PLC beta 3 Gq: Difference between revisions

No edit summary
No edit summary
Line 1: Line 1:
==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=''>
== Introduction ==
== 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 many physiological cascades. When the receptor is stimulated by ligand of some kind it increase exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) on Gαq. GTP-bound Gαq 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>
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 many physiological cascades. When the receptor is stimulated by ligand of some kind it increase exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) on Gαq. GTP-bound Gαq 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 ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Shir Navot, Michal Harel, Joel L. Sussman