Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange | Zendy

Thierry Soldati | Zendy; Allan D. Shapiro | Zendy; A. Barbara Dirac-Svejstrup | Zendy; Suzanne R. Pfefffer | Zendy

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Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange

Author(s) -

Thierry Soldati,

Allan D. Shapiro,

A. Barbara Dirac-Svejstrup,

Suzanne R. Pfefffer

Publication year - 1994

Publication title -

nature

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 15.993

H-Index - 1226

eISSN - 1476-4687

pISSN - 0028-0836

DOI - 10.1038/369076a0

Subject(s) - rab , prenylation , gtpase , endosome , guanine nucleotide exchange factor , golgi apparatus , microbiology and biotechnology , transport protein , cytosol , vesicular transport protein , small gtpase , gtp' , mannose , biology , biochemistry , chemistry , membrane , receptor , vesicle , signal transduction , endoplasmic reticulum , enzyme

The Rab GTPases are key regulators of vesicular transport. A fraction of Rab proteins is present in the cytosol, bound with GDP, complexed to a protein termed GDI. Rab9 is localized primarily to late endosomes, where it aids the transport of mannose 6-phosphate receptors to the trans-Golgi network. It has been proposed that Rab proteins are delivered to specific membranes by GDI, and that this process is accompanied by the exchange of bound GDP for GTP. In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants. Here we describe the reconstitution of the selective targeting of prenylated Rab9 protein onto late endosome membranes and show that this process is accompanied by endosome-triggered nucleotide exchange.

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