| http://purl.uniprot.org/citations/16014375 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16014375 | http://www.w3.org/2000/01/rdf-schema#comment | "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 alphaVbeta3 integrin. It involves translocation (i.e. activation) of PKCalpha from the cytosol to the membrane and/or the Triton X-100-insoluble subcellular fractions, with recruitment into a complex with alphaVbeta3 integrin, growth factor receptor-bound protein (Grb2), focal adhesion kinase (FAK) in CHO cells and proline-rich tyrosine kinase (PYK2) in osteoclasts. Engagement of alphavbeta3 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, PKCalpha 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 PKCalpha in the same molecular complex. The alphaVbeta3/PKCalpha 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,N',N'-tetraaceticacidtetra (acetoxymethyl) ester (BAPTA-AM) also inhibited PKCalpha translocation and ERK1/2 phosphorylation. Functional studies showed that alphaVbeta3 integrin-activated PKCalpha 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 alphaVbeta3 integrin engagement."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.02436"xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/author | "Baron R."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/author | "Orru L."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/author | "Teti A."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/author | "Rucci N."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/author | "Millimaggi D."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/author | "DiGiacinto C."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/pages | "3263-3275"xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/title | "A novel protein kinase C alpha-dependent signal to ERK1/2 activated by alphaVbeta3 integrin in osteoclasts and in Chinese hamster ovary (CHO) cells."xsd:string |
| http://purl.uniprot.org/citations/16014375 | http://purl.uniprot.org/core/volume | "118"xsd:string |
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