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Analysing the role of phosphatidylinositol 34.5-trisphosphate in sorting nexin 1 mediated EGF receptor cycling
Reference
C17415
Principal Investigator / Supervisor
Professor Peter Cullen
Co-Investigators /
Co-Supervisors
Professor Harry Mellor
Institution
University of Bristol
Department
Biochemistry
Funding type
Research
Value (£)
220,948
Status
Completed
Type
Research Grant
Start date
01/01/2003
End date
01/01/2006
Duration
36 months
Abstract
Sorting nexins are widely expressed proteins believed to be part of the complex of molecular machinery required for protein trafficking. Sorting nexin 1 (SNX1) - which localises to an undefined intracellular tubular-vesicular compartment - selectively decreases the amount of EGF receptor on the cell surface by enhancing the rate of receptor degradation. To carry out this function SNX1 assembles into a retromer complex. We have shown that the phox homology (PX) domain of SNX1 specifically binds phosphatidylinositol 3,4,5-trisphosphate (PIP3) - evidence suggesting PIP3 may have a signalling function away from the plasma membrane. In this proposal we wish to address the role of PIP3 in the regulation of SNX1- mediated EGF receptor degradation.
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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