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F-actin capping by cap32/34 requires heterodimeric conformation and can be inhibited with PIP2.

Abstract：

:The heterodimeric F-actin capping protein cap32/34 from Dictyostelium discoideum is a typical member of a widely distributed family of cytoskeletal proteins. To analyze its regulation and structure/function relationships we cloned and expressed the subunits separately in Escherichia coli using the ATG-expression vector pT7-7. Studies on the viscosity of F-actin solutions and the kinetics of actin polymerization in the presence of single subunits or the reconstituted protein showed that capping of F-actin absolutely requires the heterodimeric conformation. This activity can be inhibited by phosphatidyl bisphosphate (PIP2), an important component in signal transduction. The regulation of cap32/34 by PIP2 suggests an involvement of this protein in the re-organization of the actin cytoskeleton upon stimulation of D. discoideum cells with chemoattractant.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Haus U,Hartmann H,Trommler P,Noegel AA,Schleicher M

doi

10.1016/0006-291x(91)91265-e

subject

Has Abstract

pub_date

1991-12-16 00:00:00

pages

833-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)91265-E

journal_volume

181

pub_type

杂志文章

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