PLC beta 3 Gq: Difference between revisions

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New page: ==Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q== <StructureSection load='3ohm' size='340' side='right' caption='Caption for this structure' scene=''> This is ...
 
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==Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q==
==Unique bidirectional interactions of Phospholipase C beta 3 with G alpha Q==
<StructureSection load='3ohm' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='3ohm' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''PLC beta 3 Gq'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
== Function ==
== Disease ==
== Relevance ==


== Introduction ==
Phospholipase C (PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate [IP2] to the second messengers inositol 1,4,5-trisphosphate [IP3] and diacylglycerol [DAG] in an essential step for the physiological action of many hormones, neurotransmitters, growth factors, and other extracellular stimuli. These cascades use signaling complexes consisting of G alpha subunits of the Gq family of heterotrimeric guanine nucleotide–binding proteins (G proteins) and PLC-beta isozymes (β1-4). Agonist-stimulated receptors increase exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) on Gαq. GTP-bound Gαq engages and activates PLC- β3, and PLC- β3 increases up to three orders of magnitude the rate of hydrolysis of GTP by its activating G protein. This is a unique mechanism when the PLC-β3 enzyme has the ability to terminate the Gαq protein signal in addition to being activated by it.<ref>PMID:20966218</ref> <ref>PMID:23880553</ref>
== Structural highlights ==
== Structural highlights ==