PLC beta is activated by G alpha (q)

Stable Identifier
Reaction [binding]
Homo sapiens
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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
PubMed ID Title Journal Year
11753430 A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q

Sondek, J, Waldo, GL, Harden, TK, Singer, AU

Nat Struct Biol 2002
16182515 Cell signalling diversity of the Gqalpha family of heterotrimeric G proteins

Hepler, JR, Hubbard, KB

Cell Signal 2006
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