Proteomics

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A novel phosphorylation site at Ser130 adjacent to the pseudosubstrate domain regulates protein kinase C-δ activity


ABSTRACT: Protein kinase C over-expressed into rat neonatal myocytes were lysed in 8M Urea, 0.1% SDS and trypsin digested. Peptides were fractionated by SPE-SCX and enriched by TiO2. Phosphopeptides were analyzed by LC/MS on a Thermo LTQ Elite Orbitrap. Raw files were searched using Sorcerer-Sequest and post search analysis and processing was done with Scaffold and Scaffold PTM.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Cell Culture, Fetal Cardiomyocyte

SUBMITTER: Ronald Holewinski  

LAB HEAD: Jennifer Van Eyk

PROVIDER: PXD002536 | Pride | 2018-10-24

REPOSITORIES: Pride

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A novel phosphorylation site at Ser130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ.

Gong Jianli J   Holewinski Ronald J RJ   Van Eyk Jennifer E JE   Steinberg Susan F SF  

The Biochemical journal 20151106 3


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(2  ...[more]

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