Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells

Sharron X. Lin; Barth Grant; David Hirsh; Frederick R. Maxfield

doi:10.1038/35078543

Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells

Sharron X. Lin, Barth Grant, David Hirsh, Frederick R. Maxfield

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173 Scopus citations

Abstract

RME-1 is an Eps15-homology (EH)-domain protein that was identified in a genetic screen for endocytosis genes in Caenorhabditis elegans. When expressed in a CHO cell line, the worm RME-1 protein and a mouse homologue are both associated with the endocytic recycling compartment. Here we show that expression of a dominant-negative construct with a point mutation near the EH domain results in redistribution of the endocytic recycling compartment and slowing down of transferrin receptor recycling. The delivery of a TGN38 chimaeric protein to the trans-Golgi network is also slowed down. The function of Rme-1 in endocytic recycling is evolutionarily conserved in metazoans as shown by the protein's properties in C. elegans.

Original language	English (US)
Pages (from-to)	567-572
Number of pages	6
Journal	Nature Cell Biology
Volume	3
Issue number	6
DOIs	https://doi.org/10.1038/35078543
State	Published - 2001
Externally published	Yes

All Science Journal Classification (ASJC) codes

Cell Biology

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10.1038/35078543

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@article{06ed6b8e22f644e1ab9a52225c5e8831,

title = "Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells",

abstract = "RME-1 is an Eps15-homology (EH)-domain protein that was identified in a genetic screen for endocytosis genes in Caenorhabditis elegans. When expressed in a CHO cell line, the worm RME-1 protein and a mouse homologue are both associated with the endocytic recycling compartment. Here we show that expression of a dominant-negative construct with a point mutation near the EH domain results in redistribution of the endocytic recycling compartment and slowing down of transferrin receptor recycling. The delivery of a TGN38 chimaeric protein to the trans-Golgi network is also slowed down. The function of Rme-1 in endocytic recycling is evolutionarily conserved in metazoans as shown by the protein's properties in C. elegans.",

author = "Lin, {Sharron X.} and Barth Grant and David Hirsh and Maxfield, {Frederick R.}",

note = "Funding Information: ACKNOWLEDGEMENTS We thank members of the laboratory of F. R. Maxfield and D. Hirsh for discussions during the course of this study. We also thank W. Pryzlecki for technical assistance. This work was supported by a grant from NIH (to F.R.M.), an NIH National Research Service Award (to B.G.) and a March of Dimes Grant (to D.H.).",

year = "2001",

doi = "10.1038/35078543",

language = "English (US)",

volume = "3",

pages = "567--572",

journal = "Nature Cell Biology",

issn = "1465-7392",

publisher = "Nature Publishing Group",

number = "6",

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T1 - Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells

AU - Lin, Sharron X.

AU - Grant, Barth

AU - Hirsh, David

AU - Maxfield, Frederick R.

N1 - Funding Information: ACKNOWLEDGEMENTS We thank members of the laboratory of F. R. Maxfield and D. Hirsh for discussions during the course of this study. We also thank W. Pryzlecki for technical assistance. This work was supported by a grant from NIH (to F.R.M.), an NIH National Research Service Award (to B.G.) and a March of Dimes Grant (to D.H.).

PY - 2001

Y1 - 2001

N2 - RME-1 is an Eps15-homology (EH)-domain protein that was identified in a genetic screen for endocytosis genes in Caenorhabditis elegans. When expressed in a CHO cell line, the worm RME-1 protein and a mouse homologue are both associated with the endocytic recycling compartment. Here we show that expression of a dominant-negative construct with a point mutation near the EH domain results in redistribution of the endocytic recycling compartment and slowing down of transferrin receptor recycling. The delivery of a TGN38 chimaeric protein to the trans-Golgi network is also slowed down. The function of Rme-1 in endocytic recycling is evolutionarily conserved in metazoans as shown by the protein's properties in C. elegans.

AB - RME-1 is an Eps15-homology (EH)-domain protein that was identified in a genetic screen for endocytosis genes in Caenorhabditis elegans. When expressed in a CHO cell line, the worm RME-1 protein and a mouse homologue are both associated with the endocytic recycling compartment. Here we show that expression of a dominant-negative construct with a point mutation near the EH domain results in redistribution of the endocytic recycling compartment and slowing down of transferrin receptor recycling. The delivery of a TGN38 chimaeric protein to the trans-Golgi network is also slowed down. The function of Rme-1 in endocytic recycling is evolutionarily conserved in metazoans as shown by the protein's properties in C. elegans.

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Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells

Abstract

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