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Volumn 11, Issue 1, 2010, Pages 70-89

P28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon formation

Author keywords

Acetylated tubulin; ER Golgi intermediate compartment (ERGIC); Golgi fragmentation; Membrane traffic; Organelle maintenance; P24 proteins

Indexed keywords

BREFELDIN A; COAT PROTEIN COMPLEX I; GAG PROTEIN; PROTEIN P28; SMALL INTERFERING RNA; TUBULIN;

EID: 71849093794     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.01009.x     Document Type: Article
Times cited : (22)

References (80)
  • 3
    • 0037455546 scopus 로고    scopus 로고
    • The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation
    • Diao A, Rahman D, Pappin DJ, Lucocq J, Lowe M. The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J Cell Biol 2003, 160:201-212.
    • (2003) J Cell Biol , vol.160 , pp. 201-212
    • Diao, A.1    Rahman, D.2    Pappin, D.J.3    Lucocq, J.4    Lowe, M.5
  • 4
    • 0028796834 scopus 로고
    • Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes
    • Barroso M, Nelson DS, Sztul E. Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes. Proc Natl Acad Sci USA 1995, 92:527-531.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 527-531
    • Barroso, M.1    Nelson, D.S.2    Sztul, E.3
  • 5
    • 0842277809 scopus 로고    scopus 로고
    • Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis
    • Puthenveedu MA, Linstedt AD. Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis. Proc Natl Acad Sci USA 2004, 101:1253-1256.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1253-1256
    • Puthenveedu, M.A.1    Linstedt, A.D.2
  • 6
    • 33644756640 scopus 로고    scopus 로고
    • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution
    • Puthenveedu MA, Bachert C, Puri S, Lanni F, Linstedt AD. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat Cell Biol 2006, 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
  • 9
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog C, Hauri HP. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci 2006, 119:2173-2183.
    • (2006) J Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 10
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS, Glick BS. The mechanisms of vesicle budding and fusion. Cell 2004, 116:153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 11
  • 12
    • 0027220591 scopus 로고
    • Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok R, Scheel J, Horstmann H, Hauri HP, Griffiths G, Kreis TE. Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 1993, 74:71-82.
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 13
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
    • Teasdale RD, Jackson MR. Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu Rev Cell Dev Biol 1996, 12:27-54.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 15
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz J, Donaldson JG, Schweizer A, Berger EG, Hauri HP, Yuan LC, Klausner RD. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 1990, 60:821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 16
    • 0345306582 scopus 로고    scopus 로고
    • Capacity of the golgi apparatus for biogenesis from the endoplasmic reticulum
    • Puri S, Linstedt AD. Capacity of the golgi apparatus for biogenesis from the endoplasmic reticulum. Mol Biol Cell 2003, 14:5011-5018.
    • (2003) Mol Biol Cell , vol.14 , pp. 5011-5018
    • Puri, S.1    Linstedt, A.D.2
  • 18
    • 4344702375 scopus 로고    scopus 로고
    • Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase hela cells
    • Kasap M, Thomas S, Danaher E, Holton V, Jiang S, Storrie B. Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase hela cells. Traffic 2004, 5:595-605.
    • (2004) Traffic , vol.5 , pp. 595-605
    • Kasap, M.1    Thomas, S.2    Danaher, E.3    Holton, V.4    Jiang, S.5    Storrie, B.6
  • 19
    • 70149084008 scopus 로고    scopus 로고
    • The p24 family and selective transport processes at the ER-Golgi interface
    • Strating JR, Martens GJ. The p24 family and selective transport processes at the ER-Golgi interface. Biol Cell 2009, 101:495-509.
    • (2009) Biol Cell , vol.101 , pp. 495-509
    • Strating, J.R.1    Martens, G.J.2
  • 20
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muniz M, Nuoffer C, Hauri HP, Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol 2000, 148:925-930.
    • (2000) J Cell Biol , vol.148 , pp. 925-930
    • Muniz, M.1    Nuoffer, C.2    Hauri, H.P.3    Riezman, H.4
  • 21
    • 35648992037 scopus 로고    scopus 로고
    • P24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor trafficking
    • Luo W, Wang Y, Reiser G. p24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor trafficking. J Biol Chem 2007, 282:30246-30255.
    • (2007) J Biol Chem , vol.282 , pp. 30246-30255
    • Luo, W.1    Wang, Y.2    Reiser, G.3
  • 22
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller F, Singer-Kruger B, Schroder S, Kruger U, Barlowe C, Riezman H. The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J 1995, 14:1329-1339.
    • (1995) EMBO J , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 24
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler K, Veit M, Stamnes MA, Rothman JE. Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 1996, 273:1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 27
    • 0032578522 scopus 로고    scopus 로고
    • A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer
    • Harter C, Wieland FT. A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer. Proc Natl Acad Sci USA 1998, 95:11649-11654.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11649-11654
    • Harter, C.1    Wieland, F.T.2
  • 28
    • 0034677633 scopus 로고    scopus 로고
    • Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex
    • Goldberg J. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell 2000, 100:671-679.
    • (2000) Cell , vol.100 , pp. 671-679
    • Goldberg, J.1
  • 29
    • 0033895196 scopus 로고    scopus 로고
    • Coupled transport of p24 family members
    • Emery G, Rojo M, Gruenberg J. Coupled transport of p24 family members. J Cell Sci 2000, 113:2507-2516.
    • (2000) J Cell Sci , vol.113 , pp. 2507-2516
    • Emery, G.1    Rojo, M.2    Gruenberg, J.3
  • 30
    • 33750344792 scopus 로고    scopus 로고
    • Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins
    • Bethune J, Kol M, Hoffmann J, Reckmann I, Brugger B, Wieland F. Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins. Mol Cell Biol 2006, 26:8011-8021.
    • (2006) Mol Cell Biol , vol.26 , pp. 8011-8021
    • Bethune, J.1    Kol, M.2    Hoffmann, J.3    Reckmann, I.4    Brugger, B.5    Wieland, F.6
  • 32
    • 48249131211 scopus 로고    scopus 로고
    • The Cargo receptors Surf4, ERGIC-53 and p25 are required to maintain the architecture of ERGIC and Golgi
    • Mitrovic S, Ben-Tekaya H, Koegler E, Gruenberg J, Hauri HP. The Cargo receptors Surf4, ERGIC-53 and p25 are required to maintain the architecture of ERGIC and Golgi. Mol Biol Cell 2008, 19:1976-1990.
    • (2008) Mol Biol Cell , vol.19 , pp. 1976-1990
    • Mitrovic, S.1    Ben-Tekaya, H.2    Koegler, E.3    Gruenberg, J.4    Hauri, H.P.5
  • 33
    • 0347382331 scopus 로고    scopus 로고
    • The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics
    • Emery G, Parton RG, Rojo M, Gruenberg J. The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics. J Cell Sci 2003, 116:4821-4832.
    • (2003) J Cell Sci , vol.116 , pp. 4821-4832
    • Emery, G.1    Parton, R.G.2    Rojo, M.3    Gruenberg, J.4
  • 34
    • 0034708445 scopus 로고    scopus 로고
    • Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway
    • Ciufo LF, Boyd A. Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway. J Biol Chem 2000, 275:8382-8388.
    • (2000) J Biol Chem , vol.275 , pp. 8382-8388
    • Ciufo, L.F.1    Boyd, A.2
  • 35
    • 0036047057 scopus 로고    scopus 로고
    • The GOLD domain, a novel protein module involved in Golgi function and secretion
    • Anantharaman V, Aravind L. The GOLD domain, a novel protein module involved in Golgi function and secretion. Genome Biol 2002, 3:research0023.
    • (2002) Genome Biol , vol.3
    • Anantharaman, V.1    Aravind, L.2
  • 36
    • 0037195867 scopus 로고    scopus 로고
    • Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway
    • Jenne N, Frey K, Brugger B, Wieland FT. Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway. J Biol Chem 2002, 277:46504-46511.
    • (2002) J Biol Chem , vol.277 , pp. 46504-46511
    • Jenne, N.1    Frey, K.2    Brugger, B.3    Wieland, F.T.4
  • 37
    • 8744259809 scopus 로고    scopus 로고
    • Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46
    • Breuza L, Halbeisen R, Jeno P, Otte S, Barlowe C, Hong W, Hauri HP. Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J Biol Chem 2004, 279:47242-47253.
    • (2004) J Biol Chem , vol.279 , pp. 47242-47253
    • Breuza, L.1    Halbeisen, R.2    Jeno, P.3    Otte, S.4    Barlowe, C.5    Hong, W.6    Hauri, H.P.7
  • 38
    • 0034029917 scopus 로고    scopus 로고
    • Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics
    • Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W. Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res 2000, 10:703-713.
    • (2000) Genome Res , vol.10 , pp. 703-713
    • Lai, C.H.1    Chou, C.Y.2    Ch'ang, L.Y.3    Liu, C.S.4    Lin, W.5
  • 40
    • 0039517273 scopus 로고    scopus 로고
    • Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members
    • Fullekrug J, Suganuma T, Tang BL, Hong W, Storrie B, Nilsson T. Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members. Mol Biol Cell 1999, 10:1939-1955.
    • (1999) Mol Biol Cell , vol.10 , pp. 1939-1955
    • Fullekrug, J.1    Suganuma, T.2    Tang, B.L.3    Hong, W.4    Storrie, B.5    Nilsson, T.6
  • 41
    • 0032971476 scopus 로고    scopus 로고
    • P24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway
    • Gommel D, Orci L, Emig EM, Hannah MJ, Ravazzola M, Nickel W, Helms JB, Wieland FT, Sohn K. p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway. FEBS Lett 1999, 447:179-185.
    • (1999) FEBS Lett , vol.447 , pp. 179-185
    • Gommel, D.1    Orci, L.2    Emig, E.M.3    Hannah, M.J.4    Ravazzola, M.5    Nickel, W.6    Helms, J.B.7    Wieland, F.T.8    Sohn, K.9
  • 42
    • 0034033881 scopus 로고    scopus 로고
    • The transmembrane protein p23 contributes to the organization of the Golgi apparatus
    • Rojo M, Emery G, Marjomaki V, McDowall AW, Parton RG, Gruenberg J. The transmembrane protein p23 contributes to the organization of the Golgi apparatus. J Cell Sci 2000, 113:1043-1057.
    • (2000) J Cell Sci , vol.113 , pp. 1043-1057
    • Rojo, M.1    Emery, G.2    Marjomaki, V.3    McDowall, A.W.4    Parton, R.G.5    Gruenberg, J.6
  • 45
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • Watson P, Townley AK, Koka P, Palmer KJ, Stephens DJ. Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 2006, 7:1678-1687.
    • (2006) Traffic , vol.7 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 46
    • 33947099546 scopus 로고    scopus 로고
    • Replication foci dynamics: replication patterns are modulated by S-phase checkpoint kinases in fission yeast
    • Meister P, Taddei A, Ponti A, Baldacci G, Gasser SM. Replication foci dynamics: replication patterns are modulated by S-phase checkpoint kinases in fission yeast. EMBO J 2007, 26:1315-1326.
    • (2007) EMBO J , vol.26 , pp. 1315-1326
    • Meister, P.1    Taddei, A.2    Ponti, A.3    Baldacci, G.4    Gasser, S.M.5
  • 48
    • 0035842897 scopus 로고    scopus 로고
    • Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus
    • Barr FA, Preisinger C, Kopajtich R, Korner R. Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J Cell Biol 2001, 155:885-891.
    • (2001) J Cell Biol , vol.155 , pp. 885-891
    • Barr, F.A.1    Preisinger, C.2    Kopajtich, R.3    Korner, R.4
  • 50
    • 0030868332 scopus 로고    scopus 로고
    • P23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway
    • Nickel W, Sohn K, Bunning C, Wieland FT. p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway. Proc Natl Acad Sci USA 1997, 94:11393-11398.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11393-11398
    • Nickel, W.1    Sohn, K.2    Bunning, C.3    Wieland, F.T.4
  • 51
    • 33750932783 scopus 로고    scopus 로고
    • A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex
    • Stauber T, Simpson JC, Pepperkok R, Vernos I. A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex. Curr Biol 2006, 16:2245-2251.
    • (2006) Curr Biol , vol.16 , pp. 2245-2251
    • Stauber, T.1    Simpson, J.C.2    Pepperkok, R.3    Vernos, I.4
  • 52
    • 47249163819 scopus 로고    scopus 로고
    • Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1
    • Styers ML, O'Connor AK, Grabski R, Cormet-Boyaka E, Sztul E. Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1. Am J Physiol Cell Physiol 2008, 294:C1485-C1498.
    • (2008) Am J Physiol Cell Physiol , vol.294
    • Styers, M.L.1    O'Connor, A.K.2    Grabski, R.3    Cormet-Boyaka, E.4    Sztul, E.5
  • 54
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J 1990, 9:3153-3162.
    • (1990) EMBO J , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 55
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson P, Letourneur F. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 1994, 263:1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 56
    • 40849088168 scopus 로고    scopus 로고
    • The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus
    • Aguilera-Romero A, Kaminska J, Spang A, Riezman H, Muniz M. The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus. J Cell Biol 2008, 180:713-720.
    • (2008) J Cell Biol , vol.180 , pp. 713-720
    • Aguilera-Romero, A.1    Kaminska, J.2    Spang, A.3    Riezman, H.4    Muniz, M.5
  • 59
    • 0033549551 scopus 로고    scopus 로고
    • A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system
    • Shorter J, Warren G. A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. J Cell Biol 1999, 146:57-70.
    • (1999) J Cell Biol , vol.146 , pp. 57-70
    • Shorter, J.1    Warren, G.2
  • 60
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, Barr FA. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J 1999, 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
  • 61
    • 0037926394 scopus 로고    scopus 로고
    • A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
    • Wang Y, Seemann J, Pypaert M, Shorter J, Warren G. A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J 2003, 22:3279-3290.
    • (2003) EMBO J , vol.22 , pp. 3279-3290
    • Wang, Y.1    Seemann, J.2    Pypaert, M.3    Shorter, J.4    Warren, G.5
  • 63
    • 51349095514 scopus 로고    scopus 로고
    • GRASP55 regulates Golgi ribbon formation
    • Feinstein TN, Linstedt AD. GRASP55 regulates Golgi ribbon formation. Mol Biol Cell 2008, 19:2696-2707.
    • (2008) Mol Biol Cell , vol.19 , pp. 2696-2707
    • Feinstein, T.N.1    Linstedt, A.D.2
  • 64
    • 39449124362 scopus 로고    scopus 로고
    • The Golgi protein GM130 regulates centrosome morphology and function
    • Kodani A, Sutterlin C. The Golgi protein GM130 regulates centrosome morphology and function. Mol Biol Cell 2008, 19:745-753.
    • (2008) Mol Biol Cell , vol.19 , pp. 745-753
    • Kodani, A.1    Sutterlin, C.2
  • 65
    • 21844468961 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division
    • Sutterlin C, Polishchuk R, Pecot M, Malhotra V. The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division. Mol Biol Cell 2005, 16:3211-3222.
    • (2005) Mol Biol Cell , vol.16 , pp. 3211-3222
    • Sutterlin, C.1    Polishchuk, R.2    Pecot, M.3    Malhotra, V.4
  • 66
    • 45749158566 scopus 로고    scopus 로고
    • Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport
    • Wang Y, Wei JH, Bisel B, Tang D, Seemann J. Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport. PLoS ONE 2008, 3:e1647.
    • (2008) PLoS ONE , vol.3
    • Wang, Y.1    Wei, J.H.2    Bisel, B.3    Tang, D.4    Seemann, J.5
  • 68
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R, Ursell T, Wiggins P, Sens P. Emerging roles for lipids in shaping membrane-protein function. Nature 2009, 459:379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 69
    • 71849095898 scopus 로고    scopus 로고
    • Role of p24 protein in individual lipid sorting within the early secretory pathway
    • Contreras F-X. Role of p24 protein in individual lipid sorting within the early secretory pathway. Eur J Cell Biol 2009, 88:12-13.
    • (2009) Eur J Cell Biol , vol.88 , pp. 12-13
    • Contreras, F.-.X.1
  • 70
    • 69949178740 scopus 로고    scopus 로고
    • Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells
    • Miller PM, Folkmann AW, Maia AR, Efimova N, Efimov A, Kaverina I. Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells. Nat Cell Biol 2009, 11:1069-1080.
    • (2009) Nat Cell Biol , vol.11 , pp. 1069-1080
    • Miller, P.M.1    Folkmann, A.W.2    Maia, A.R.3    Efimova, N.4    Efimov, A.5    Kaverina, I.6
  • 71
    • 39149121834 scopus 로고    scopus 로고
    • Tubulin modifications and their cellular functions
    • Hammond JW, Cai D, Verhey KJ. Tubulin modifications and their cellular functions. Curr Opin Cell Biol 2008, 20:71-76.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 71-76
    • Hammond, J.W.1    Cai, D.2    Verhey, K.J.3
  • 72
    • 67349287493 scopus 로고    scopus 로고
    • Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130
    • Rivero S, Cardenas J, Bornens M, Rios RM. Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130. EMBO J 2009, 28:1016-1028.
    • (2009) EMBO J , vol.28 , pp. 1016-1028
    • Rivero, S.1    Cardenas, J.2    Bornens, M.3    Rios, R.M.4
  • 73
    • 65249115901 scopus 로고    scopus 로고
    • A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing
    • Yadav S, Puri S, Linstedt AD. A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing. Mol Biol Cell 2009, 20:1728-1736.
    • (2009) Mol Biol Cell , vol.20 , pp. 1728-1736
    • Yadav, S.1    Puri, S.2    Linstedt, A.D.3
  • 74
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer A, Fransen JA, Bachi T, Ginsel L, Hauri HP. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J Cell Biol 1988, 107:1643-1653.
    • (1988) J Cell Biol , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 75
  • 76
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt AD, Hauri HP. Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol Biol Cell 1993, 4:679-693.
    • (1993) Mol Biol Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.P.2
  • 77
    • 0030921043 scopus 로고    scopus 로고
    • Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein
    • Linstedt AD, Mehta A, Suhan J, Reggio H, Hauri HP. Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein. Mol Biol Cell 1997, 8:1073-1087.
    • (1997) Mol Biol Cell , vol.8 , pp. 1073-1087
    • Linstedt, A.D.1    Mehta, A.2    Suhan, J.3    Reggio, H.4    Hauri, H.P.5
  • 78
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 2003, 31:3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 79
    • 0001420820 scopus 로고
    • A modified procedure for lead staining of thin sections
    • Millonig G. A modified procedure for lead staining of thin sections. J Biophys Biochem Cytol 1961, 11:736-739.
    • (1961) J Biophys Biochem Cytol , vol.11 , pp. 736-739
    • Millonig, G.1
  • 80
    • 34547760398 scopus 로고    scopus 로고
    • Improved maturation of CFTR by an ER export signal
    • Wendeler MW, Nufer O, Hauri HP. Improved maturation of CFTR by an ER export signal. FASEB J 2007, 21:2352-2358.
    • (2007) FASEB J , vol.21 , pp. 2352-2358
    • Wendeler, M.W.1    Nufer, O.2    Hauri, H.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.