ArticleThe Biochemical journal2001
Involvement of Hic-5 in platelet activation: integrin alphaIIbbeta3-dependent tyrosine phosphorylation and association with proline-rich tyrosine kinase 2.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Paxillin actions in the nucleus.Steroids · 2018Review
- Hic-5 Regulates Actin Cytoskeletal Reorganization and Expression of Fibrogenic Markers and Myocilin in Trabecular Meshwork Cells.Investigative ophthalmology & visual science · 2015Article
- Pro32Pro33 mutations in the integrin β3 PSI domain result in αIIbβ3 priming and enhanced adhesion: reversal of the hypercoagulability phenotype by the Src inhibitor SKI-606.Molecular pharmacology · 2014Article
- Paxillin is an intrinsic negative regulator of platelet activation in mice.Thrombosis journal · 2014Article
- Cell-matrix adhesion of podocytes in physiology and disease.Nature reviews. Nephrology · 2013Review
- HIC-5: A Mobile Molecular Scaffold Regulating the Anchorage Dependence of Cell Growth.International journal of cell biology · 2012Article
- What is vinculin needed for in platelets?Journal of thrombosis and haemostasis : JTH · 2010Article
- Hic-5 is required for fetal gene expression and cytoskeletal organization of neonatal cardiac myocytes.Journal of molecular and cellular cardiology · 2009Article
- Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets.The Biochemical journal · 2007Article
- Serotonin-, protein kinase C-, and Hic-5-associated redistribution of the platelet serotonin transporter.The Journal of biological chemistry · 2006Article
- Subcellular targeting of oxidants during endothelial cell migration.The Journal of cell biology · 2005Article
- The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hic-5 and paxillin, members of the LIM protein family, have been shown to be localized in focal adhesion and to have a role in integrin-mediated signalling. In the present study we examined the involvement of Hic-5 in human platelet activation: platelets express Hic-5 but not paxillin, whereas human umbilical-vein vascular endothelial cells and MEG-01 cells express mainly paxillin. When platelets were stimulated with thrombin, collagen or the stable thromboxane A(2) analogue U46619, Hic-5 was markedly tyrosine-phosphorylated, in a manner dependent on integrin alphaIIbbeta3-mediated aggregation. In addition, direct activation of protein kinase C with PMA resulted in tyrosine phosphorylation of Hic-5 only when platelets were fully aggregated with the exogenous addition of fibrinogen. Furthermore, PMA-induced Hic-5 tyrosine phosphorylation was also observed when platelets adhered to immobilized fibrinogen. In studies on immunoprecipitation and immunodepletion, Hic-5 seemed to associate with proline-rich tyrosine kinase 2 (Pyk2) but only marginally with focal adhesion kinase. When platelets were stimulated with thrombin, both Hic-5 and Pyk2 translocated to the cytoskeleton from the cytosol and membrane fractions in a manner dependent on alphaIIbbeta3-mediated aggregation. Finally, on stimulation with PMA, Hic-5, as well as Pyk2, translocated to the cell periphery, where a meshwork of actin filaments assembled after adhesion to immobilized fibrinogen. Our results suggest that Hic-5 might be important in platelet aggregation and adhesion, in a manner dependent on alphaIIbbeta3-mediated outside-in signalling, through association with Pyk2.
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