Dissociation of SHP-1 from spinophilin during platelet activation exposes an inhibitory binding site for protein phosphatase-1 (PP1)

We have recently shown that a critical regulatory node in the platelet signaling network lies immediately downstream of platelet receptors for thrombin and TxA2. This node is comprised of a scaffold protein (spinophilin, SPL), a protein tyrosine phosphatase (SHP-1), and either of the two members of...

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Veröffentlicht in:	PloS one 2015-03, Vol.10 (3), p.e0119496-e0119496
Hauptverfasser:	Ma, Peisong, Foote, Darci C, Sinnamon, Andrew J, Brass, Lawrence F
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine diphosphate Animals Binding Sites Biochemistry Blood platelets Blood Platelets - metabolism Blood Platelets - physiology Cell culture Cell cycle Chemical properties CHO Cells Collagen Cricetulus Dissociation G proteins Humans Isoforms Kinases Light Medicine Microfilament Proteins - blood Muscle proteins Myosin Nerve Tissue Proteins - blood Overexpression Pharmacology Phosphatase Phosphatases Phosphoprotein phosphatase Phosphorylation Platelet Activation - physiology Platelets Protein binding Protein phosphatase Protein Tyrosine Phosphatase, Non-Receptor Type 6 - blood Protein-serine/threonine phosphatase Protein-tyrosine-phosphatase Proteins Receptors Receptors, Neuropeptide Y - blood Regulators RGS Proteins - blood Serine SHP-1 protein Signaling Spinophilin Substrates Threonine Threonine phosphatase Thrombin Thrombin - metabolism Tyrosine
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