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Regulation of protein kinase c-epsilon function in fibroblasts by a ser729 phosphatase b-cop and myosin
Reference
C14680
Principal Investigator / Supervisor
Dr Martin Rumsby
Co-Investigators /
Co-Supervisors
Dr Karen England
Institution
University of York
Department
Biology
Funding type
Research
Value (£)
217,716
Status
Completed
Type
Research Grant
Start date
02/07/2001
End date
01/04/2005
Duration
45 months
Abstract
Our results indicate that phosphorylation of Ser729 in protein kinase C-epsilon in cells specifies a perinuclear localisation: without this phosphate the kinase is cytosolic. This study aims to characterise the protein phosphatase involved in Ser729 dephosphorylation, the signals that activate it on cell passage and that inhibit it as cells grow to confluence. We will establish precisely what organelle PKE-e is associated with at the perinuclear site. Mutagenicity studies will reveal how phosphorylation at Ser729 specifies interactions with binding proteins, b-COP and myosin while GFP-conjugated PKC-e constructs will define how phosphorylation determines intracellular localisation. This research will extend knowledge on PKC-e function.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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