{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T01:14:25Z","timestamp":1780449265076,"version":"3.54.1"},"reference-count":55,"publisher":"Rockefeller University Press","issue":"2","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2001,1,22]]},"abstract":"<jats:p>The macrophage colony stimulating factor (M-CSF) and \u03b1v\u03b23 integrins play critical roles in osteoclast function. This study examines M-CSF\u2013 and adhesion-induced signaling in prefusion osteoclasts (pOCs) derived from Src-deficient and wild-type mice. Src-deficient cells attach to but do not spread on vitronectin (Vn)-coated surfaces and, contrary to wild-type cells, their adhesion does not lead to tyrosine phosphorylation of molecules activated by adhesion, including PYK2, p130Cas, paxillin, and PLC-\u03b3. However, in response to M-CSF, Src\u2212\/\u2212 pOCs spread and migrate on Vn in an \u03b1v\u03b23-dependent manner. Involvement of PLC-\u03b3 activation is suggested by using a PLC inhibitor, U73122, which blocks both adhesion- and M-CSF\u2013mediated cell spreading. Furthermore, in Src\u2212\/\u2212 pOCs M-CSF, together with filamentous actin, causes recruitment of \u03b23 integrin and PLC-\u03b3 to adhesion contacts and induces stable association of \u03b23 integrin with PLC-\u03b3, phosphatidylinositol 3-kinase, and PYK2. Moreover, direct interaction of PYK2 and PLC-\u03b3 can be induced by either adhesion or M-CSF, suggesting that this interaction may enable the formation of integrin-associated complexes. Furthermore, this study suggests that in pOCs PLC-\u03b3 is a common downstream mediator for adhesion and growth factor signals. M-CSF\u2013initiated signaling modulates the \u03b1v\u03b23 integrin-mediated cytoskeletal reorganization in prefusion osteoclasts in the absence of c-Src, possibly via PLC-\u03b3.<\/jats:p>","DOI":"10.1083\/jcb.152.2.361","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:46:23Z","timestamp":1027701983000},"page":"361-374","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":82,"title":["Convergence of \u03b1v\u03b23Integrin\u2013And Macrophage Colony Stimulating Factor\u2013Mediated Signals on Phospholipase C\u03b3 in Prefusion Osteoclasts"],"prefix":"10.1083","volume":"152","author":[{"given":"Ichiro","family":"Nakamura","sequence":"first","affiliation":[{"name":"aDepartment of Bone Biology and Osteoporosis Research, Merck Research Laboratories, West Point, Pennsylvania 19486"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorraine","family":"Lipfert","sequence":"additional","affiliation":[{"name":"aDepartment of Bone Biology and Osteoporosis Research, Merck Research Laboratories, West Point, Pennsylvania 19486"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gideon A.","family":"Rodan","sequence":"additional","affiliation":[{"name":"aDepartment of Bone Biology and Osteoporosis Research, Merck Research Laboratories, West Point, Pennsylvania 19486"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Le T.","family":"Duong","sequence":"additional","affiliation":[{"name":"aDepartment of Bone Biology and Osteoporosis Research, Merck Research Laboratories, West Point, Pennsylvania 19486"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2001,1,22]]},"reference":[{"key":"2023072902534073200_Adelsmanetal1999","doi-asserted-by":"crossref","first-page":"2861","DOI":"10.1091\/mbc.10.9.2861","article-title":"Stimulation of \u03b21-integrin function by epidermal growth factor and heregulin-\u03b2 has distinct requirements for erbB2 but a similar dependence on phosphoinositide 3-OH kinase","volume":"10","author":"Adelsman","year":"1999","journal-title":"Mol. 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