{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Meyers CMG"],"funding":["NIAMS NIH HHS"],"pagination":["116393"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9035101"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["159"],"pubmed_abstract":["Protein kinase D (PRKD) family kinases are required for formation and function of osteoclasts. However, the substrates of PRKD in osteoclasts are unknown. To identify PRKD-dependent protein phosphorylation in osteoclasts, we performed a quantitative LC-MS/MS phosphoproteomics screen for proteins showing differential phosphorylation in osteoclasts after treatment with the PRKD inhibitor CRT0066101. We identified 757 phosphopeptides showing significant changes following PRKD inhibition. Among the changes, we found a group of 13 proteins showing decreased phosphorylation at PRKD consensus phosphorylation motifs. This group includes histone deacetylase 5 (HDAC5), which is a previously validated PRKD target. Considering this known interaction, work suggesting HDACs may be important regulators o"],"journal":["Bone"],"pubmed_title":["Histone deacetylase 5 is a phosphorylation substrate of protein kinase D in osteoclasts."],"pmcid":["PMC9035101"],"funding_grant_id":["R01 AR061352"],"pubmed_authors":["Meyers CMG","Faulkner B","Cohn JM","Burciaga SD","Kazemi P","Mansky KC","Jensen ED"],"additional_accession":[]},"is_claimable":false,"name":"Histone deacetylase 5 is a phosphorylation substrate of protein kinase D in osteoclasts.","description":"Protein kinase D (PRKD) family kinases are required for formation and function of osteoclasts. However, the substrates of PRKD in osteoclasts are unknown. To identify PRKD-dependent protein phosphorylation in osteoclasts, we performed a quantitative LC-MS/MS phosphoproteomics screen for proteins showing differential phosphorylation in osteoclasts after treatment with the PRKD inhibitor CRT0066101. We identified 757 phosphopeptides showing significant changes following PRKD inhibition. Among the changes, we found a group of 13 proteins showing decreased phosphorylation at PRKD consensus phosphorylation motifs. This group includes histone deacetylase 5 (HDAC5), which is a previously validated PRKD target. Considering this known interaction, work suggesting HDACs may be important regulators o","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2025-04-26T23:02:20.15Z","creation":"2025-04-06T17:24:21.032Z"},"accession":"S-EPMC9035101","cross_references":{"pubmed":["35318161"],"doi":["10.1016/j.bone.2022.116393"]}}