期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 26, 页码 23607-23615出版社
ELSEVIER
DOI: 10.1074/jbc.M101034200
关键词
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Rab-GTPase regulates the fusion between two specific vesicles. It is well documented that, for their biological function, Rab proteins need to be prenylated for attachment to the vesicle membrane. In contrast, we showed in the present investigation that SopE, a type III secretory protein of Salmonella, translocates onto Salmonella-containing phagosomes (LSP) and mediates the recruitment of non-prenylated RabB (Rab5:Delta C4) on LSP in GTP form. Simultaneously, SopE present in infected cell cytosol acts as an RabB specific exchange factor and converts the inactive Rab-GDP to the G;TP form. The non-prenylated Rab5 subsequently promoted efficient fusion of LSP with early endosomes. This is the first demonstration that a prenylation-deficient Rab protein retains biological activity and can promote vesicle fusion, if it is recruited on the membrane by some other method.
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