| Structural highlights
2qtv is a 3 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Gene: | SEC23 (ATCC 18824), SAR1 (ATCC 18824), SEC31, WEB1 (ATCC 18824) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SEC23_YEAST] Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [SEC31_YEAST] Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.[23] [24] [25] [26] [27] [28] [SAR1_YEAST] Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP by SEC12 binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits.[29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [40] [41] [42]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The COPII vesicular coat forms on the endoplasmic reticulum from Sar1-GTP, Sec23/24 and Sec13/31 protein subunits. Here, we define the interaction between Sec23/24.Sar1 and Sec13/31, involving a 40 residue Sec31 fragment. In the crystal structure of the ternary complex, Sec31 binds as an extended polypeptide across a composite surface of the Sec23 and Sar1-GTP molecules, explaining the stepwise character of Sec23/24.Sar1 and Sec13/31 recruitment to the membrane. The Sec31 fragment stimulates GAP activity of Sec23/24, and a convergence of Sec31 and Sec23 residues at the Sar1 GTPase active site explains how GTP hydrolysis is triggered leading to COPII coat disassembly. The Sec31 active fragment is accommodated in a binding groove supported in part by Sec23 residue Phe380. Substitution of the corresponding residue F382L in human Sec23A causes cranio-lenticulo-sutural dysplasia, and we suggest that this mutation disrupts the nucleation of COPII coat proteins at endoplasmic reticulum exit sites.
Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31.,Bi X, Mancias JD, Goldberg J Dev Cell. 2007 Nov;13(5):635-45. PMID:17981133[43]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hicke L, Schekman R. Yeast Sec23p acts in the cytoplasm to promote protein transport from the endoplasmic reticulum to the Golgi complex in vivo and in vitro. EMBO J. 1989 Jun;8(6):1677-84. PMID:2670558
- ↑ Novick P, Field C, Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 1980 Aug;21(1):205-15. PMID:6996832
- ↑ Novick P, Ferro S, Schekman R. Order of events in the yeast secretory pathway. Cell. 1981 Aug;25(2):461-9. PMID:7026045
- ↑ Baker D, Hicke L, Rexach M, Schleyer M, Schekman R. Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell. 1988 Jul 29;54(3):335-44. PMID:3293799
- ↑ Ruohola H, Kabcenell AK, Ferro-Novick S. Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant. J Cell Biol. 1988 Oct;107(4):1465-76. PMID:3049622
- ↑ Kaiser CA, Schekman R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell. 1990 May 18;61(4):723-33. PMID:2188733
- ↑ Hicke L, Yoshihisa T, Schekman R. Sec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum. Mol Biol Cell. 1992 Jun;3(6):667-76. PMID:1498369
- ↑ Liang S, Lacroute F, Kepes F. Multicopy STS1 restores both protein transport and ribosomal RNA stability in a new yeast sec23 mutant allele. Eur J Cell Biol. 1993 Dec;62(2):270-81. PMID:7925484
- ↑ Yoshihisa T, Barlowe C, Schekman R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science. 1993 Mar 5;259(5100):1466-8. PMID:8451644
- ↑ Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R, Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 1995 Dec 29;83(7):1183-96. PMID:8548805
- ↑ Kuehn MJ, Schekman R, Ljungdahl PO. Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J Cell Biol. 1996 Nov;135(3):585-95. PMID:8909535
- ↑ Sutterlin C, Doering TL, Schimmoller F, Schroder S, Riezman H. Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J Cell Sci. 1997 Nov;110 ( Pt 21):2703-14. PMID:9427388
- ↑ Campbell JL, Schekman R. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):837-42. PMID:9023343
- ↑ Morin-Ganet MN, Rambourg A, Clermont Y, Kepes F. Role of endoplasmic reticulum-derived vesicles in the formation of Golgi elements in sec23 and sec18 Saccharomyces Cerevisiae mutants. Anat Rec. 1998 Jun;251(2):256-64. PMID:9624457
- ↑ Kuehn MJ, Herrmann JM, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature. 1998 Jan 8;391(6663):187-90. PMID:9428766 doi:http://dx.doi.org/10.1038/34438
- ↑ Penalver E, Lucero P, Moreno E, Lagunas R. Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. J Bacteriol. 1999 Apr;181(8):2555-63. PMID:10198022
- ↑ Shimoni Y, Kurihara T, Ravazzola M, Amherdt M, Orci L, Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol. 2000 Nov 27;151(5):973-84. PMID:11086000
- ↑ Matsuoka K, Schekman R. The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting. Methods. 2000 Apr;20(4):417-28. PMID:10720463 doi:10.1006/meth.2000.0955
- ↑ Mossessova E, Bickford LC, Goldberg J. SNARE selectivity of the COPII coat. Cell. 2003 Aug 22;114(4):483-95. PMID:12941276
- ↑ Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004 Jan 9;279(2):1330-5. Epub 2003 Nov 19. PMID:14627716 doi:10.1074/jbc.C300457200
- ↑ Schuldiner M, Collins SR, Thompson NJ, Denic V, Bhamidipati A, Punna T, Ihmels J, Andrews B, Boone C, Greenblatt JF, Weissman JS, Krogan NJ. Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell. 2005 Nov 4;123(3):507-19. PMID:16269340 doi:S0092-8674(05)00868-8
- ↑ Cai H, Yu S, Menon S, Cai Y, Lazarova D, Fu C, Reinisch K, Hay JC, Ferro-Novick S. TRAPPI tethers COPII vesicles by binding the coat subunit Sec23. Nature. 2007 Feb 22;445(7130):941-4. Epub 2007 Feb 7. PMID:17287728 doi:http://dx.doi.org/10.1038/nature05527
- ↑ Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R, Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 1995 Dec 29;83(7):1183-96. PMID:8548805
- ↑ Wuestehube LJ, Duden R, Eun A, Hamamoto S, Korn P, Ram R, Schekman R. New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Genetics. 1996 Feb;142(2):393-406. PMID:8852839
- ↑ Salama NR, Chuang JS, Schekman RW. Sec31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum. Mol Biol Cell. 1997 Feb;8(2):205-17. PMID:9190202
- ↑ Campbell JL, Schekman R. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):837-42. PMID:9023343
- ↑ Matsuoka K, Schekman R. The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting. Methods. 2000 Apr;20(4):417-28. PMID:10720463 doi:10.1006/meth.2000.0955
- ↑ Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004 Jan 9;279(2):1330-5. Epub 2003 Nov 19. PMID:14627716 doi:10.1074/jbc.C300457200
- ↑ Nakano A, Muramatsu M. A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J Cell Biol. 1989 Dec;109(6 Pt 1):2677-91. PMID:2512296
- ↑ d'Enfert C, Wuestehube LJ, Lila T, Schekman R. Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p promotes formation of transport vesicles from the ER. J Cell Biol. 1991 Aug;114(4):663-70. PMID:1907973
- ↑ Oka T, Nishikawa S, Nakano A. Reconstitution of GTP-binding Sar1 protein function in ER to Golgi transport. J Cell Biol. 1991 Aug;114(4):671-9. PMID:1907974
- ↑ Oka T, Nakano A. Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast. J Cell Biol. 1994 Feb;124(4):425-34. PMID:8106544
- ↑ Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R, Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 1995 Dec 29;83(7):1183-96. PMID:8548805
- ↑ Yeung T, Barlowe C, Schekman R. Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum. J Biol Chem. 1995 Dec 22;270(51):30567-70. PMID:8530490
- ↑ Campbell JL, Schekman R. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):837-42. PMID:9023343
- ↑ Saito Y, Kimura K, Oka T, Nakano A. Activities of mutant Sar1 proteins in guanine nucleotide binding, GTP hydrolysis, and cell-free transport from the endoplasmic reticulum to the Golgi apparatus. J Biochem. 1998 Oct;124(4):816-23. PMID:9756629
- ↑ Kuehn MJ, Herrmann JM, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature. 1998 Jan 8;391(6663):187-90. PMID:9428766 doi:http://dx.doi.org/10.1038/34438
- ↑ Matsuoka K, Schekman R. The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting. Methods. 2000 Apr;20(4):417-28. PMID:10720463 doi:10.1006/meth.2000.0955
- ↑ Antonny B, Madden D, Hamamoto S, Orci L, Schekman R. Dynamics of the COPII coat with GTP and stable analogues. Nat Cell Biol. 2001 Jun;3(6):531-7. PMID:11389436 doi:http://dx.doi.org/10.1038/35078500
- ↑ Pathre P, Shome K, Blumental-Perry A, Bielli A, Haney CJ, Alber S, Watkins SC, Romero G, Aridor M. Activation of phospholipase D by the small GTPase Sar1p is required to support COPII assembly and ER export. EMBO J. 2003 Aug 15;22(16):4059-69. PMID:12912905 doi:http://dx.doi.org/10.1093/emboj/cdg390
- ↑ Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004 Jan 9;279(2):1330-5. Epub 2003 Nov 19. PMID:14627716 doi:10.1074/jbc.C300457200
- ↑ Sato K, Nakano A. Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat Struct Mol Biol. 2005 Feb;12(2):167-74. Epub 2005 Jan 23. PMID:15665868 doi:http://dx.doi.org/nsmb893
- ↑ 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 Nov;13(5):635-45. PMID:17981133 doi:10.1016/j.devcel.2007.10.006
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