Award details

Functional characterisation of BiP subdomains to unravel its function in protein synthesis folding and quality control by the ER

ReferenceC10150
Principal Investigator / Supervisor Dr Jurgen Denecke
Co-Investigators /
Co-Supervisors
Institution University of Leeds
DepartmentPlant Biochemistry & Biotechnology
Funding typeResearch
Value (£) 175,124
StatusCompleted
TypeResearch Grant
Start date 01/02/1999
End date 01/11/2003
Duration57 months

Abstract

The aim of this study is to provide insight into the domains of BiP that are important for its function in the ER. The work proposed is based on three very important findings which we want to extend systematically: 1) We have obtained the first evidence for a BiP-calreticulin complex. The finding is exciting as its shows that ER chaperones act in large protein complexes, and further work is needed to characterise the complex. 2) We have also established the first in vivo BiP activity assay in which alpha-amylase synthesis during ER stress is restored by BiP co-expression. This assay will allow us to generate functional mutants and test if they are still capable of binding to calreticulin or malfolded proteins. 3) We have shown that BiP is transported to the vacuoles when overproduced. We want to identify the vacuolar targeting signal and test if vacuolar transport of BiP is induced when BiP is bound to a malfolded protein. This would establish if the vacuole is part of the quality control machinery

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 X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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