Translocation of an SH2‐containing protein tyrosine phosphatase (SH‐PTP1) to the cytoskeleton of thrombin‐activated platelets
- 18 April 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 343 (1), 89-93
- https://doi.org/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 pp60 c-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.Keywords
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