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Biochemical studies of membrane proteins.
Reference
BBS/B/01812
Principal Investigator / Supervisor
Professor Peter Cullen
Co-Investigators /
Co-Supervisors
Institution
University of Bristol
Department
Biochemistry
Funding type
Research
Value (£)
187,743
Status
Completed
Type
Research Grant
Start date
01/09/2004
End date
31/08/2007
Duration
36 months
Abstract
Ras proteins function as binary switches cycling between inactive GDP-and active GTP-bound forms. These proteins transduce signals from cell surface receptors into the cytoplasm via specific effector pathways and have achieved notoriety as oncogenes. Oncogenic Ras proteins, which are locked in the active state as a result of being insensitive to inactivation catalysed by Ras GTPase-activating proteins (RasGAPs), are constitutively active in transforming mammalian cells (20 per cent of human tumours contain activating Ras mutations). Here we address how the ubiquitious phosphoinositide regulated RasGAPs, GAP1IP4BP and GAP1m, coordinate the regulation of Ras GTPases during receptor activation.
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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