Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Skare P,Karlsson Rdoi
10.1016/s0014-5793(02)02913-7keywords:
subject
Has Abstractpub_date
2002-07-03 00:00:00pages
119-24issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302029137journal_volume
522pub_type
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