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• W2201539761 abstract "ABSTRACT The non-receptor tyrosine kinase Src was shown to be essential for osteoclast function in vivo. We have previously reported that engagement of αvβ3 integrin in osteoclasts induces tyrosine phosphorylation and activation of the adhesion kinase PYK2 and the adaptor protein p130Cas in a Src-dependent manner. The objective of this study was to analyse the role of c-Src in the αvβ3 integrin-dependent recruitment of signalling and cytoskeletal molecules in osteoclasts during bone resorption. Using prefusion osteoclasts (pOCs) obtained from cocultures of osteoblasts and spleen cells isolated from Src−/− mice or their normal littermates, we found: (1) similar expression levels and ligand binding affinities of αvβ3 integrins in Src−/− and Src+/? pOCs, (2) reduced adhesion and spreading of Src−/− pOCs, (3) defective organisation of the microfilament proteins, F-actin, vinculin and paxillin, and of PYK2 and p130Cas in the sealing zone of Src−/− OCLs, and (4) hyperclustering of αvβ3 integrins together with microfilament and signalling proteins in the basal membrane of Src-deficient OCLs. In normal OCLs, the tyrosine kinase inhibitor tyrphostin A9 inhibits actin ring formation, bone resorption and tyrosine phosphorylation of several proteins, including c-Src. Furthermore, tyrphostin A9 induced similar hyperclustering of αvβ3 integrins in osteoclasts as observed in Src−/− OCLs. Taken together, these findings suggest that normal localisation of αvβ3 and recruitment of its downstream effectors to the appropriate compartments of the osteoclast during resorption depend on Src kinase activity." @default.
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• W2201539761 date "2001-01-01" @default.
• W2201539761 modified "2023-10-14" @default.
• W2201539761 title "Abnormal localisation and hyperclustering of αVβ3 integrins and associated proteins in Src-deficient or tyrphostin A9-treated osteoclasts" @default.
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• W2201539761 doi "https://doi.org/10.1242/jcs.114.1.149" @default.
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