Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling

Barth Grant; Yinhua Zhang; Marie Christine Paupard; Sharron X. Lin; David H. Hall; David Hirsh

doi:10.1038/35078549

Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling

Barth Grant
, Yinhua Zhang
, Marie Christine Paupard
, Sharron X. Lin
, David H. Hall
, David Hirsh

Neuroscience

Research output: Contribution to journal › Article › peer-review

232 Scopus citations

Abstract

In genetic screens for new endocytosis genes in Caenorhabditis elegans we identified RME-1, a member of a conserved class of Eps15-homology (EH)-domain proteins. Here we show that RME-1 is associated with the periphery of endocytic organelles, which is consistent with a direct role in endocytic transport. Endocytic defects in rme-1 mutants indicate that the protein is likely to have a function in endocytic recycling. Evidence from studies of mammalian RME-1 also points to a function for RME-1 in recycling, specifically in the exit of membrane proteins from recycling endosomes. These studies show a conserved function in endocytic recycling for the RME-1 family of EH proteins.

Original language	English (US)
Pages (from-to)	573-579
Number of pages	7
Journal	Nature Cell Biology
Volume	3
Issue number	6
DOIs	https://doi.org/10.1038/35078549
State	Published - 2001

ASJC Scopus subject areas

Cell Biology

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10.1038/35078549

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@article{dbe7f6e156764306a0e4c9c1f05e86fe,

title = "Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling",

abstract = "In genetic screens for new endocytosis genes in Caenorhabditis elegans we identified RME-1, a member of a conserved class of Eps15-homology (EH)-domain proteins. Here we show that RME-1 is associated with the periphery of endocytic organelles, which is consistent with a direct role in endocytic transport. Endocytic defects in rme-1 mutants indicate that the protein is likely to have a function in endocytic recycling. Evidence from studies of mammalian RME-1 also points to a function for RME-1 in recycling, specifically in the exit of membrane proteins from recycling endosomes. These studies show a conserved function in endocytic recycling for the RME-1 family of EH proteins.",

author = "Barth Grant and Yinhua Zhang and Paupard, \{Marie Christine\} and Lin, \{Sharron X.\} and Hall, \{David H.\} and David Hirsh",

note = "Funding Information: ACKNOWLEDGMENTS We thank L. Pedraza and W. Pryzlecki for technical assistance; H. Fares, V. Irikura, Y. Kohara, X. Li and A. Melendez for reagents and strains; and Q. Al-Aqwati, H. Fares, I. Greenwald, F. Maxfield and H. Wilkinson for discussions during this work and for comments on this manuscript. We also thank H. Fares and I. Greenwald for the gift of rme-1 mutant strains. Many of the strains used in this work were provided by the Caenorhabditis Genetics Center. This work was supported by a grant from NIH to D.H.H., by a NIH National Service Research Award to B.G. and by a March of Dimes Grant to D.H. Correspondence and request for materials should be addressed to B.G. The nucleotide sequences of rme-1 mRNAs have been deposited at Genbank under accession numbers AF357878, AF357877 and AF357876.",

year = "2001",

doi = "10.1038/35078549",

language = "English (US)",

volume = "3",

pages = "573--579",

journal = "Nature Cell Biology",

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AU - Grant, Barth

AU - Zhang, Yinhua

AU - Paupard, Marie Christine

AU - Lin, Sharron X.

AU - Hall, David H.

AU - Hirsh, David

N1 - Funding Information: ACKNOWLEDGMENTS We thank L. Pedraza and W. Pryzlecki for technical assistance; H. Fares, V. Irikura, Y. Kohara, X. Li and A. Melendez for reagents and strains; and Q. Al-Aqwati, H. Fares, I. Greenwald, F. Maxfield and H. Wilkinson for discussions during this work and for comments on this manuscript. We also thank H. Fares and I. Greenwald for the gift of rme-1 mutant strains. Many of the strains used in this work were provided by the Caenorhabditis Genetics Center. This work was supported by a grant from NIH to D.H.H., by a NIH National Service Research Award to B.G. and by a March of Dimes Grant to D.H. Correspondence and request for materials should be addressed to B.G. The nucleotide sequences of rme-1 mRNAs have been deposited at Genbank under accession numbers AF357878, AF357877 and AF357876.

PY - 2001

Y1 - 2001

N2 - In genetic screens for new endocytosis genes in Caenorhabditis elegans we identified RME-1, a member of a conserved class of Eps15-homology (EH)-domain proteins. Here we show that RME-1 is associated with the periphery of endocytic organelles, which is consistent with a direct role in endocytic transport. Endocytic defects in rme-1 mutants indicate that the protein is likely to have a function in endocytic recycling. Evidence from studies of mammalian RME-1 also points to a function for RME-1 in recycling, specifically in the exit of membrane proteins from recycling endosomes. These studies show a conserved function in endocytic recycling for the RME-1 family of EH proteins.

AB - In genetic screens for new endocytosis genes in Caenorhabditis elegans we identified RME-1, a member of a conserved class of Eps15-homology (EH)-domain proteins. Here we show that RME-1 is associated with the periphery of endocytic organelles, which is consistent with a direct role in endocytic transport. Endocytic defects in rme-1 mutants indicate that the protein is likely to have a function in endocytic recycling. Evidence from studies of mammalian RME-1 also points to a function for RME-1 in recycling, specifically in the exit of membrane proteins from recycling endosomes. These studies show a conserved function in endocytic recycling for the RME-1 family of EH proteins.

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Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling

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