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Volumn 22, Issue 4, 2010, Pages 454-460

Structure and mechanism in membrane trafficking

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; COAT PROTEIN COMPLEX II; PROTEIN DSL1; PROTEIN TRAPP; UNCLASSIFIED DRUG; VESICULAR TRANSPORT PROTEIN;

EID: 77955050491     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.03.011     Document Type: Review
Times cited : (32)

References (58)
  • 1
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino J.S., Glick B.S. 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
  • 2
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution
    • Sutton R.B., Fasshauer D., Jahn R., Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution. Nature 1998, 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 3
    • 33745737926 scopus 로고    scopus 로고
    • Membrane deformation by protein coats
    • Antonny B. Membrane deformation by protein coats. Curr Opin Cell Biol 2006, 18:386-394.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 386-394
    • Antonny, B.1
  • 4
    • 34147129193 scopus 로고    scopus 로고
    • Structural design of cage and coat scaffolds that direct membrane traffic
    • Stagg S.M., LaPointe P., Balch W.E. Structural design of cage and coat scaffolds that direct membrane traffic. Curr Opin Struct Biol 2007, 17:221-228.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 221-228
    • Stagg, S.M.1    LaPointe, P.2    Balch, W.E.3
  • 5
    • 77949532806 scopus 로고    scopus 로고
    • New insights into the structural mechanisms of the COPII coat
    • Russell C., Stagg S.M. New insights into the structural mechanisms of the COPII coat. Traffic 2010, 11:303-310.
    • (2010) Traffic , vol.11 , pp. 303-310
    • Russell, C.1    Stagg, S.M.2
  • 6
    • 67949124784 scopus 로고    scopus 로고
    • On vesicle formation and tethering in the ER-Golgi shuttle
    • Spang A. On vesicle formation and tethering in the ER-Golgi shuttle. Curr Opin Cell Biol 2009, 21:531-536.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 531-536
    • Spang, A.1
  • 11
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • Fath S., Mancias J.D., Bi X., Goldberg J. Structure and organization of coat proteins in the COPII cage. Cell 2007, 129:1325-1336.
    • (2007) Cell , vol.129 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 12
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • Bi X., Corpina R.A., Goldberg J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 2002, 419:271-277.
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 13
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: achieving specificity in membrane traffic
    • Grosshans B.L., Ortiz D., Novick P. Rabs and their effectors: achieving specificity in membrane traffic. Proc Natl Acad Sci U S A 2006, 103:11821-11827.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 14
    • 34247623568 scopus 로고    scopus 로고
    • Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle
    • Cai H., Reinisch K., Ferro-Novick S. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell 2007, 12:671-682.
    • (2007) Dev Cell , vol.12 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 16
    • 69949175597 scopus 로고    scopus 로고
    • A link between ER tethering and COP-I vesicle uncoating
    • Zink S., Wenzel D., Wurm C.A., Schmitt H.D. A link between ER tethering and COP-I vesicle uncoating. Dev Cell 2009, 17:403-416.
    • (2009) Dev Cell , vol.17 , pp. 403-416
    • Zink, S.1    Wenzel, D.2    Wurm, C.A.3    Schmitt, H.D.4
  • 18
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: membrane-molding macromolecules
    • Frost A., Unger V.M., De Camilli P. The BAR domain superfamily: membrane-molding macromolecules. Cell 2009, 137:191-196.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 21
  • 22
    • 33846817369 scopus 로고    scopus 로고
    • Structural basis for the actin-binding function of missing-in-metastasis
    • Lee S.H., Kerff F., Chereau D., Ferron F., Klug A., Dominguez R. Structural basis for the actin-binding function of missing-in-metastasis. Structure 2007, 15:145-155.
    • (2007) Structure , vol.15 , pp. 145-155
    • Lee, S.H.1    Kerff, F.2    Chereau, D.3    Ferron, F.4    Klug, A.5    Dominguez, R.6
  • 26
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • Hanson P.I., Roth R., Lin Y., Heuser J.E. Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J Cell Biol 2008, 180:389-402.
    • (2008) J Cell Biol , vol.180 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 30
    • 70450223107 scopus 로고    scopus 로고
    • Role of vesicle tethering factors in the ER-Golgi membrane traffic
    • Sztul E., Lupashin V. Role of vesicle tethering factors in the ER-Golgi membrane traffic. FEBS Lett 2009, 583:3770-3783.
    • (2009) FEBS Lett , vol.583 , pp. 3770-3783
    • Sztul, E.1    Lupashin, V.2
  • 31
    • 33847648364 scopus 로고    scopus 로고
    • Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins
    • Koumandou V.L., Dacks J.B., Coulson R.M., Field M.C. Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins. BMC Evol Biol 2007, 7:29.
    • (2007) BMC Evol Biol , vol.7 , pp. 29
    • Koumandou, V.L.1    Dacks, J.B.2    Coulson, R.M.3    Field, M.C.4
  • 32
    • 28544432477 scopus 로고    scopus 로고
    • The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
    • Dong G., Hutagalung A.H., Fu C., Novick P., Reinisch K.M. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol 2005, 12:1094-1100.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1094-1100
    • Dong, G.1    Hutagalung, A.H.2    Fu, C.3    Novick, P.4    Reinisch, K.M.5
  • 34
    • 33744933711 scopus 로고    scopus 로고
    • The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
    • Sivaram M.V., Furgason M.L., Brewer D.N., Munson M. The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Nat Struct Mol Biol 2006, 13:555-556.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 555-556
    • Sivaram, M.V.1    Furgason, M.L.2    Brewer, D.N.3    Munson, M.4
  • 35
    • 59649120867 scopus 로고    scopus 로고
    • Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
    • Tripathi A., Ren Y., Jeffrey P.D., Hughson F.M. Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. Nat Struct Mol Biol 2009, 16:114-123.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 114-123
    • Tripathi, A.1    Ren, Y.2    Jeffrey, P.D.3    Hughson, F.M.4
  • 37
    • 27144456598 scopus 로고    scopus 로고
    • Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
    • Wu S., Mehta S.Q., Pichaud F., Bellen H.J., Quiocho F.A. Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat Struct Mol Biol 2005, 12:879-885.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 879-885
    • Wu, S.1    Mehta, S.Q.2    Pichaud, F.3    Bellen, H.J.4    Quiocho, F.A.5
  • 38
    • 71149117138 scopus 로고    scopus 로고
    • A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
    • Ren Y., Yip C.K., Tripathi A., Huie D., Jeffrey P.D., Walz T., Hughson F.M. A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1. Cell 2009, 139:1119-1129.
    • (2009) Cell , vol.139 , pp. 1119-1129
    • Ren, Y.1    Yip, C.K.2    Tripathi, A.3    Huie, D.4    Jeffrey, P.D.5    Walz, T.6    Hughson, F.M.7
  • 39
    • 1842482412 scopus 로고    scopus 로고
    • Tip20p prohibits back-fusion of COPII vesicles with the endoplasmic reticulum
    • Kamena F., Spang A. Tip20p prohibits back-fusion of COPII vesicles with the endoplasmic reticulum. Science 2004, 304:286-289.
    • (2004) Science , vol.304 , pp. 286-289
    • Kamena, F.1    Spang, A.2
  • 40
    • 24344480456 scopus 로고    scopus 로고
    • Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
    • Kraynack B.A., Chan A., Rosenthal E., Essid M., Umansky B., Waters M.G., Schmitt H.D. Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol Biol Cell 2005, 16:3963-3977.
    • (2005) Mol Biol Cell , vol.16 , pp. 3963-3977
    • Kraynack, B.A.1    Chan, A.2    Rosenthal, E.3    Essid, M.4    Umansky, B.5    Waters, M.G.6    Schmitt, H.D.7
  • 41
    • 0035914416 scopus 로고    scopus 로고
    • The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast
    • Andag U., Neumann T., Schmitt H.D. The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J Biol Chem 2001, 276:39150-39160.
    • (2001) J Biol Chem , vol.276 , pp. 39150-39160
    • Andag, U.1    Neumann, T.2    Schmitt, H.D.3
  • 42
    • 0347695021 scopus 로고    scopus 로고
    • Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat
    • Andag U., Schmitt H.D. Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat. J Biol Chem 2003, 278:51722-51734.
    • (2003) J Biol Chem , vol.278 , pp. 51722-51734
    • Andag, U.1    Schmitt, H.D.2
  • 47
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on ypt1p
    • Wang W., Sacher M., Ferro-Novick S. TRAPP stimulates guanine nucleotide exchange on ypt1p. J Cell Biol 2000, 151:289-296.
    • (2000) J Cell Biol , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 48
    • 0037147148 scopus 로고    scopus 로고
    • Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda
    • Jang S.B., Kim Y.G., Cho Y.S., Suh P.G., Kim K.H., Oh B.H. Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda. J Biol Chem 2002, 277:49863-49869.
    • (2002) J Biol Chem , vol.277 , pp. 49863-49869
    • Jang, S.B.1    Kim, Y.G.2    Cho, Y.S.3    Suh, P.G.4    Kim, K.H.5    Oh, B.H.6
  • 49
  • 51
    • 26844574974 scopus 로고    scopus 로고
    • The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex
    • Kummel D., Muller J.J., Roske Y., Misselwitz R., Bussow K., Heinemann U. The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex. EMBO Rep 2005, 6:787-793.
    • (2005) EMBO Rep , vol.6 , pp. 787-793
    • Kummel, D.1    Muller, J.J.2    Roske, Y.3    Misselwitz, R.4    Bussow, K.5    Heinemann, U.6
  • 56
    • 44449097226 scopus 로고    scopus 로고
    • Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex
    • Im Y.J., Hurley J.H. Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. Dev Cell 2008, 14:902-913.
    • (2008) Dev Cell , vol.14 , pp. 902-913
    • Im, Y.J.1    Hurley, J.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.