A likely role for a novel PH-domain containing protein, PEPP2, in connecting membrane and cytoskeleton

Biocell. 2012 Dec;36(3):127-32.


PH domains (pleckstrin homology) are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular apartments with assistances of alternative binding partners. PH domain-containing proteins are found to be involved in a wide range of cellular events, including signalling, cytoskeleton rearrangement and vesicular trafficking. Here we showed that a novel PH domain-containing protein, PEPP2, displayed moderate phosphoinositide binding specificity. Full length PEPP2 associated with both plasma membrane and microtubules. The membrane-associated PEPP2 nucleated at cell-cell contacts and the leading edge of migrating cells. Overexpression of PEPP2 increased membrane microviscosity, indicating a potential role of PEPP2 in regulating function of membrane and microtubules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Androstadienes / pharmacology
  • Animals
  • COS Cells
  • Cell Membrane / metabolism*
  • Chlorocebus aethiops
  • Cytoskeleton / metabolism*
  • Diffusion
  • Glutathione Transferase / metabolism
  • Homeodomain Proteins / metabolism*
  • Lipids / chemistry
  • Microscopy, Fluorescence
  • Microtubules / metabolism
  • Models, Biological
  • Phosphatidylinositols / chemistry
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Signal Transduction
  • Viscosity
  • Wortmannin
  • Wound Healing


  • Androstadienes
  • Homeodomain Proteins
  • Lipids
  • Phosphatidylinositols
  • RHOXF2 protein, human
  • Recombinant Fusion Proteins
  • Glutathione Transferase
  • Wortmannin