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Mol Biol Cell. 2010 Aug 15;21(16):2930-43. doi: 10.1091/mbc.E10-02-0149. Epub 2010 Jun 23.

EHBP-1 functions with RAB-10 during endocytic recycling in Caenorhabditis elegans.

Author information

1
Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA.

Abstract

Caenorhabditis elegans RAB-10 functions in endocytic recycling in polarized cells, regulating basolateral cargo transport in the intestinal epithelia and postsynaptic cargo transport in interneurons. A similar role was found for mammalian Rab10 in MDCK cells, suggesting that a conserved mechanism regulates these related pathways in metazoans. In a yeast two-hybrid screen for binding partners of RAB-10 we identified EHBP-1, a calponin homology domain (CH) protein, whose mammalian homolog Ehbp1 was previously shown to function during endocytic transport of GLUT4 in adipocytes. In vivo we find that EHBP-1-GFP colocalizes with RFP-RAB-10 on endosomal structures of the intestine and interneurons and that ehbp-1 loss-of-function mutants share with rab-10 mutants specific endosome morphology and cargo localization defects. We also show that loss of EHBP-1 disrupts transport of membrane proteins to the plasma membrane of the nonpolarized germline cells, a defect that can be phenocopied by codepletion of RAB-10 and its closest paralog RAB-8. These results indicate that RAB-10 and EHBP-1 function together in many cell types and suggests that there are differences in the level of redundancy among Rab family members in polarized versus nonpolarized cells.

PMID:
20573983
PMCID:
PMC2921114
DOI:
10.1091/mbc.E10-02-0149
[Indexed for MEDLINE]
Free PMC Article

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