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TitleGβγ engages PLCβ3 at multiple sites to reorient and facilitate its activation.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateJan 14, 2026
AuthorsIsaac J Fisher / Kanishka Senarath / Kennedy Outlaw / Kaushik Muralidharan / Elisabeth E Garland-Kuntz / Michelle Van Camp / Tommy Komay / Asuka Inoue / Eva Kostenis / Nevin A Lambert / Angeline M Lyon /
PubMed AbstractPhospholipase C β (PLCβ) enzymes are activated by heterotrimeric G protein subunits, increasing hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) at the plasma membrane. All four human ...Phospholipase C β (PLCβ) enzymes are activated by heterotrimeric G protein subunits, increasing hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) at the plasma membrane. All four human PLCβ isoforms (PLCβ1-4) are activated by Gα, while PLCβ1-3 are activated to varying extents by Gβγ. The binding sites for Gα on PLCβ are well-established and much has been learned about its mechanism of activation, but comparatively little is known about Gβγ-dependent activation. In this work, we used cryo-electron microscopy (cryo-EM) single particle analysis (SPA), functional assays, and bioluminescence resonance energy transfer (BRET) to investigate how Gβγ interacts with PLCβ3 in concert with activated Gα to regulate phospholipase activity. Gβγ heterodimers bind multiple surfaces of PLCβ3 to promote activation but alone do not recruit the enzyme to the plasma membrane. Instead, Gβγ facilitates activation by Gα, most likely by reorienting the phospholipase catalytic site at the membrane to maximize PIP2 hydrolysis and downstream Ca release. Cell-based functional assays demonstrate that Gβγ is required for maximal PLCβ3 activation even when G heterotrimers are the sole source of Gβγ. Together, these findings demonstrate that Gβγ acts as a critical positive allosteric modulator that regularly acts in concert with Gα to activate PLCβ3 at the plasma membrane.
External linksbioRxiv / PubMed:41648476 / PubMed Central
MethodsEM (single particle)
Resolution4.4 - 7.0 Å
Structure data

72655

9y7h

EMDB-72655, PDB-9y7h:
Gb1g2 crosslinked to PLCb3
Method: EM (single particle) / Resolution: 4.4 Å

72732

9yao

EMDB-72732, PDB-9yao:
Gbg crosslinked to PLCb3 - second conformation
Method: EM (single particle) / Resolution: 7.0 Å

72733

9yap

EMDB-72733, PDB-9yap:
Gbg crosslinked to PLCb3 - second conformation
Method: EM (single particle) / Resolution: 4.5 Å

Chemicals

ChemComp-ME7:
1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione)

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
KeywordsSIGNALING PROTEIN / heterotrimeric G protein / phospholipase / lipase / calcium signaling / G protein

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