A Highlights from MBoC Selection: EHBP-1 Functions with RAB-10 during Endocytic Recycling in Caenorhabditis elegans |
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Authors: | Anbing Shi Carlos Chih-Hsiung Chen Riju Banerjee Doreen Glodowski Anjon Audhya Christopher Rongo Barth D. Grant |
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Affiliation: | *Department of Molecular Biology and Biochemistry.;‡Department of Genetics and the Waksman Institute, Rutgers University, Piscataway, NJ 08854; and ;§Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53706 |
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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. |
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