Authors: | Mossessova, E.; Bickford, L. C.; Goldberg, J. |
Article Title: | SNARE selectivity of the COPII coat |
Abstract: | 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. |
Keywords: | controlled study; unclassified drug; nonhuman; protein motif; protein assembly; protein protein interaction; protein; protein binding; membrane proteins; endoplasmic reticulum; amino acid sequence; carrier proteins; substrate specificity; protein transport; phosphoproteins; binding site; models, molecular; crystallography, x-ray; protein structure, tertiary; yeast; saccharomyces cerevisiae proteins; protein subunit; guanosine triphosphate; amino acid motifs; macromolecular substances; receptors, cell surface; golgi complex; vesicular transport proteins; cop-coated vesicles; membrane transport proteins; snare protein; qa-snare proteins; r-snare proteins; snare proteins; priority journal; article; qc-snare proteins; bet1 protein; sar1 protein; sec22 protein; sed5 protein |
Journal Title: | Cell |
Volume: | 114 |
Issue: | 4 |
ISSN: | 0092-8674 |
Publisher: | Cell Press |
Date Published: | 2003-08-22 |
Start Page: | 483 |
End Page: | 495 |
Language: | English |
DOI: | 10.1016/s0092-8674(03)00608-1 |
PUBMED: | 12941276 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Export Date: 12 September 2014 -- Source: Scopus |