Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets

R Y Li; F Gaits; A Ragab; J M Ragab-Thomas; H Chap

doi:10.1016/0014-5793(94)80613-6

Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets

FEBS Lett. 1994 Apr 18;343(1):89-93. doi: 10.1016/0014-5793(94)80613-6.

Authors

R Y Li¹, F Gaits, A Ragab, J M Ragab-Thomas, H Chap

Affiliation

¹ INSERM Unité 326, Phospholipides Membranaires, Signalisation Cellulaire et Lipoprotéines, Université Paul Sabatier, Hôpital Purpan, Toulouse, France.

PMID: 7512933
DOI: 10.1016/0014-5793(94)80613-6

Abstract

A significant protein tyrosine phosphatase (PTP) activity was found to be associated with the cytoskeleton of thrombin-stimulated platelets. Translocation of the enzyme became maximal within 1-2 min of thrombin stimulation and was suppressed by cytochalasin D or upon inhibition of aggregation. Immunoblotting as well as immunoprecipitation revealed that a PTP with two SH2 domains (SH-PTP1) displayed the same behaviour, translocation to the cytoskeleton showing the same time course as that observed for pp60c-src. We conclude that SH-PTP1 might represent a critical enzyme in the complex interplay between the various proteins regulating protein tyrosine phosphorylation in the cytoskeletal matrix.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Biological Transport
Blood Platelets / drug effects*
Blood Platelets / enzymology
Cytoskeleton / enzymology*
Humans
In Vitro Techniques
Protein Tyrosine Phosphatases / metabolism*
Proto-Oncogene Proteins pp60(c-src) / metabolism
Thrombin / pharmacology*

Substances

Proto-Oncogene Proteins pp60(c-src)
Protein Tyrosine Phosphatases
Thrombin