Crystal structure of the COPII coat subunit, Sec24, complexed with a peptide from the SNARE protein Bet1Crystal structure of the COPII coat subunit, Sec24, complexed with a peptide from the SNARE protein Bet1
Structural highlights
1pcx is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[SEC24_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. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter.[1][2][3][4][5][6][7][8][9][10][11][12][13] [BET1_YEAST] SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.[14][15]
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 coat buds transport vesicles from the endoplasmic reticulum that incorporate cargo and SNARE molecules. Here, we show that recognition of the ER-Golgi SNAREs Bet1, Sed5, and Sec22 occurs through three binding sites on the Sec23/24 subcomplex of yeast COPII. The A site binds to the YNNSNPF motif of Sed5. The B site binds to Lxx-L/M-E sequences present in both the Bet1 and Sed5 molecules, as well as to the DxE cargo-sorting signal. A third, spatially distinct site binds to Sec22. COPII selects the free v-SNARE form of Bet1 because the LxxLE sequence is sequestered in the four-helix bundle of the v-/t-SNARE complex. COPII favors Sed5 within the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinhibitory contacts to expose the YNNSNPF motif. The COPII coat seems to be a specific conductor of the fusogenic forms of these SNAREs, suggesting how vesicle fusion specificity may be programmed during budding.
SNARE selectivity of the COPII coat.,Mossessova E, Bickford LC, Goldberg J Cell. 2003 Aug 22;114(4):483-95. PMID:12941276[16]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑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
↑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
↑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
↑Peng R, De Antoni A, Gallwitz D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem. 2000 Apr 14;275(15):11521-8. PMID:10753972
↑Higashio H, Kimata Y, Kiriyama T, Hirata A, Kohno K. Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum. J Biol Chem. 2000 Jun 9;275(23):17900-8. PMID:10749860 doi:http://dx.doi.org/10.1074/jbc.M000751200
↑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
↑Kurihara T, Hamamoto S, Gimeno RE, Kaiser CA, Schekman R, Yoshihisa T. Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. Mol Biol Cell. 2000 Mar;11(3):983-98. PMID:10712514
↑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 Aug 22;114(4):497-509. PMID:12941277
↑Hamasaki M, Noda T, Ohsumi Y. The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct. 2003 Feb;28(1):49-54. PMID:12655150
↑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
↑Newman AP, Groesch ME, Ferro-Novick S. Bos1p, a membrane protein required for ER to Golgi transport in yeast, co-purifies with the carrier vesicles and with Bet1p and the ER membrane. EMBO J. 1992 Oct;11(10):3609-17. PMID:1396561
