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Molecular basis of PP2A regulation through methylation-dependent assembly of heterotrimers
Reference
B18126
Principal Investigator / Supervisor
Professor Snezana Djordjevic
Co-Investigators /
Co-Supervisors
Institution
University College London
Department
Structural Molecular Biology
Funding type
Research
Value (£)
175,564
Status
Completed
Type
Research Grant
Start date
15/02/2003
End date
15/02/2006
Duration
36 months
Abstract
Protein phosphataste 2A is a ubiquitous enzyme with a range of diverse substrates. Substrate specificity and subcellular localisation is determined by more than 20 different regulatory subunits. Binding of regulatory subunits and heterotrimeric formation is dependent on carboxymethylation of the conserved terminal leucine residue of the catalytic subunit. This covalent modification is catalysed by the specific S-adenosylmethinine dependent methyltransferase while the reverse reaction of methylester hydrolysis is carried out by the unique methylesterase. How the two methylation enzymes are regulated is not known. The object of this proposal is to establish the molecular basis of the mechanisms of heterotrimeric assembly by investigating the three-dimensional structures of the methylation enzymes and their respective complexes with the catalytic subunit of PP2A.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
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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