Pleckstrin homology domains and phospholipid-induced cytoskeletal reorganization

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 rol...

Full description

Saved in:
Bibliographic Details
Published inThrombosis and haemostasis Vol. 82; no. 2; p. 399
Main Authors Ma, A D, Abrams, C S
Format Journal Article
LanguageEnglish
Published Germany 01.08.1999
Subjects
Actins - physiology
Amino Acid Motifs
Animals
Blood Proteins - chemistry
Blood Proteins - physiology
Caenorhabditis elegans Proteins
Cytoskeleton - physiology
GTP-Binding Proteins
Humans
Phospholipids - physiology
Phosphoproteins
Phosphorylation
Platelet Activation - physiology
Protein Structure, Tertiary
RGS Proteins
Signal Transduction
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0340-6245
DOI:10.1055/s-0037-1615859