Journal
STRUCTURE
Volume 11, Issue 3, Pages 347-357Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(03)00034-0
Keywords
GDI; Rab; prenylation; vesicle transport; REP
Funding
- NCI NIH HHS [CA 78819] Funding Source: Medline
- NEI NIH HHS [EY 11606] Funding Source: Medline
- NIGMS NIH HHS [GM33301, GM42336] Funding Source: Medline
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Rab GTPases, key regulators of membrane targeting and fusion, require the covalent attachment of geranylgeranyl lipids to their C terminus for function. To elucidate the role of lipid in Rab recycling, we have determined the crystal structure of Rab guanine nucleotide dissociation inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand (H2N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding platform in a shallow hydrophobic groove. Mutation of the binding pocket in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to promote release of the GDI-Rab[GDP] complex from the membrane.
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