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

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 Lett

journal_title

FEBS letters

authors

Skare P,Karlsson R

doi

10.1016/s0014-5793(02)02913-7

keywords:

subject

Has Abstract

pub_date

2002-07-03 00:00:00

pages

119-24

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302029137

journal_volume

522

pub_type

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