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Rab proteins as membrane organizers
Cellular organelles in the exocytic and endocytic pathways have a distinctive spatial distribution and communicate through an elaborate system of vesiculo-tubular transport. Rab proteins and their…
Rab Conversion as a Mechanism of Progression from Early to Late Endosomes
Rab11 regulates recycling through the pericentriolar recycling endosome
- O. Ullrich, S. Reinsch, S. Urbé, M. Zerial, R. Parton
- BiologyThe Journal of cell biology
- 2 November 1996
A novel role for rab11 in controlling traffic through the recycling endosome is suggested after functional studies showed that the early steps of uptake and recycling for transferrin were not affected by overexpression of rab11 proteins.
Distinct Membrane Domains on Endosomes in the Recycling Pathway Visualized by Multicolor Imaging of Rab4, Rab5, and Rab11
- B. Sönnichsen, S. De Renzis, E. Nielsen, J. Rietdorf, M. Zerial
- Biology, ChemistryThe Journal of cell biology
- 15 May 2000
It is proposed that endosomes are organized as a mosaic of different Rab domains created through the recruitment of specific effector proteins, which cooperatively act to generate a restricted environment on the membrane.
EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
The identification of EEA1 as a direct Rab5 effector provides a molecular link between PI(3)K and Rab5, and its restricted distribution to early endosomes indicates that EEA 1 may confer directionality to Rab5-dependent endocytic transport.
Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.
- H. Stenmark, R. Parton, O. Steele‐Mortimer, A. Lütcke, J. Gruenberg, M. Zerial
- BiologyThe EMBO journal
- 1 March 1994
The opposite effects of the rab5 Q79L and S34N mutants suggest that rab5:GTP is required prior to membrane fusion, whereas GTP hydrolysis by rab5 occurs after membrane fusion and functions to inactivate the protein.
Identification of the Switch in Early-to-Late Endosome Transition
The Rab5 effector EEA1 is a core component of endosome docking
It is shown that Rab5-interacting soluble proteins can completely substitute for cytosol in an in vivo endosome-fusion assay, and that the Rab5 effector EEA1 is the only factor necessary to confer minimal fusion activity.
rab5 controls early endosome fusion in vitro