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The role of calcium binding proteins in regulating inositol 1,4,5-triphosphate receptors

ReferenceBBS/E/B/0000L096
Principal Investigator / Supervisor Dr Martin Bootman
Co-Investigators /
Co-Supervisors
Institution Babraham Institute
DepartmentBabraham Institute Department
Funding typeResearch
Value (£) 107,839
StatusCompleted
TypeInstitute Project
Start date 01/01/2004
End date 31/12/2007
Duration48 months

Abstract

Calcium (Ca2+) is a universal intracellular messenger controlling a diverse array of cellular activities. In most cells, Ca2+ has its major signalling function when it is elevated in the cytosolic compartment. From there it can also diffuse into the nucleus or be sequestered by organelles such as mitochondria. Cells generally utilize both extracellular and intracellular Ca2+ sources to generate physiological signals. The major store of Ca2+ within cells is the endoplasmic or sarcoplasmic reticulum (E/SR). Ca2+ can be released from this pool by a variety of intracellular messengers. One of the most prominent mechanisms for releasing Ca2+ stores is via the phosphoinositide pathway, whereby hormonal/ neurotransmitter stimulation of cells activates the production of inositol 1,4,5-trisphosphate (InsP3) production. InsP3 binds to specific ligand-gated channels (InsP3Rs) on the surface of the E/SR and causes the flux of Ca2+ from the lumen of the stores to the cytoplasm. We are interested in proteins that modulate the activity of InsP3Rs. We have demonstrated that a family of neuronally-expressed `Calcium Binding Proteins¿ (CaBPs) directly interact with InsP3Rs and regulate their ability to release Ca2+.

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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