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Title activates hydrolysis by recruiting and orienting on the membrane surface.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 20, Page e2301121120, Year 2023
Publish dateMay 16, 2023
AuthorsMaria E Falzone / Roderick MacKinnon /
PubMed Abstract catalyze the hydrolysis of phosphatidylinositol 4, 5-bisphosphate [Formula: see text] into [Formula: see text] [Formula: see text] and [Formula: see text]  [Formula: see text]. [Formula: see text] ... catalyze the hydrolysis of phosphatidylinositol 4, 5-bisphosphate [Formula: see text] into [Formula: see text] [Formula: see text] and [Formula: see text]  [Formula: see text]. [Formula: see text] regulates the activity of many membrane proteins, while and lead to increased intracellular Ca levels and activate protein kinase C, respectively. are regulated by G protein-coupled receptors through direct interaction with [Formula: see text] and [Formula: see text] and are aqueous-soluble enzymes that must bind to the cell membrane to act on their lipid substrate. This study addresses the mechanism by which [Formula: see text] activates 3. We show that 3 functions as a slow Michaelis-Menten enzyme ( [Formula: see text] ) on membrane surfaces. We used membrane partitioning experiments to study the solution-membrane localization equilibrium of 3. Its partition coefficient is such that only a small quantity of 3 exists in the membrane in the absence of [Formula: see text] . When [Formula: see text] is present, equilibrium binding on the membrane surface increases 3 in the membrane, increasing [Formula: see text] in proportion. Atomic structures on membrane vesicle surfaces show that two [Formula: see text] anchor 3 with its catalytic site oriented toward the membrane surface. Taken together, the enzyme kinetic, membrane partitioning, and structural data show that [Formula: see text] activates by increasing its concentration on the membrane surface and orienting its catalytic core to engage [Formula: see text] . This principle of activation explains rapid stimulated catalysis with low background activity, which is essential to the biological processes mediated by [Formula: see text], and .
External linksProc Natl Acad Sci U S A / PubMed:37172014 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.6 Å
Structure data

28266

8emv

EMDB-28266, PDB-8emv:
Phospholipase C beta 3 (PLCb3) in solution
Method: EM (single particle) / Resolution: 3.6 Å

28267

8emw

EMDB-28267, PDB-8emw:
Phospholipase C beta 3 (PLCb3) in complex with Gbg on liposomes
Method: EM (single particle) / Resolution: 3.5 Å

28268

8emx

EMDB-28268, PDB-8emx:
Phospholipase C beta 3 (PLCb3) in complex with Gbg on lipid nanodiscs
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / PIP2 degradation / IP3 production / DAG production / G protein signaling

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