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Evidence for two interaction regions for phosphatidylinositol(4,5)‐bisphosphate on mammalian profilin I
Author(s) -
Skare Petra,
Karlsson Roger
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02913-7
Subject(s) - profilin , phosphatidylinositol , phosphatidylinositol 4,5 bisphosphate , actina , actin , binding site , biochemistry , chemistry , actin remodeling , mutant , pi , microbiology and biotechnology , biology , biophysics , actin cytoskeleton , gene , signal transduction , cytoskeleton , cell
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:β‐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.