Pleckstrin homology domains and phospholipid-induced cytoskeletal reorganization.

Abstract:

:At the moment of hemostasis, the platelet must be able to reorganize its cytoskeleton through a complexly orchestrated signaling cascade that is regulated, in part, by polyphosphoinositides. In the past 6 years, evidence has accumulated that PH domains bind these polyphosphoinositides and play a role in cytoskeletal changes. Work to date implies that the amino-terminal PH domain of pleckstrin induces a shift of F-actin towards the cell cortex and participates in the production of lamellipodia. The effect of pleckstrin on actin is, in turn, regulated by the phosphorylation of pleckstrin by PKC. Evidence also suggests that PH domains of Dbl family exchange factors play a role in the PI3K-stimulated activation of Rac. It is likely that the PH domains of pleckstrin, as well as the PH domains of the Dbl family of exchange factors, are only a few examples of PH domains that are able to influence the organization of the cytoskeleton.

journal_name

Thromb Haemost

authors

Ma AD,Abrams CS

keywords:

subject

Has Abstract

pub_date

1999-08-01 00:00:00

pages

399-406

issue

2

eissn

0340-6245

issn

2567-689X

pii

99080399

journal_volume

82

pub_type

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