http://purl.uniprot.org/citations/19592646 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19592646 | http://www.w3.org/2000/01/rdf-schema#comment | "The capacity of the osteoclast (OC) to resorb bone is dictated by cytoskeletal organization, which in turn emanates from signals derived from the alpha(v)beta(3) integrin and c-Fms. Syk is key to these signals and, in other cells, this tyrosine kinase exerts its effects via intermediaries including the SLP adaptors, SLP-76 and BLNK (B cell linker). Thus, we asked whether these two SLP proteins regulate OC function. We find BLNK-deficient OCs are normal, whereas cytoskeletal organization of those lacking SLP-76 is delayed, thus modestly reducing bone resorption in vitro. Cytoskeletal organization and bone resorption are more profoundly arrested in cultured OCs deficient in BLNK and SLP-76 double knockout (DKO) phenotypes. In contrast, stimulated bone resorption in vivo is inhibited approximately 40% in either SLP-76(-/-) or DKO mice. This observation, taken with the fact that DKO OCs are rescued by retroviral transduction of only SLP-76, indicates that SLP-76 is the dominant SLP family member in the resorptive process. We also find SLP-76 is phosphorylated in a Syk-dependent manner. Furthermore, in the absence of the adaptor protein, integrin-mediated phosphorylation of Vav3, the OC cytoskeleton-organizing guanine nucleotide exchange factor, is abrogated. In keeping with a central role of SLP-76/Vav3 association in osteoclastic resorption, retroviral transduction of SLP-76, in which the Vav binding site is disrupted (3YF), fails to normalize the cytoskeleton of DKO OCs and the resorptive capacity of the cells. Finally, c-Fms-activated Syk also exerts its OC cytoskeleton-organizing effect in a SLP-76/Vav3-dependent manner."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.0804206"xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/author | "Zou W."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/author | "Ross F.P."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/author | "Teitelbaum S.L."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/author | "Maltzman J.S."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/author | "Reeve J.L."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/pages | "1804-1812"xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/title | "SLP-76 couples Syk to the osteoclast cytoskeleton."xsd:string |
http://purl.uniprot.org/citations/19592646 | http://purl.uniprot.org/core/volume | "183"xsd:string |
http://purl.uniprot.org/citations/19592646 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19592646 |
http://purl.uniprot.org/citations/19592646 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19592646 |
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http://purl.uniprot.org/uniprot/#_D3YWR2-mappedCitation-19592646 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19592646 |
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http://purl.uniprot.org/uniprot/#_P13747-mappedCitation-19592646 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19592646 |