Mechanisms of EHD/RME-1 protein function in endocytic transport

Barth D. Grant, Steven H Caplan

Research output: Contribution to journalReview article

102 Citations (Scopus)

Abstract

The evolutionarily conserved Eps15 homology domain (EHD)/ receptor-mediated endocytosis (RME)-1 family of C-terminal EH domain proteins has recently come under intense scrutiny because of its importance in intracellular membrane transport, especially with regard to the recycling of receptors from endosomes to the plasma membrane. Recent studies have shed new light on the mode by which these adenosine triphosphatases function on endosomal membranes in mammals and Caenorhabditis elegans. This review highlights our current understanding of the physiological roles of these proteins in vivo, discussing conserved features as well as emerging functional differences between individual mammalian paralogs. In addition, these findings are discussed in light of the identification of novel EHD/RME-1 protein and lipid interactions and new structural data for proteins in this family, indicating intriguing similarities to the Dynamin superfamily of large guanosine triphosphatases.

Original languageEnglish (US)
Pages (from-to)2043-2052
Number of pages10
JournalTraffic
Volume9
Issue number12
DOIs
StatePublished - Nov 20 2008

Fingerprint

Endocytosis
Dynamins
Intracellular Membranes
Proteins
Guanosine
Endosomes
Caenorhabditis elegans
Membranes
Individuality
Mammals
Adenosine Triphosphatases
Cell membranes
Cell Membrane
Lipids
Recycling

Keywords

  • C. elegans
  • EH domain
  • EHD1
  • EHD2
  • EHD3
  • EHD4
  • Endocytic trafficking
  • RME-1
  • Rab effectors
  • Recycling

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Mechanisms of EHD/RME-1 protein function in endocytic transport. / Grant, Barth D.; Caplan, Steven H.

In: Traffic, Vol. 9, No. 12, 20.11.2008, p. 2043-2052.

Research output: Contribution to journalReview article

Grant, Barth D. ; Caplan, Steven H. / Mechanisms of EHD/RME-1 protein function in endocytic transport. In: Traffic. 2008 ; Vol. 9, No. 12. pp. 2043-2052.
@article{2dff091f70dc43669a3c529596884c9d,
title = "Mechanisms of EHD/RME-1 protein function in endocytic transport",
abstract = "The evolutionarily conserved Eps15 homology domain (EHD)/ receptor-mediated endocytosis (RME)-1 family of C-terminal EH domain proteins has recently come under intense scrutiny because of its importance in intracellular membrane transport, especially with regard to the recycling of receptors from endosomes to the plasma membrane. Recent studies have shed new light on the mode by which these adenosine triphosphatases function on endosomal membranes in mammals and Caenorhabditis elegans. This review highlights our current understanding of the physiological roles of these proteins in vivo, discussing conserved features as well as emerging functional differences between individual mammalian paralogs. In addition, these findings are discussed in light of the identification of novel EHD/RME-1 protein and lipid interactions and new structural data for proteins in this family, indicating intriguing similarities to the Dynamin superfamily of large guanosine triphosphatases.",
keywords = "C. elegans, EH domain, EHD1, EHD2, EHD3, EHD4, Endocytic trafficking, RME-1, Rab effectors, Recycling",
author = "Grant, {Barth D.} and Caplan, {Steven H}",
year = "2008",
month = "11",
day = "20",
doi = "10.1111/j.1600-0854.2008.00834.x",
language = "English (US)",
volume = "9",
pages = "2043--2052",
journal = "Traffic",
issn = "1398-9219",
publisher = "Blackwell Munksgaard",
number = "12",

}

TY - JOUR

T1 - Mechanisms of EHD/RME-1 protein function in endocytic transport

AU - Grant, Barth D.

AU - Caplan, Steven H

PY - 2008/11/20

Y1 - 2008/11/20

N2 - The evolutionarily conserved Eps15 homology domain (EHD)/ receptor-mediated endocytosis (RME)-1 family of C-terminal EH domain proteins has recently come under intense scrutiny because of its importance in intracellular membrane transport, especially with regard to the recycling of receptors from endosomes to the plasma membrane. Recent studies have shed new light on the mode by which these adenosine triphosphatases function on endosomal membranes in mammals and Caenorhabditis elegans. This review highlights our current understanding of the physiological roles of these proteins in vivo, discussing conserved features as well as emerging functional differences between individual mammalian paralogs. In addition, these findings are discussed in light of the identification of novel EHD/RME-1 protein and lipid interactions and new structural data for proteins in this family, indicating intriguing similarities to the Dynamin superfamily of large guanosine triphosphatases.

AB - The evolutionarily conserved Eps15 homology domain (EHD)/ receptor-mediated endocytosis (RME)-1 family of C-terminal EH domain proteins has recently come under intense scrutiny because of its importance in intracellular membrane transport, especially with regard to the recycling of receptors from endosomes to the plasma membrane. Recent studies have shed new light on the mode by which these adenosine triphosphatases function on endosomal membranes in mammals and Caenorhabditis elegans. This review highlights our current understanding of the physiological roles of these proteins in vivo, discussing conserved features as well as emerging functional differences between individual mammalian paralogs. In addition, these findings are discussed in light of the identification of novel EHD/RME-1 protein and lipid interactions and new structural data for proteins in this family, indicating intriguing similarities to the Dynamin superfamily of large guanosine triphosphatases.

KW - C. elegans

KW - EH domain

KW - EHD1

KW - EHD2

KW - EHD3

KW - EHD4

KW - Endocytic trafficking

KW - RME-1

KW - Rab effectors

KW - Recycling

UR - http://www.scopus.com/inward/record.url?scp=56149084770&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=56149084770&partnerID=8YFLogxK

U2 - 10.1111/j.1600-0854.2008.00834.x

DO - 10.1111/j.1600-0854.2008.00834.x

M3 - Review article

C2 - 18801062

AN - SCOPUS:56149084770

VL - 9

SP - 2043

EP - 2052

JO - Traffic

JF - Traffic

SN - 1398-9219

IS - 12

ER -