ArticleNature structural & molecular biology2011
An autoinhibitory helix in the C-terminal region of phospholipase C-β mediates Gαq activation.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Article
- Small peptides derived from the autoinhibitory XY linker of phospholipase C-β isoforms inhibit enzyme activity and reduce inflammation.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2026Article
- Structural insights into Phospholipase Cε activity and regulation.The Journal of biological chemistry · 2026Review
- An integrated mechanism of GProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A molecular mechanism to diversify CaNature communications · 2024Article
- The mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Molecular regulation of PLCβ signaling.Methods in enzymology · 2023Review
- Control of GαScience advances · 2022Article
- Expression of the C-Terminal Domain of Phospholipase Cβ3 Inhibits Signaling via Gαq-Coupled Receptors and Transient Receptor Potential Channels.International journal of molecular sciences · 2022Article
- Characterization of the membrane interactions of phospholipase Cγ reveals key features of the active enzyme.Science advances · 2022Article
- Uveal melanoma-associated mutations in PLCβ4 are constitutively activating and promote melanocyte proliferation and tumorigenesis.Science signaling · 2021Article
- From spikes to intercellular waves: Tuning intercellular calcium signaling dynamics modulates organ size control.PLoS computational biology · 2021Article
- Structure and regulation of phospholipase Cβ and ε at the membrane.Chemistry and physics of lipids · 2021Review
- Structure of phospholipase Cε reveals an integrated RA1 domain and previously unidentified regulatory elements.Communications biology · 2020Article
- Activation of Phospholipase C β by Gβγ and GαStructure (London, England : 1993) · 2020Article
- Crystal structure of human PLD1 provides insight into activation by PI(4,5)PNature chemical biology · 2020Article
- Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations.eLife · 2019Article
- Intramolecular electrostatic interactions contribute to phospholipase Cβ3 autoinhibition.Cellular signalling · 2019Article
- GαBiochemistry · 2019Article
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Authors and funding
9 authors.
Funding
Abstract
The enzyme phospholipase C-β (PLCβ) is a crucial regulator of intracellular calcium levels whose activity is controlled by heptahelical receptors that couple to members of the Gq family of heterotrimeric G proteins. We have determined atomic structures of two invertebrate homologs of PLCβ (PLC21) from cephalopod retina and identified a helix from the C-terminal regulatory region that interacts with a conserved surface of the catalytic core of the enzyme. Mutations designed to disrupt the analogous interaction in human PLCβ3 considerably increase basal activity and diminish stimulation by Gαq. Gαq binding requires displacement of the autoinhibitory helix from the catalytic core, thus providing an allosteric mechanism for activation of PLCβ.
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