AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling

Saumya Pant, Mahak Sharma, Kruti Patel, Steve Caplan, Chavela M. Carr, Barth D. Grant

Research output: Contribution to journalArticle

129 Scopus citations

Abstract

RME-1/EHD1 (receptor mediated endocytosis/Eps15 homology-domain containing 1) family proteins are key residents of the recycling endosome, which are required for endosome-to-plasma membrane transport in Caenorhabditis elegans and mammals. Recent studies suggest similarities between the RME-1/EHD proteins and the Dynamin GTPase superfamily of mechanochemical pinchases, which promote membrane fission. Here we show that endogenous C. elegans AMPH-1, the only C. elegans member of the Amphiphysin/BIN1 family of BAR (Bin1-Amphiphysin-Rvs161p/ 167p)-domain-containing proteins, colocalizes with RME-1 on recycling endosomes in vivo, that amph-1-deletion mutants are defective in recycling endosome morphology and function, and that binding of AMPH-1 Asn-Pro-Phe(Asp/Glu) sequences to the RME-1 EH-domain promotes the recycling of transmembrane cargo. We also show a requirement for human BIN1 (also known as Amphiphysin 2) in EHD1-regulated endocytic recycling. In vitro, we find that purified recombinant AMPH-1-RME-1 complexes produce short, coated membrane tubules that are qualitatively distinct from those produced by either protein alone. Our results indicate that AMPH-1 and RME-1 cooperatively regulate endocytic recycling, probably through functions required for the production of cargo carriers that exit the recycling endosome for the cell surface.

Original languageEnglish (US)
Pages (from-to)1399-1410
Number of pages12
JournalNature Cell Biology
Volume11
Issue number12
DOIs
StatePublished - Dec 2009

ASJC Scopus subject areas

  • Cell Biology

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    Pant, S., Sharma, M., Patel, K., Caplan, S., Carr, C. M., & Grant, B. D. (2009). AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. Nature Cell Biology, 11(12), 1399-1410. https://doi.org/10.1038/ncb1986