Evidence for two interaction regions for phosphatidylinositol(4,5)-bisphosphate on mammalian profilin I.
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.[1]References
- Evidence for two interaction regions for phosphatidylinositol(4,5)-bisphosphate on mammalian profilin I. Skare, P., Karlsson, R. FEBS Lett. (2002) [Pubmed]
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