Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets.
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.
Li
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INSERM Unité 326, Phospholipides Membranaires, Signalisation Cellulaire et Lipoprotéines, Université Paul Sabatier, Hôpital Purpan, Toulouse, France.
Gaits
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Ragab
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Ragab-Thomas
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JM
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D001692:Biological Transport; D001792:Blood Platelets / Q000187:drug effects* / Q000201:enzymology; D003599:Cytoskeleton / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D016392:Proto-Oncogene Proteins pp60(c-src) / Q000378:metabolism; D013917:Thrombin / Q000494:pharmacology*
D016392:Proto-Oncogene Proteins pp60(c-src); D017027:Protein Tyrosine Phosphatases; D013917:Thrombin