| http://purl.uniprot.org/citations/22103330 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22103330 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosphorylation of the BH3 (Bcl-2 homology domain 3)-only protein BAD (Bcl-2/Bcl-X(L)-antagonist, causing cell death) can either directly disrupt its association with the pro-survival proteins Bcl-X(L) and/or Bcl-2, or cause association of BAD with 14-3-3 proteins. In the present study, we further characterize phosphorylation of BAD at Ser170, a unique site with unclear function. We provide further evidence that mutation of Ser170 to a phospho-mimetic aspartic acid residue (S170D) can have a profound inhibitory effect on the pro-apoptosis function of BAD. Furthermore, mutated BAD with an alanine substitution inhibited cell proliferation, slowing progression specifically through S-phase. We identify the kinase responsible for phosphorylation at this site as CaMKII-γ (γ isoform of Ca2+/calmodulin-dependent kinase II), but not the other three isoforms of CaMKII, revealing an extraordinary specificity among these closely related kinases. Furthermore, cytokine treatment increased BAD-Ser170-directed CaMKII-γ activity and phosphorylation of CaMKII-γ at an activating site, and CaMKII activity directed to the BAD-Ser170 site was elevated during S-phase. Treating cells with a selective inhibitor of CaMKII caused apoptosis in cells expressing BAD, but not in cells expressing the BAD-S170D mutant. The present study provides support for BAD-Ser170 phosphorylation playing a key role not only in regulating BAD's pro-apoptotic activity, but also in cell proliferation."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20111256"xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/author | "Cox M.E."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/author | "Duronio V."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/author | "Hojabrpour P."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/author | "Ghaffari M."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/author | "Waissbluth I."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/pages | "139-149"xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/title | "CaMKII-gamma mediates phosphorylation of BAD at Ser170 to regulate cytokine-dependent survival and proliferation."xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://purl.uniprot.org/core/volume | "442"xsd:string |
| http://purl.uniprot.org/citations/22103330 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22103330 |
| http://purl.uniprot.org/citations/22103330 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22103330 |
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