Key result
Experiments with cross-linked profilin:beta-actin and mutant profilins demonstrate two distinct regions on mammalian profilin I that mediate electrostatic interaction with PI(4,5)P(2).
The study identifies two distinct regions on mammalian profilin I that mediate electrostatic interactions with phosphatidylinositol lipids.
Does not support clinical translation; hypothesis-generating for profilin I-lipid interactions in cellular signaling.
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.
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Skare et al. (2002) studied this question. Phosphatidylinositol(4,5)-bisphosphate (PI(4,5)P(2)) was evaluated on Binding regions on mammalian profilin I. Experiments with cross-linked profilin:beta-actin and mutant profilins demonstrate two distinct regions on mammalian profilin I that mediate electrostatic interaction with PI(4,5)P(2).
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