{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gong J"],"funding":["NHLBI NIH HHS"],"pagination":["311-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5022567"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["473(3)"],"pubmed_abstract":["Protein kinase C-δ (PKCδ) is a signalling kinase that regulates many cellular responses. Although most studies focus on allosteric mechanisms that activate PKCδ at membranes, PKCδ also is controlled via multi-site phosphorylation [Gong et al. (2015) Mol. Cell. Biol. 35: , 1727-1740]. The present study uses MS-based methods to identify PKCδ phosphorylation at Thr(50) and Ser(645) (in resting and PMA-treated cardiomyocytes) as well as Thr(37), Thr(38), Ser(130), Thr(164), Thr(211), Thr(215), Ser(218), Thr(295), Ser(299) and Thr(656) (as sites that increase with PMA). We focused on the consequences of phosphorylation at Ser(130) and Thr(141) (sites just N-terminal to the pseudosubstrate domain). We show that S130D and T141E substitutions co-operate to increase PKCδ's basal lipid-independent a"],"journal":["The Biochemical journal"],"pubmed_title":["A novel phosphorylation site at Ser130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ."],"pmcid":["PMC5022567"],"funding_grant_id":["R01 HL123061","R01 HL77860","HL123061","HV-10-05","R01 HL077860"],"pubmed_authors":["Steinberg SF","Van Eyk JE","Gong J","Holewinski RJ"],"additional_accession":[]},"is_claimable":false,"name":"A novel phosphorylation site at Ser130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ.","description":"Protein kinase C-δ (PKCδ) is a signalling kinase that regulates many cellular responses. Although most studies focus on allosteric mechanisms that activate PKCδ at membranes, PKCδ also is controlled via multi-site phosphorylation [Gong et al. (2015) Mol. Cell. Biol. 35: , 1727-1740]. The present study uses MS-based methods to identify PKCδ phosphorylation at Thr(50) and Ser(645) (in resting and PMA-treated cardiomyocytes) as well as Thr(37), Thr(38), Ser(130), Thr(164), Thr(211), Thr(215), Ser(218), Thr(295), Ser(299) and Thr(656) (as sites that increase with PMA). We focused on the consequences of phosphorylation at Ser(130) and Thr(141) (sites just N-terminal to the pseudosubstrate domain). We show that S130D and T141E substitutions co-operate to increase PKCδ's basal lipid-independent a","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Feb","modification":"2025-04-25T23:59:35.469Z","creation":"2019-06-06T16:20:34Z"},"accession":"S-EPMC5022567","cross_references":{"pubmed":["26546672"],"doi":["10.1042/bj20150812","10.1042/BJ20150812"]}}