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JCS ePress online publication date 12 Jul 2005
doi: 10.1242/jcs.02436

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Research Article

A novel protein kinase C {alpha}-dependent signal to ERK1/2 activated by {alpha}V{beta}3 integrin in osteoclasts and in Chinese hamster ovary (CHO) cells


Nadia Rucci, Claudia DiGiacinto, Luigi Orrù, Danilo Millimaggi, Roland Baron, and Anna Teti*
* Author for correspondence (e-mail: teti{at}univaq.it)

We identified a novel protein kinase C (PKC){alpha}-dependent signal to extracellular signal-regulated kinase (ERK)1/2 in mouse osteoclasts and Chinese hamster ovary (CHO) cells, specifically activated by the {alpha}V{beta}3 integrin. It involves translocation (i.e. activation) of PKC{alpha} from the cytosol to the membrane and/or the Triton X-100-insoluble subcellular fractions, with recruitment into a complex with {alpha}V{beta}3 integrin, growth factor receptor-bound protein (Grb2), focal adhesion kinase (FAK) in CHO cells and proline-rich tyrosine kinase (PYK2) in osteoclasts. Engagement of {alpha}v{beta}3 integrin triggered ERK1/2 phosphorylation, but the underlying molecular mechanism was surprisingly independent of the well known Shc/Ras/Raf-1 cascade, and of phosphorylated MAP/ERK kinase (MEK)1/2, so far the only recognized direct activator of ERK1/2. In contrast, PKC{alpha} was involved in ERK1/2 activation because inhibition of its activity prevented ERK1/2 phosphorylation. The tyrosine kinase c-Src also contributed to ERK1/2 activation, however, it did not interact with PKC{alpha} in the same molecular complex. The {alpha}V{beta}3/PKC{alpha} complex formation was fully dependent upon the intracellular calcium concentration ([Ca2+]i), and the use of the intracellular Ca2+ chelator 1,2-bis(o-amino-phenoxy)ethane-N,N,N9,N9-tetraaceticacidtetra (acetoxy-methyl) ester (BAPTA-AM) also inhibited PKC{alpha} translocation and ERK1/2 phosphorylation. Functional studies showed that {alpha}V{beta}3 integrin-activated PKC{alpha} was involved in cell migration and osteoclast bone resorption, but had no effect on the ability of cells to attach to LM609, suggesting a role in events downstream of {alpha}V{beta}3 integrin engagement.
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