Structural highlights
4q66 is a 12 chain structure with sequence from Baker's yeast and Saccharomyces cerevisiae r008. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 4gns, 4in3 |
| Gene: | CAL3, Chs5, L8543.18, R008_L12446, YLR330W (Saccharomyces cerevisiae R008), BCH1, YMR237W, YM9959.19 (Baker's yeast), ARF1, YDL192W, D1244 (Baker's yeast) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[ARF1_YEAST] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.[1] [BCH1_YEAST] Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3.[2] [3] [4]
Publication Abstract from PubMed
Cargo adaptor subunits of vesicle coat protein complexes sort transmembrane proteins to distinct membrane compartments in eukaryotic cells. The exomer complex is the only cargo adaptor known to sort proteins at the trans-Golgi network into secretory vesicles. Exomer function is regulated by the Arf1 GTPase, a master regulator of trafficking at the Golgi. We report the structure of exomer bound to two copies of Arf1. Exomer interacts with each Arf1 molecule via two surfaces, one of which is a noncanonical interface that regulates GTP hydrolysis. The structure uncovers an unexpected membrane-proximal hydrophobic element that exomer uses in cooperation with Arf1 to remodel membranes. Given the constrained motion of the exomer hinge region, we envision that exomer dynamically positions multiple membrane insertion elements to drive membrane fission. In contrast to other known cargo adaptors, exomer therefore couples two functions, cargo sorting and membrane fission, into a single complex.
Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor.,Paczkowski JE, Fromme JC Dev Cell. 2014 Sep 8;30(5):610-24. doi: 10.1016/j.devcel.2014.07.014. PMID:25203211[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Trautwein M, Dengjel J, Schirle M, Spang A. Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae. Mol Biol Cell. 2004 Nov;15(11):5021-37. Epub 2004 Sep 8. PMID:15356266 doi:http://dx.doi.org/10.1091/mbc.E04-05-0411
- ↑ Trautwein M, Schindler C, Gauss R, Dengjel J, Hartmann E, Spang A. Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi. EMBO J. 2006 Mar 8;25(5):943-54. Epub 2006 Feb 23. PMID:16498409 doi:7601007
- ↑ Wang CW, Hamamoto S, Orci L, Schekman R. Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast. J Cell Biol. 2006 Sep 25;174(7):973-83. PMID:17000877 doi:10.1083/jcb.200605106
- ↑ Sanchatjate S, Schekman R. Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface. Mol Biol Cell. 2006 Oct;17(10):4157-66. Epub 2006 Jul 19. PMID:16855022 doi:10.1091/mbc.E06-03-0210
- ↑ Paczkowski JE, Fromme JC. Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor. Dev Cell. 2014 Sep 8;30(5):610-24. doi: 10.1016/j.devcel.2014.07.014. PMID:25203211 doi:http://dx.doi.org/10.1016/j.devcel.2014.07.014
