메뉴 건너뛰기




Volumn 11, Issue 3, 2010, Pages 303-310

New insights into the structural mechanisms of the COPII coat

Author keywords

Coated vesicle; COPII; Sar1; Sec13 31; Sec23 24; Secretory pathway; Structure

Indexed keywords

CHYLOMICRON; CLATHRIN; COAT PROTEIN; COAT PROTEIN COMPLEX II; COLLAGEN; PROCOLLAGEN; SNARE PROTEIN; SYNTAXIN;

EID: 77949532806     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.01026.x     Document Type: Article
Times cited : (58)

References (43)
  • 1
    • 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
  • 3
    • 33747386160 scopus 로고    scopus 로고
    • An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+
    • Rao Y, Bian C, Yuan C, Li Y, Chen L, Ye X. An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+. Biochem Biophys Res Commun 2006, 348:908-915.
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 908-915
    • Rao, Y.1    Bian, C.2    Yuan, C.3    Li, Y.4    Chen, L.5    Ye, X.6
  • 4
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • Bi X, Corpina RA, 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
  • 5
    • 0035842886 scopus 로고    scopus 로고
    • Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export.
    • Huang M, Weissman JT, Beraud-Dufour S, Luan P, Wang C, Chen W. Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export. J Cell Biol 2001, 155:937-948.
    • (2001) J Cell Biol , vol.155 , pp. 937-948
    • Huang, M.1    Weissman, J.T.2    Beraud-Dufour, S.3    Luan, P.4    Wang, C.5    Chen, W.6
  • 6
    • 0034946168 scopus 로고    scopus 로고
    • The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export
    • Weissman JT, Plutner H, Balch WE. The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export. Traffic 2001, 2:465-475.
    • (2001) Traffic , vol.2 , pp. 465-475
    • Weissman, J.T.1    Plutner, H.2    Balch, W.E.3
  • 7
    • 0030891289 scopus 로고    scopus 로고
    • N-Terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • Antonny B, Beraud-Dufour S, Chardin P, Chabre M. N-Terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 1997, 36:4675-4684.
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 8
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 1998, 95:237-248.
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 9
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication
    • Pasqualato S, Renault L, Cherfils J. Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep 2002, 3:1035-1041.
    • (2002) EMBO Rep , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 10
    • 23944488301 scopus 로고    scopus 로고
    • Sar1P N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • Lee MC, Orci L, Hamamoto S, Futai E, Ravazzola M, Schekman R. Sar1P N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 2005, 122:605-617.
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 12
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • Bielli A, Haney CJ, Gabreski G, Watkins SC, Bannykh SI, Aridor M. Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J Cell Biol 2005, 171:919-924.
    • (2005) J Cell Biol , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 13
    • 34548411897 scopus 로고    scopus 로고
    • Molecular mechanisms of COPII vesicle formation
    • Lee MC, Miller EA. Molecular mechanisms of COPII vesicle formation. Semin Cell Dev Biol 2007, 18:424-434.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 424-434
    • Lee, M.C.1    Miller, E.A.2
  • 15
    • 69949183624 scopus 로고    scopus 로고
    • Conserved functions of membrane active GTPases in coated vesicle formation
    • Pucadyil TJ, Schmid SL. Conserved functions of membrane active GTPases in coated vesicle formation. Science 2009, 325:1217-1220.
    • (2009) Science , vol.325 , pp. 1217-1220
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 16
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • Yoshihisa T, Barlowe C, Schekman R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 1993, 259:1466-1468.
    • (1993) Science , vol.259 , pp. 1466-1468
    • Yoshihisa, T.1    Barlowe, C.2    Schekman, R.3
  • 17
    • 33749128067 scopus 로고    scopus 로고
    • Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-golgi trafficking
    • Boyadjiev SA, Fromme JC, Ben J, Chong SS, Nauta C, Hur DJ. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-golgi trafficking. Nat Genet 2006, 38:1192-1197.
    • (2006) Nat Genet , vol.38 , pp. 1192-1197
    • Boyadjiev, S.A.1    Fromme, J.C.2    Ben, J.3    Chong, S.S.4    Nauta, C.5    Hur, D.J.6
  • 18
    • 68149162593 scopus 로고    scopus 로고
    • Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II
    • Schwarz K, Iolascon A, Verissimo F, Trede NS, Horsley W, Chen W. Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II. Nat Genet 2009, 41:936-940.
    • (2009) Nat Genet , vol.41 , pp. 936-940
    • Schwarz, K.1    Iolascon, A.2    Verissimo, F.3    Trede, N.S.4    Horsley, W.5    Chen, W.6
  • 20
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka K, Orci L, Amherdt M, Bednarek SY, Hamamoto S, Schekman R, Yeung T. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 1998, 93:263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 23
    • 35549004893 scopus 로고    scopus 로고
    • Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31.
    • Bi X, Mancias JD, Goldberg J. Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Dev Cell 2007, 13:635-645.
    • (2007) Dev Cell , vol.13 , pp. 635-645
    • Bi, X.1    Mancias, J.D.2    Goldberg, J.3
  • 24
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova E, Bickford LC, Goldberg J. SNARE selectivity of the COPII coat. Cell 2003, 114:483-495.
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 25
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, Orci L, Schekman R. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 2003, 114:497-509.
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 26
  • 27
    • 55549137036 scopus 로고    scopus 로고
    • Structural basis of cargo membrane protein discrimination by the human COPII coat machinery
    • Mancias JD, Goldberg J. Structural basis of cargo membrane protein discrimination by the human COPII coat machinery. EMBO J 2008, 27:2918-2928.
    • (2008) EMBO J , vol.27 , pp. 2918-2928
    • Mancias, J.D.1    Goldberg, J.2
  • 28
    • 34247579058 scopus 로고    scopus 로고
    • The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope
    • Mancias JD, Goldberg J. The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol Cell 2007, 26:403-414.
    • (2007) Mol Cell , vol.26 , pp. 403-414
    • Mancias, J.D.1    Goldberg, J.2
  • 29
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • Fath S, Mancias JD, 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
  • 31
    • 0027454503 scopus 로고
    • The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins
    • Salama NR, Yeung T, Schekman RW. The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO J 1993, 12:4073-4082.
    • (1993) EMBO J , vol.12 , pp. 4073-4082
    • Salama, N.R.1    Yeung, T.2    Schekman, R.W.3
  • 33
    • 34147129193 scopus 로고    scopus 로고
    • Structural design of cage and coat scaffolds that direct membrane traffic
    • Stagg SM, Lapointe P, Balch WE. 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
  • 34
    • 15544367075 scopus 로고    scopus 로고
    • Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis
    • Sato K, Nakano A. Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat Struct Mol Biol 2005, 12:167-174.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 167-174
    • Sato, K.1    Nakano, A.2
  • 35
    • 70350763840 scopus 로고    scopus 로고
    • Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane.
    • Tabata KV, Sato K, Ide T, Nishizaka T, Nakano A, Noji H. Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane. EMBO J 2009, 28:3279-289.
    • (2009) EMBO J , vol.28 , pp. 3279-3289
    • Tabata, K.V.1    Sato, K.2    Ide, T.3    Nishizaka, T.4    Nakano, A.5    Noji, H.6
  • 36
    • 0020444307 scopus 로고
    • Structural implications from an electronmicroscopic comparison of procollagen V with procollagen I, pC-collagen I, procollagen IV, and a Drosophila procollagen
    • Bachinger HP, Doege KJ, Petschek JP, Fessler LI, Fessler JH. Structural implications from an electronmicroscopic comparison of procollagen V with procollagen I, pC-collagen I, procollagen IV, and a Drosophila procollagen. J Biol Chem 1982, 257:14590-14592.
    • (1982) J Biol Chem , vol.257 , pp. 14590-14592
    • Bachinger, H.P.1    Doege, K.J.2    Petschek, J.P.3    Fessler, L.I.4    Fessler, J.H.5
  • 37
    • 0037439881 scopus 로고    scopus 로고
    • COPII proteins are required for golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle
    • Siddiqi SA, Gorelick FS, Mahan JT, Mansbach CM. COPII proteins are required for golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle. J Cell Sci 2003, 116:415-427.
    • (2003) J Cell Sci , vol.116 , pp. 415-427
    • Siddiqi, S.A.1    Gorelick, F.S.2    Mahan, J.T.3    Mansbach, C.M.4
  • 38
    • 22044441866 scopus 로고    scopus 로고
    • COPII-coated vesicles: flexible enough for large cargo?
    • Fromme JC, Schekman R. COPII-coated vesicles: flexible enough for large cargo? Curr Opin Cell Biol 2005, 17:345-352.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 345-352
    • Fromme, J.C.1    Schekman, R.2
  • 40
    • 1842452932 scopus 로고    scopus 로고
    • The intracellular transport of chylomicrons requires the small GTPase, Sar1b
    • Shoulders CC, Stephens DJ, Jones B. The intracellular transport of chylomicrons requires the small GTPase, Sar1b. Curr Opin Lipidol 2004, 15:191-197.
    • (2004) Curr Opin Lipidol , vol.15 , pp. 191-197
    • Shoulders, C.C.1    Stephens, D.J.2    Jones, B.3
  • 41
    • 55049134801 scopus 로고    scopus 로고
    • Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development
    • Townley AK, Feng Y, Schmidt K, Carter DA, Porter R, Verkade P, Stephens DJ. Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development. J Cell Sci 2008, 121:3025-3034.
    • (2008) J Cell Sci , vol.121 , pp. 3025-3034
    • Townley, A.K.1    Feng, Y.2    Schmidt, K.3    Carter, D.A.4    Porter, R.5    Verkade, P.6    Stephens, D.J.7
  • 43
    • 61449242669 scopus 로고    scopus 로고
    • TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites
    • Saito K, Chen M, Bard F, Chen S, Zhou H, Woodley D. TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 2009, 136:891-902.
    • (2009) Cell , vol.136 , pp. 891-902
    • Saito, K.1    Chen, M.2    Bard, F.3    Chen, S.4    Zhou, H.5    Woodley, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.