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TitleStructural basis for Rab6 activation by the Ric1-Rgp1 complex.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10561, Year 2024
Publish dateDec 4, 2024
AuthorsJ Ryan Feathers / Ryan C Vignogna / J Christopher Fromme /
PubMed AbstractRab GTPases act as molecular switches to regulate organelle homeostasis and membrane trafficking. Rab6 plays a central role in regulating cargo flux through the Golgi and is activated via nucleotide ...Rab GTPases act as molecular switches to regulate organelle homeostasis and membrane trafficking. Rab6 plays a central role in regulating cargo flux through the Golgi and is activated via nucleotide exchange by the Ric1-Rgp1 protein complex. Ric1-Rgp1 is conserved throughout eukaryotes but the structural and mechanistic basis for its function has not been established. Here we report the cryoEM structure of a Ric1-Rgp1-Rab6 complex representing a key intermediate of the nucleotide exchange reaction. Ric1-Rgp1 interacts with the nucleotide-binding domain of Rab6 using an uncharacterized helical domain, which we establish as a RabGEF domain by identifying residues required for Rab6 activation. Unexpectedly, the complex uses an arrestin fold to interact with the Rab6 hypervariable domain, indicating that interactions with the unstructured C-terminal regions of Rab GTPases may be a common binding mechanism used by their activators. Collectively, our findings provide a detailed mechanistic understanding of regulated Rab6 activation at the Golgi.
External linksNat Commun / PubMed:39632878 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

43997

9ayr

EMDB-43997, PDB-9ayr:
Structure of a Ric1-Rgp1-Rab6 activation intermediate
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsPROTEIN TRANSPORT / GEF / GTPASE / RAB

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