Rme-1 Regulates the Distribution and Function of the Endocytic Recycling Compartment in Mammalian Cells

Nat Cell Biol. 2001 Jun;3(6):567-72. doi: 10.1038/35078543.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • CHO Cells
  • Caenorhabditis elegans Proteins*
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / physiology*
  • Cell Compartmentation / physiology*
  • Cricetinae
  • Furin
  • Glycoproteins*
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins / metabolism
  • Membrane Proteins*
  • Mice
  • Mutation
  • Phosphoproteins / chemistry
  • Phosphoproteins / genetics
  • Phosphoproteins / physiology*
  • Protein Structure, Tertiary
  • Subtilisins / metabolism
  • Transferrin / metabolism
  • Transport Vesicles / physiology*

Substances

  • Adaptor Proteins, Signal Transducing
  • Caenorhabditis elegans Proteins
  • Calcium-Binding Proteins
  • Eps15 protein, mouse
  • Glycoproteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Phosphoproteins
  • RME-1 protein, C elegans
  • Tgoln1 protein, mouse
  • Tgoln2 protein, mouse
  • Transferrin
  • Subtilisins
  • Furin