Source:http://www.reactome.org/biopax/48887BiochemicalReaction3546
| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
Authored: Le Novere, N, Jassal, B, 2004-03-31 12:22:05,
Edited: Jassal, B, 2008-11-06 10:17:49,
Reviewed: Castagnoli, L, 2008-11-06 12:55:54,
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.
|
| biopax3:xref | |
| biopax3:dataSource | |
| biopax3:displayName |
Activation of PLC beta-1/4
|
| biopax3:left | |
| biopax3:right |