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Article

Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations.

eLife - 31 Dec 2019

Hajicek Nicole, Keith Nicholas C, Siraliev-Perez Edhriz, Temple Brenda Rs, Huang Weigang, Zhang Qisheng, Harden T Kendall, Sondek John

Abstract excerpt

Direct activation of the human phospholipase C-γ isozymes (PLC-γ1, -γ2) by tyrosine phosphorylation is fundamental to the control of diverse biological processes, including chemotaxis, platelet aggregation, and adaptive immunity. In turn, aberrant activation of PLC-γ1 and PLC-γ2 is implicated in inflammation, autoimmunity, and cancer. Although structures of isolated domains from PLC-γ isozymes are available,...

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Identifiers

PMID: 31889510
DOI: 10.7554/eLife.51700
PMCID: PMC7004563

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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