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Published online 30 October 2000. doi:10.1083/jcb.151.3.601
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© The Rockefeller University Press, 0021-9525/2000//601 $5.00
The Journal of Cell Biology, Volume 151, Number 3, , 2000 601-612

Original Article

Rabenosyn-5, a Novel Rab5 Effector, Is Complexed with Hvps45 and Recruited to Endosomes through a Fyve Finger Domain



Erik Nielsena, Savvas Christoforidisa, Sandrine Uttenweiler-Josephb, Marta Miaczynskaa, Frederique Dewittec, Matthias Wilmb, Bernard Hoflackc, and Marino Zeriala

a Max-Planck-Institute for Molecular Cell Biology and Genetics, 01307 Dresden, Germany
b European Molecular Biology Laboratory, 69117 Heidelberg, Germany
c Institut de Biologie de Lille, Centre National de la Recherche Scientifique EP 525/Institut Pasteur de Lille 1, 59021 Lille, France
Max-Planck-Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse, 01307 Dresden, Germany.49-6221-387-51249-6221-387-232

Rab5 regulates endocytic membrane traffic by specifically recruiting cytosolic effector proteins to their site of action on early endosomal membranes. We have characterized a new Rab5 effector complex involved in endosomal fusion events. This complex includes a novel protein, Rabenosyn-5, which, like the previously characterized Rab5 effector early endosome antigen 1 (EEA1), contains an FYVE finger domain and is recruited in a phosphatidylinositol-3-kinase–dependent fashion to early endosomes. Rabenosyn-5 is complexed to the Sec1-like protein hVPS45. hVPS45 does not interact directly with Rab5, therefore Rabenosyn-5 serves as a molecular link between hVPS45 and the Rab5 GTPase. This property suggests that Rabenosyn-5 is a closer mammalian functional homologue of yeast Vac1p than EEA1. Furthermore, although both EEA1 and Rabenosyn-5 are required for early endosomal fusion, only overexpression of Rabenosyn-5 inhibits cathepsin D processing, suggesting that the two proteins play distinct roles in endosomal trafficking. We propose that Rab5-dependent formation of membrane domains enriched in phosphatidylinositol-3-phosphate has evolved as a mechanism for the recruitment of multiple effector proteins to mammalian early endosomes, and that these domains are multifunctional, depending on the differing activities of the effector proteins recruited.

Key Words: endocytosis • Rab5 • hVPS45 • EEA1 • Rabenosyn-5

© 2000 The Rockefeller University Press

S. Christoforidis' present address is Laboratory of Biological Chemistry, Medical School, University of Ioannina, 45110 Ioannina, Greece.

Abbreviations used in this paper: CCV, clathrin-coated vesicle; EEA1, early endosome antigen 1; EGFP, enhanced GFP; EH, E15 homology; EST, expressed sequence tag; GFP, green fluorescent protein; GST, glutathione S-transferase; NSF, N-ethylmaleimide–sensitive factor; P, phosphate; PC, phosphatidylcholine; PI, phosphatidylinositol; PVC, prevacuolar compartment; SNAP, soluble NSF attachment protein; SNARE, SNAP receptor.


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