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Defining the role of a nuclear/cytoplasmic shuttling protein involved in signal transduction by use of the proteomics

ReferenceBBS/B/02681
Principal Investigator / Supervisor Professor Anthony David Whetton
Co-Investigators /
Co-Supervisors
Professor Simon James Gaskell
Institution The University of Manchester
DepartmentMedical and Human Sciences
Funding typeResearch
Value (£) 226,930
StatusCompleted
TypeResearch Grant
Start date 01/01/2005
End date 31/05/2008
Duration41 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative Proteomics and Cell Function (PCF) [2003-2004]
Funding SchemeX – not Funded via a specific Funding Scheme
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