Oh P. Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases. J. Biol. Chem. 270 24 (1995) 14399-14404
    • (1995) J. Biol. Chem. , vol.270 , Issue.24 , pp. 14399-14404
    • Schnitzer, J.E.1    Liu, J.2    Oh, P.3
  • 187
    • 0035965995 scopus 로고    scopus 로고
    • Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo
    • Schubert W., Frank P.G., Razani B., Park D.S., Chow C., and Lisanti M.P. Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo. J. Biol. Chem. 276 52 (2001) 48619-48622
    • (2001) J. Biol. Chem. , vol.276 , Issue.52 , pp. 48619-48622
    • Schubert, W.1    Frank, P.G.2    Razani, B.3    Park, D.S.4    Chow, C.5    Lisanti, M.P.6
  • 188
    • 33645294371 scopus 로고    scopus 로고
    • Controversy fuels trafficking of GPI-anchored proteins
    • Schuck S., and Simons K. Controversy fuels trafficking of GPI-anchored proteins. J. Cell Biol. 172 7 (2006) 963-965
    • (2006) J. Cell Biol. , vol.172 , Issue.7 , pp. 963-965
    • Schuck, S.1    Simons, K.2
  • 189
    • 0037018151 scopus 로고    scopus 로고
    • Transferrin receptor recycling in the absence of perinuclear recycling endosomes
    • Sheff D., Pelletier L., O'Connell C.B., Warren G., and Mellman I. Transferrin receptor recycling in the absence of perinuclear recycling endosomes. J. Cell Biol. 156 5 (2002) 797-804
    • (2002) J. Cell Biol. , vol.156 , Issue.5 , pp. 797-804
    • Sheff, D.1    Pelletier, L.2    O'Connell, C.B.3    Warren, G.4    Mellman, I.5
  • 190
    • 0037143761 scopus 로고    scopus 로고
    • Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting
    • Shenolikar S., Voltz J.W., Minkoff C.M., Wade J.B., and Weinman E.J. Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting. Proc. Natl. Acad. Sci. USA 99 17 (2002) 11470-11475
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.17 , pp. 11470-11475
    • Shenolikar, S.1    Voltz, J.W.2    Minkoff, C.M.3    Wade, J.B.4    Weinman, E.J.5
  • 191
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination
    • Shenoy S.K., and Lefkowitz R.J. Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination. J. Biol. Chem. 278 16 (2003) 14498-14506
    • (2003) J. Biol. Chem. , vol.278 , Issue.16 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 192
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih S.C., Sloper-Mould K.E., and Hicke L. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J. 19 2 (2000) 187-198
    • (2000) EMBO J. , vol.19 , Issue.2 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 193
    • 27244457650 scopus 로고    scopus 로고
    • The AP-3 clathrin-associated complex is essential for embryonic and larval development in Caenorhabditis elegans
    • Shim J., and Lee J. The AP-3 clathrin-associated complex is essential for embryonic and larval development in Caenorhabditis elegans. Mol. Cells 19 3 (2005) 452-457
    • (2005) Mol. Cells , vol.19 , Issue.3 , pp. 452-457
    • Shim, J.1    Lee, J.2
  • 194
    • 2942711520 scopus 로고    scopus 로고
    • RalA but not RalB enhances polarized delivery of membrane proteins to the basolateral surface of epithelial cells
    • Shipitsin M., and Feig L.A. RalA but not RalB enhances polarized delivery of membrane proteins to the basolateral surface of epithelial cells. Mol. Cell. Biol. 24 13 (2004) 5746-5756
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.13 , pp. 5746-5756
    • Shipitsin, M.1    Feig, L.A.2
  • 195
    • 0036167130 scopus 로고    scopus 로고
    • AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells
    • Simmen T., Honing S., Icking A., Tikkanen R., and Hunziker W. AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. Nat. Cell Biol. 4 2 (2002) 154-159
    • (2002) Nat. Cell Biol. , vol.4 , Issue.2 , pp. 154-159
    • Simmen, T.1    Honing, S.2    Icking, A.3    Tikkanen, R.4    Hunziker, W.5
  • 196
    • 0034529050 scopus 로고    scopus 로고
    • Cell biology-How cells handle cholesterol
    • Simons K., and Ikonen E. Cell biology-How cells handle cholesterol. Science 290 5497 (2000) 1721-1726
    • (2000) Science , vol.290 , Issue.5497 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 199
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner T., Bennett M.K., Whiteheart S.W., Scheller R.H., and Rothman J.E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75 3 (1993) 409-418
    • (1993) Cell , vol.75 , Issue.3 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 200
    • 3142583466 scopus 로고    scopus 로고
    • Cargo recognition during clathrin-mediated endocytosis: A team effort
    • Sorkin A. Cargo recognition during clathrin-mediated endocytosis: A team effort. Curr. Opin. Cell Biol. 16 4 (2004) 392-399
    • (2004) Curr. Opin. Cell Biol. , vol.16 , Issue.4 , pp. 392-399
    • Sorkin, A.1
  • 203
    • 0036428014 scopus 로고    scopus 로고
    • The molecular machinery for the biogenesis of lysosome-related organelles: Lessons from Hermansky-Pudlak syndrome
    • Starcevic M., Nazarian R., and Dell'Angelica E.C. The molecular machinery for the biogenesis of lysosome-related organelles: Lessons from Hermansky-Pudlak syndrome. Semin. Cell Dev. Biol. 13 4 (2002) 271-278
    • (2002) Semin. Cell Dev. Biol. , vol.13 , Issue.4 , pp. 271-278
    • Starcevic, M.1    Nazarian, R.2    Dell'Angelica, E.C.3
  • 204
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton R.B., Fasshauer D., Jahn R., and Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395 6700 (1998) 347-353
    • (1998) Nature , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 205
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved PAR protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., and Ohno S. Atypical protein kinase C is involved in the evolutionarily conserved PAR protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152 6 (2001) 1183-1196
    • (2001) J. Cell Biol. , vol.152 , Issue.6 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 206
    • 0037404459 scopus 로고    scopus 로고
    • Identification of an apical sorting determinant in the cytoplasmic tail of megalin
    • Takeda T., Yamazaki H., and Farquhar M.G. Identification of an apical sorting determinant in the cytoplasmic tail of megalin. Am. J. Physiol.-Cell Physiol. 284 5 (2003) C1105-C1113
    • (2003) Am. J. Physiol.-Cell Physiol. , vol.284 , Issue.5
    • Takeda, T.1    Yamazaki, H.2    Farquhar, M.G.3
  • 207
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., and De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature 374 6518 (1995) 186-190
    • (1995) Nature , vol.374 , Issue.6518 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 208
    • 0346752326 scopus 로고    scopus 로고
    • Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL
    • Tall R.D., Alonso M.A., and Roth M.G. Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL. Traffic 4 12 (2003) 838-849
    • (2003) Traffic , vol.4 , Issue.12 , pp. 838-849
    • Tall, R.D.1    Alonso, M.A.2    Roth, M.G.3
  • 209
    • 34547629068 scopus 로고    scopus 로고
    • Interaction of carboxyl-terminal peptides of cytosolic-tail of apactin with PDZ domains of NHERF/EBP50 and PDZK-1/CAP70
    • Tandon C., De Lisle R.C., Boulatnikov I., and Naik P.K. Interaction of carboxyl-terminal peptides of cytosolic-tail of apactin with PDZ domains of NHERF/EBP50 and PDZK-1/CAP70. Mol. Cell. Biochem. 302 1-2 (2007) 157-167
    • (2007) Mol. Cell. Biochem. , vol.302 , Issue.1-2 , pp. 157-167
    • Tandon, C.1    De Lisle, R.C.2    Boulatnikov, I.3    Naik, P.K.4
  • 210
    • 4444236958 scopus 로고    scopus 로고
    • Control of immune responses by trafficking cell surface proteins, vesicles and lipid rafts to and from the immunological synapse
    • Taner S.B., Onfelt B., Pirinen N.J., McCann F.E., Magee A.I., and Davis D.M. Control of immune responses by trafficking cell surface proteins, vesicles and lipid rafts to and from the immunological synapse. Traffic 5 9 (2004) 651-661
    • (2004) Traffic , vol.5 , Issue.9 , pp. 651-661
    • Taner, S.B.1    Onfelt, B.2    Pirinen, N.J.3    McCann, F.E.4    Magee, A.I.5    Davis, D.M.6
  • 211
    • 0027094236 scopus 로고
    • The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11-binding and Ca-2+-binding sites
    • Thiel C., Osborn M., and Gerke V. The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11-binding and Ca-2+-binding sites. J. Cell Sci. 103 Part 3 (1992) 733-742
    • (1992) J. Cell Sci. , vol.103 , Issue.PART 3 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 212
    • 0026649584 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide
    • Thomas P.J., Shenbagamurthi P., Sondek J., Hullihen J.M., and Pedersen P.L. The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide. J. Biol. Chem. 267 9 (1992) 5727-5730
    • (1992) J. Biol. Chem. , vol.267 , Issue.9 , pp. 5727-5730
    • Thomas, P.J.1    Shenbagamurthi, P.2    Sondek, J.3    Hullihen, J.M.4    Pedersen, P.L.5
  • 213
    • 0027407766 scopus 로고
    • Vesicular stomatitis-virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine
    • Thomas D.C., Brewer C.B., and Roth M.G. Vesicular stomatitis-virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine. J. Biol. Chem. 268 5 (1993) 3313-3320
    • (1993) J. Biol. Chem. , vol.268 , Issue.5 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 214
    • 34347369621 scopus 로고    scopus 로고
    • Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains
    • Thompson A., Nessler R., Wisco D., Anderson E., Winckler B., and Sheff D. Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains. Mol. Biol. Cell 18 7 (2007) 2687-2697
    • (2007) Mol. Biol. Cell , vol.18 , Issue.7 , pp. 2687-2697
    • Thompson, A.1    Nessler, R.2    Wisco, D.3    Anderson, E.4    Winckler, B.5    Sheff, D.6
  • 215
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomsen P., Roepstorff K., Stahlhut M., and Van Deurs B. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol. Biol. Cell 13 1 (2002) 238-250
    • (2002) Mol. Biol. Cell , vol.13 , Issue.1 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    Van Deurs, B.4
  • 216
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen M.L., Skretting G., Van Deurs B., and Sandvig K. Internalization of cholera toxin by different endocytic mechanisms. J. Cell Sci. 114 20 (2001) 3737-3747
    • (2001) J. Cell Sci. , vol.114 , Issue.20 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    Van Deurs, B.3    Sandvig, K.4
  • 218
    • 14744304957 scopus 로고    scopus 로고
    • Phosphoregulation of Arp2/3-dependent actin assembly during receptor-mediated endocytosis
    • Toshima J., Toshima J.Y., Martin A.C., and Drubin D.G. Phosphoregulation of Arp2/3-dependent actin assembly during receptor-mediated endocytosis. Nat. Cell Biol. 7 3 (2005) 246-254
    • (2005) Nat. Cell Biol. , vol.7 , Issue.3 , pp. 246-254
    • Toshima, J.1    Toshima, J.Y.2    Martin, A.C.3    Drubin, D.G.4
  • 219
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: Crossing cellular barriers
    • Tuma P.L., and Hubbard A.L. Transcytosis: Crossing cellular barriers. Physiol. Rev. 83 3 (2003) 871-932
    • (2003) Physiol. Rev. , vol.83 , Issue.3 , pp. 871-932
    • Tuma, P.L.1    Hubbard, A.L.2
  • 220
    • 0035904227 scopus 로고    scopus 로고
    • Vps34p differentially regulates endocytosis from the apical and basolateral domains in polarized hepatic cells
    • Tuma P.L., Nyasae L.K., Backer J.M., and Hubbard A.L. Vps34p differentially regulates endocytosis from the apical and basolateral domains in polarized hepatic cells. J. Cell Biol. 154 6 (2001) 1197-1208
    • (2001) J. Cell Biol. , vol.154 , Issue.6 , pp. 1197-1208
    • Tuma, P.L.1    Nyasae, L.K.2    Backer, J.M.3    Hubbard, A.L.4
  • 222
    • 26244457213 scopus 로고    scopus 로고
    • Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing
    • Ungermann C., and Langosch D. Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing. J. Cell Sci. 118 17 (2005) 3819-3828
    • (2005) J. Cell Sci. , vol.118 , Issue.17 , pp. 3819-3828
    • Ungermann, C.1    Langosch, D.2
  • 223
    • 4644308982 scopus 로고    scopus 로고
    • The H,K-ATPase beta subunit as a model to study the role of N-glycosylation in membrane trafficking and apical sorting
    • Vagin O., Turdikulova S., and Sachs G. The H,K-ATPase beta subunit as a model to study the role of N-glycosylation in membrane trafficking and apical sorting. J. Biol. Chem. 279 37 (2004) 39026-39034
    • (2004) J. Biol. Chem. , vol.279 , Issue.37 , pp. 39026-39034
    • Vagin, O.1    Turdikulova, S.2    Sachs, G.3
  • 224
    • 33748963740 scopus 로고    scopus 로고
    • Intra-endosomal membrane traffic
    • van der Goot F.G., and Gruenberg J. Intra-endosomal membrane traffic. Trends Cell Biol. 16 10 (2006) 514-521
    • (2006) Trends Cell Biol. , vol.16 , Issue.10 , pp. 514-521
    • van der Goot, F.G.1    Gruenberg, J.2
  • 225
    • 0029058691 scopus 로고
    • The oligosaccharides have an essential but indirect role in sorting gp80 (clusterin, trpm-2) to the apical surface of MDCK cells
    • Wagner M., Morgans C., and Kochbrandt C. The oligosaccharides have an essential but indirect role in sorting gp80 (clusterin, trpm-2) to the apical surface of MDCK cells. Eur. J. Cell Biol. 67 1 (1995) 84-88
    • (1995) Eur. J. Cell Biol. , vol.67 , Issue.1 , pp. 84-88
    • Wagner, M.1    Morgans, C.2    Kochbrandt, C.3
  • 226
    • 0034252821 scopus 로고    scopus 로고
    • Membrane tethering and fusion in the secretory and endocytic pathways
    • Waters M.G., and Hughson F.M. Membrane tethering and fusion in the secretory and endocytic pathways. Traffic 1 8 (2000) 588-597
    • (2000) Traffic , vol.1 , Issue.8 , pp. 588-597
    • Waters, M.G.1    Hughson, F.M.2
  • 227
    • 34548288267 scopus 로고    scopus 로고
    • Toxin entry and trafficking in mammalian cells
    • Watson P., and Spooner R.A. Toxin entry and trafficking in mammalian cells. Adv. Drug Deliv. Rev. 58 15 (2006) 1581-1596
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , Issue.15 , pp. 1581-1596
    • Watson, P.1    Spooner, R.A.2
  • 229
    • 0033840979 scopus 로고    scopus 로고
    • EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts
    • Wilson J.M., De Hoop M., Zorzi N., Toh B., Dotti C.G., and Parton R.G. EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts. Mol. Biol. Cell 11 8 (2000) 2657-2671
    • (2000) Mol. Biol. Cell , vol.11 , Issue.8 , pp. 2657-2671
    • Wilson, J.M.1    De Hoop, M.2    Zorzi, N.3    Toh, B.4    Dotti, C.G.5    Parton, R.G.6
  • 230
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis
    • Wolfe B.L., and Trejo J. Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis. Traffic 8 5 (2007) 462-470
    • (2007) Traffic , vol.8 , Issue.5 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 233
    • 0012480985 scopus 로고    scopus 로고
    • Cell biology of acid secretion by the parietal cell
    • Yao X.B., and Forte J.G. Cell biology of acid secretion by the parietal cell. Annu. Rev. Physiol. 65 (2003) 103-131
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 103-131
    • Yao, X.B.1    Forte, J.G.2
  • 234
    • 0032956497 scopus 로고    scopus 로고
    • New perspectives on mechanisms involved in generating epithelial cell polarity
    • Yeaman C., Grindstaff K.K., and Nelson W.J. New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol. Rev. 79 1 (1999) 73-98
    • (1999) Physiol. Rev. , vol.79 , Issue.1 , pp. 73-98
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 235
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman C., LeGall A.H., Baldwin A.N., Monlauzeur L., LeBivic A., and Rodriguez-Boulan E. The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J. Cell Biol. 139 4 (1997) 929-940
    • (1997) J. Cell Biol. , vol.139 , Issue.4 , pp. 929-940
    • Yeaman, C.1    LeGall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    LeBivic, A.5    Rodriguez-Boulan, E.6
  • 236
    • 0037040897 scopus 로고    scopus 로고
    • + exchanger isoform 3 revisited-The roles of SGX1 and NHERF2
    • + exchanger isoform 3 revisited-The roles of SGX1 and NHERF2. J. Biol. Chem. 277 10 (2002) 7676-7683
    • (2002) J. Biol. Chem. , vol.277 , Issue.10 , pp. 7676-7683
    • Yun, C.C.1    Chen, Y.P.2    Lang, F.3
  • 237
    • 33751204464 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates the assembly of epithelial tight junctions
    • Zhang L., Li J., Young L.H., and Caplan M.J. AMP-activated protein kinase regulates the assembly of epithelial tight junctions. Proc. Natl. Acad. Sci. USA 103 46 (2006) 17272-17277
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.46 , pp. 17272-17277
    • Zhang, L.1    Li, J.2    Young, L.H.3    Caplan, M.J.4
  • 238
    • 33846521353 scopus 로고    scopus 로고
    • Regulation of epithelial tight junction assembly and disassembly by AMP-activated protein kinase
    • Zheng B., and Cantley L.C. Regulation of epithelial tight junction assembly and disassembly by AMP-activated protein kinase. Proc. Natl. Acad. Sci. USA 104 3 (2007) 819-822
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.3 , pp. 819-822
    • Zheng, B.1    Cantley, L.C.2
  • 239
    • 33748313081 scopus 로고    scopus 로고
    • The prevalence and significance of PDZ domain-phosphoinositide interactions
    • Zimmermann P. The prevalence and significance of PDZ domain-phosphoinositide interactions. Biochim. Biophys. Acta - Mol. Cell Biol. Lipids 1761 8 (2006) 947-956
    • (2006) Biochim. Biophys. Acta - Mol. Cell Biol. Lipids , vol.1761 , Issue.8 , pp. 947-956
    • Zimmermann, P.1


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