Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis

J Cell Biol. 2006 Jan 16;172(2):269-79. doi: 10.1083/jcb.200508091.

Abstract

The conserved FER-CIP4 homology (FCH) domain is found in the pombe Cdc15 homology (PCH) protein family members, including formin-binding protein 17 (FBP17). However, the amino acid sequence homology extends beyond the FCH domain. We have termed this region the extended FC (EFC) domain. We found that FBP17 coordinated membrane deformation with actin cytoskeleton reorganization during endocytosis. The EFC domains of FBP17, CIP4, and other PCH protein family members show weak homology to the Bin-amphiphysin-Rvs (BAR) domain. The EFC domains bound strongly to phosphatidylserine and phosphatidylinositol 4,5-bisphosphate and deformed the plasma membrane and liposomes into narrow tubules. Most PCH proteins possess an SH3 domain that is known to bind to dynamin and that recruited and activated neural Wiskott-Aldrich syndrome protein (N-WASP) at the plasma membrane. FBP17 and/or CIP4 contributed to the formation of the protein complex, including N-WASP and dynamin-2, in the early stage of endocytosis. Furthermore, knockdown of endogenous FBP17 and CIP4 impaired endocytosis. Our data indicate that PCH protein family members couple membrane deformation to actin cytoskeleton reorganization in various cellular processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Chlorocebus aethiops
  • Cytoskeleton / metabolism*
  • Dynamin II / genetics
  • Dynamin II / metabolism
  • Endocytosis / physiology*
  • ErbB Receptors / genetics
  • ErbB Receptors / metabolism
  • Fatty Acid-Binding Proteins
  • Humans
  • Liposomes / chemistry
  • Mice
  • Molecular Sequence Data
  • Phosphatidylinositols / metabolism
  • Protein Structure, Tertiary
  • RNA Interference
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Sequence Alignment
  • Wiskott-Aldrich Syndrome Protein, Neuronal / genetics
  • Wiskott-Aldrich Syndrome Protein, Neuronal / metabolism

Substances

  • Actins
  • Carrier Proteins
  • FNBP1 protein, human
  • Fatty Acid-Binding Proteins
  • Liposomes
  • Phosphatidylinositols
  • Recombinant Fusion Proteins
  • Wiskott-Aldrich Syndrome Protein, Neuronal
  • ErbB Receptors
  • Dynamin II