GTPase activity of Rab5 acts as a timer for endocytic membrane fusion
Article Abstract:
Nucleotide triphosphate hydrolysis of GTP by the Rab protein, Rab5, takes place without the intervention of membrane fusion, and the effector Rabaptin-5 inhibits the process. Kinetic analysis of GTPase activity in endocytic membrane fusion using xanthosine 5'-triphosphate-bound mutant supports this observation, and reveals cyclic occurrence of the binding/hydrolysis in the membrane bound Rab5. Nucleotide hydrolysis by Rab5 determines the frequency of membrane fusion/docking events, and this protein is extremely useful for regulation of intercellular transport.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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The Rab5 effector EEA1 is a core component of endosome docking
Article Abstract:
The interplay between soluble factors and SNAREs is required for intracellular membrane docking and fusion. It has been demonstrated that SNARES operated at multiple transport steps and may pair promiscuously, which challenges the role of SNAREs in conveying vesicle targeting. It is shown that Rab5-interacting soluble proteins can substitute for cytosol and that the Rab5 effector EEA1 is the only factor required for minimal fusion activity.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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EEA1 links Pl(3)K function to Rab5 regulation of endosome fusion
Article Abstract:
The early-endosomal autoantigen EEA1 binds to activated Rab5 and regulates Rab5-dependent membrane fusion. This finding indicates that EEA1 is a new Rab5 effector. It is possible that EEA1 is recruited initially to early endosomes through binding to Rab5-GTP. It may then be stabilized further on the membrane by interaction of its FYVE finger with PtdIns(3)P. EEA1 may confer directionality to Rab5-dependent endocytic transport.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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