PLC beta 3 Gq: Difference between revisions
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== Introduction == | == Introduction == | ||
Phospholipase C (PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate [ | Phospholipase C beta 3 (PLC-β3) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate [PIP2] 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 in which 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 == | ||
The Gαq subunit consists two domains, one is the GTPase domain and the other is the alpha helical domain. These domains include three regions called <scene name='70/701452/Fig2/ | The Gαq subunit consists two domains, one is the GTPase domain and the other is the alpha helical domain. These domains include three regions called <scene name='70/701452/Fig2/5'>switch regions I-III</scene>. | ||
<scene name='70/701452/Fig1/9'>The PLC- β3 has several domains</scene> consisting of N-terminal PH domain, a series of four EF hands, a catalytic TIM barrel that the X/Y linker connect its two halves and a C2 domain. | <scene name='70/701452/Fig1/9'>The PLC- β3 has several domains</scene> consisting of N-terminal PH domain, a series of four EF hands, a catalytic TIM barrel that the X/Y linker connect its two halves and a C2 domain. | ||