An ACAP1-containing clathrin coat complex for endocytic recycling

J Cell Biol. 2007 Jul 30;178(3):453-64. doi: 10.1083/jcb.200608033.

Abstract

Whether coat proteins play a widespread role in endocytic recycling remains unclear. We find that ACAP1, a GTPase-activating protein (GAP) for ADP-ribosylation factor (ARF) 6, is part of a novel clathrin coat complex that is regulated by ARF6 for endocytic recycling in two key physiological settings, stimulation-dependent recycling of integrin that is critical for cell migration and insulin-stimulated recycling of glucose transporter type 4 (Glut4), which is required for glucose homeostasis. These findings not only advance a basic understanding of an early mechanistic step in endocytic recycling but also shed key mechanistic insights into major physiological events for which this transport plays a critical role.

Publication types

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

MeSH terms

  • 3T3-L1 Cells
  • ADP-Ribosylation Factor 6
  • ADP-Ribosylation Factors / metabolism
  • Amino Acid Sequence
  • Animals
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Clathrin / genetics
  • Clathrin / metabolism*
  • Coat Protein Complex I / genetics
  • Coat Protein Complex I / metabolism*
  • Endocytosis / physiology*
  • Endosomes / metabolism*
  • Endosomes / ultrastructure
  • GTPase-Activating Proteins / genetics
  • GTPase-Activating Proteins / metabolism*
  • Glucose Transporter Type 4 / genetics
  • Glucose Transporter Type 4 / metabolism
  • Humans
  • Integrins / metabolism
  • Mice
  • Molecular Sequence Data
  • Multiprotein Complexes
  • Sequence Alignment

Substances

  • ACAP1 protein, human
  • ADP-Ribosylation Factor 6
  • Clathrin
  • Coat Protein Complex I
  • GTPase-Activating Proteins
  • Glucose Transporter Type 4
  • Integrins
  • Multiprotein Complexes
  • ADP-Ribosylation Factors
  • ARF6 protein, human
  • Arf6 protein, mouse