Article abstract
Nature Cell Biology 7, 559 - 569 (2005)
Published online: 15 May 2005 | doi:10.1038/ncb1261
Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the clathrin-coated pit
Miyuki Sato1, Ken Sato1,3, Paul Fonarev1, Chih-Jen Huang2, Willisa Liou2 & Barth D. Grant1
Abstract
Here we identify a new regulator of endocytosis called RME-6. RME-6 is evolutionarily conserved among metazoans and contains Ras-GAP (GTPase-activating protein)-like and Vps9 domains. Consistent with the known catalytic function of Vps9 domains in Rab5 GDP/GTP exchange, we found that RME-6 binds specifically to Caenorhabditis elegans RAB-5 in the GDP-bound conformation, and rme-6 mutants have phenotypes that indicate low RAB-5 activity. However, unlike other Rab5-associated proteins, a rescuing green fluorescent protein (GFP)–RME-6 fusion protein primarily localizes to clathrin-coated pits, physically interacts with 
-adaptin, a clathrin adaptor protein, and requires clathrin to achieve its cortical localization. In rme-6 mutants, transport from the plasma membrane to endosomes is defective, and small 110-nm endocytic vesicles accumulate just below the plasma membrane. These results suggest a mechanism for the activation of Rab5 in clathrin-coated pits or clathrin-coated vesicles that is essential for the delivery of endocytic cargo to early endosomes.
- Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA.
- Department of Anatomy, Chang Gung University, Kwei-Shan Tao-Yuan, Taiwan, 333, R.O.C.
- Molecular Membrane Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan.
Correspondence to: Barth D. Grant1 e-mail: grant@biology.rutgers.edu
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