@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",
issn = "1465-7392",
publisher = "Nature Publishing Group",
number = "6",
}