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Defining the role of a nuclear/cytoplasmic shuttling protein involved in signal transduction by use of the proteomics
Reference
BBS/B/02681
Principal Investigator / Supervisor
Professor Anthony David Whetton
Co-Investigators /
Co-Supervisors
Professor Simon James Gaskell
Institution
The University of Manchester
Department
Medical and Human Sciences
Funding type
Research
Value (£)
226,930
Status
Completed
Type
Research Grant
Start date
01/01/2005
End date
31/05/2008
Duration
41 months
Abstract
Fms Interacting Protein, FMIP, interacts with a receptor tyrosine kinase, Fms, at the plasma membrane but is found predominantly in the nucleus. Protein kinases C-mediated phosphorylation influences subcellular localisation. FMIP can suppress transactivation by a transcription factor, C/EBP, and the knockout mouse dies within 3 days of conception. Our FMIP monoclonal antibodies have enabled us to show that FMIP levels are regulated post-translationally, falling precipitously as multipotent hematopoietic cells commit to differentiation. Our aim is to characterise the binding partners of FMIP using a proteomic approach and assess phosphorylation effects on this process via site directed mutagenesis. We will also investigate FMIP proteolysis. Our objective is to understand the role of this novel protein more fully using proteomics.
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
Proteomics and Cell Function (PCF) [2003-2004]
Funding Scheme
X – not Funded via a specific Funding Scheme
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