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

Barth D. Grant, Steve Caplan

Research output: Contribution to journalReview articlepeer-review

114 Scopus citations


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
Issue number12
StatePublished - 2008

All Science Journal Classification (ASJC) codes

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


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


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