Activation of PLC beta-1

Stable Identifier
R-BTA-374858
Type
Reaction [binding]
Species
Bos taurus
Compartment
cytosol, plasma membrane
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Activation of PLC beta-1
The active form of G protein alpha subunit q (Gq-alpha) was found to activate phospholipase C beta-1 (PLC-beta1), in investigations using bovine membranes. Subsequently, all 4 human isoforms have been shown to be activated by Gq, though activation of PLCbeta-4 is limited. In recombinant assays, several activated rat G alpha q family members were found to stimulate human PLC-beta isoforms with the same rank order of decreasing potency. PLC-beta1 stimulation was slightly more than for PLC-beta3; PLC-beta3 stimulation was 10-fold greater than for beta-2. PLC-beta2 is expressed specifically in hematopoietic cells. PLC-beta acts directly on Gq to accelerate hydrolysis of bound GTP, thus PLC-betas are GTPase activating proteins (GAPs). The crystal structure of the C-terminal region from Turkey PLC-beta, revealed a novel fold composed almost entirely of three long helices forming a coiled-coil that dimerizes along its long axis in an antiparallel orientation. The extent of the dimer interface and gel exclusion chromatography data suggest that PLC-betas are functionally dimeric.
Literature References
Participants
Input
Output
Orthologous Events
Activation of PLC beta-1/4 (Homo sapiens)
PLC beta is activated by G alpha (q) (Homo sapiens)
Authored
Le Novere, N  (2004-03-31)
Jassal, B  (2004-03-31)
Reviewed
Akkerman, JW  (2009-06-03)
Created
Jassal, B  (2008-08-05)
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