Evidence for two interaction regions for phosphatidylinositol(4,5)-bisphosphate on mammalian profilin I

FEBS Lett. 2002 Jul 3;522(1-3):119-24. doi: 10.1016/s0014-5793(02)02913-7.


The binding of phosphatidylinositol(4,5)-bisphosphate (PI(4,5)P(2)) to profilin at a region distinct from the actin interaction surface is demonstrated by experiments with covalently cross-linked profilin:beta-actin. The result is in agreement with observations made with several mutant profilins and provides strong evidence for two regions on mammalian profilin mediating electrostatic interaction with phosphatidylinositol lipids; one close to the binding site for poly(L-proline), and one partially overlapping with the actin-binding surface. Congruent with this, two plant profilins, which have a reduced number of positive amino acids in one of these regions, displayed a dramatically lower binding to PI(4,5)P(2) compared to human profilin I.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arabidopsis / genetics
  • Arabidopsis Proteins
  • Binding Sites
  • Contractile Proteins*
  • Cross-Linking Reagents
  • Humans
  • Mammals
  • Micelles
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Phosphatidylinositol 4,5-Diphosphate / metabolism*
  • Profilins
  • Protein Structure, Tertiary


  • Arabidopsis Proteins
  • Contractile Proteins
  • Cross-Linking Reagents
  • Micelles
  • Microfilament Proteins
  • PRF1 protein, Arabidopsis
  • Phosphatidylinositol 4,5-Diphosphate
  • Profilins