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

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

Research output: Contribution to journalArticle

119 Citations (Scopus)

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 1 2009

Fingerprint

Endosomes
Caenorhabditis elegans
Dynamins
Proteins
Membranes
GTP Phosphohydrolases
Recycling
Viperidae
Endocytosis
Mammals
Cell Membrane
amphiphysin

ASJC Scopus subject areas

  • Cell Biology

Cite this

Pant, S., Sharma, M., Patel, K., Caplan, S. H., 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

AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. / Pant, Saumya; Sharma, Mahak; Patel, Kruti; Caplan, Steven H; Carr, Chavela M.; Grant, Barth D.

In: Nature Cell Biology, Vol. 11, No. 12, 01.12.2009, p. 1399-1410.

Research output: Contribution to journalArticle

Pant, S, Sharma, M, Patel, K, Caplan, SH, Carr, CM & Grant, BD 2009, 'AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling', Nature Cell Biology, vol. 11, no. 12, pp. 1399-1410. https://doi.org/10.1038/ncb1986
Pant, Saumya ; Sharma, Mahak ; Patel, Kruti ; Caplan, Steven H ; Carr, Chavela M. ; Grant, Barth D. / AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. In: Nature Cell Biology. 2009 ; Vol. 11, No. 12. pp. 1399-1410.
@article{71213aa5a2e449ac8bf114ea9c65b76a,
title = "AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling",
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.",
author = "Saumya Pant and Mahak Sharma and Kruti Patel and Caplan, {Steven H} and Carr, {Chavela M.} and Grant, {Barth D.}",
year = "2009",
month = "12",
day = "1",
doi = "10.1038/ncb1986",
language = "English (US)",
volume = "11",
pages = "1399--1410",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Nature Publishing Group",
number = "12",

}

TY - JOUR

T1 - AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling

AU - Pant, Saumya

AU - Sharma, Mahak

AU - Patel, Kruti

AU - Caplan, Steven H

AU - Carr, Chavela M.

AU - Grant, Barth D.

PY - 2009/12/1

Y1 - 2009/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=73349097586&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=73349097586&partnerID=8YFLogxK

U2 - 10.1038/ncb1986

DO - 10.1038/ncb1986

M3 - Article

VL - 11

SP - 1399

EP - 1410

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 12

ER -