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Role of actin binding protein phosphorylation in platelet cytoskeleton assembly.

Abstract：

:Actin binding protein from human blood platelets is shown to exist in the resting platelet as a phosphorylated protein and contains two residues of phosphate per 260,000 kd. Removal of one-half of these residues with E. coli alkaline phosphatase results in the loss of its ability to crosslink F-actin into a low speed sedimentable complex (its cytoskeleton) and to bind to an F-actin affinity column. Thus, phosphorylation-dephosphorylation of ABP may be an important regulatory mechanism by which the platelet regulates its shape via its cytoskeletal structure.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zhuang QQ,Rosenberg S,Lawrence J,Stracher A

doi

10.1016/0006-291x(84)91332-9

subject

Has Abstract

pub_date

1984-01-30 00:00:00

pages

508-13

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)91332-9

journal_volume

118

pub_type

杂志文章

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