{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T16:02:40Z","timestamp":1770739360388,"version":"3.49.0"},"reference-count":55,"publisher":"Canadian Science Publishing","issue":"1","license":[{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochem. Cell Biol."],"published-print":{"date-parts":[[2009,2]]},"abstract":"<jats:p> The haemopoietic cell kinase (Hck) plays an important but poorly understood role in coupling chemoattractant stimuli to the actin cytoskeletal rearrangement required for neutrophil polarization and chemotaxis. Here, we show that Hck coimmunoprecipitates with the cytoskeletal regulatory Wiskott\u2013Aldrich syndrome protein (WASp) and mammalian diaphanous-related formin 1 (mDia1) in chemoattractant-stimulated neutrophils, and that the 3 proteins inducibly colocalize with one another at the leading edge of chemotaxing cells. Hck interaction with WASp was found to be mediated by the Hck SH3 domain binding to the WASp proline-rich region, while Hck interaction with mDia1 was indirect but was required for binding to WASp. In contrast to wild-type cells, both WASp- and mDia1-deficient neutrophils showed severe impairment of chemokine-induced Hck membrane translocation and induction of Hck binding to WASp, and Hck activation and WASp tyrosine phosphorylation were impaired in mDia1<jats:sup>\u2212\/\u2212<\/jats:sup> cells. Thus, chemotactic stimulation appears to induce an mDia1\/Hck\/WASp complex required for Hck membrane targeting and for induction of the Hck-mediated WASp tyrosine phosphorylation thought to be required for WASp-driven actin polymerization. These findings reveal that Hck functions in neutrophils to be realized, at least in part, via its interaction with mDia1 and WASp, and identifies the mDia1\/Hck\/WASp axis as a cytoskeletal signaling interface linking tyrosine phosphorylation to chemotactic and, possibly, other actin-based neutrophil responses. <\/jats:p>","DOI":"10.1139\/o08-130","type":"journal-article","created":{"date-parts":[[2009,2,20]],"date-time":"2009-02-20T16:13:18Z","timestamp":1235146398000},"page":"207-216","source":"Crossref","is-referenced-by-count":19,"title":["Src kinase Hck association with the WASp and mDia1 cytoskeletal regulators promotes chemoattractant-induced Hck membrane targeting and activation in neutrophilsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB\u2019s 51st Annual Meeting\u00a0\u2013 Epigenetics and Chromatin Dynamics, and has undergone the Journal\u2019s usual peer review process."],"prefix":"10.1139","volume":"87","author":[{"given":"Yongquan","family":"Shi","sequence":"first","affiliation":[{"name":"Department of Medicine, Immunology, and Molecular and Medical Genetics, University of Toronto, Toronto, ON  M5G\u00a01X5, Canada"},{"name":"Samuel Lunenfeld and Toronto General Hospital Research Institutes, Mount Sinai Hospital, 600 University Avenue, Room 778D, Toronto, ON  M5G\u00a01X5, Canada"},{"name":"Department of Hematology, Xijing Hospital, The Fourth Military Medical University, Xian, Shaanxi, China."},{"name":"Laboratory for Cell Structure & Signal Integration, Van Andel Institute, Grand Rapids, MI 49503, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Baoxia","family":"Dong","sequence":"additional","affiliation":[{"name":"Department of Medicine, Immunology, and Molecular and Medical Genetics, University of Toronto, Toronto, ON  M5G\u00a01X5, Canada"},{"name":"Samuel Lunenfeld and Toronto General Hospital Research 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