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A role for Pin1 in MAPK-dependent stabilisation of AP-1 proteins?
Reference
BBS/B/01111
Principal Investigator / Supervisor
Dr Simon Cook
Co-Investigators /
Co-Supervisors
Institution
Babraham Institute
Department
Babraham Institute Department
Funding type
Research
Value (£)
194,973
Status
Completed
Type
Research Grant
Start date
29/10/2004
End date
28/04/2008
Duration
42 months
Abstract
Pin1, a peptidyl prolyl isomerase (PPI), regulates protein conformation by binding to phosphorylated S-P or T-P motifs via its WW domain and catalysing their cis-trans isomerisation. Phosphorylation of c-Fos, Fra-1 and Fra-2 by ERK, and c-Jun by JNK, inhibits their proteasomal degradation. ERK and JNK are proline-directed protein kinases that phosphorylate S-P or T-P motifs. We have found that c-Fos, Fra-1 and Fra-2 bind to Pin1 via its WW domain in an ERK- and phosphorylation-dependent fashion. The same applies for c-Jun and JNK. This project will identify the sites of ERK-dependent phosphorylation which serve as Pin1 binding sites and the role of Pin1 in regulating Fos/Fra/c-Jun stability, DNA binding and AP-1 activity.
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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