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Article

Cancer-associated mutations in the p85α N-terminal SH2 domain activate a spectrum of receptor tyrosine kinases.

Proceedings of the National Academy of Sciences of the United States of America - 14 Sept 2021

Li Xinran, Lau Amy Y T, Ng Angel S N, Aldehaiman Abdullah, Zhou Yuan, Ng Patrick K S, Arold Stefan T, Cheung Lydia W T

Abstract excerpt

The phosphoinositide 3-kinase regulatory subunit p85α is a key regulator of kinase signaling and is frequently mutated in cancers. In the present study, we showed that in addition to weakening the inhibitory interaction between p85α and p110α, a group of driver mutations in the p85α N-terminal SH2 domain activated EGFR, HER2, HER3, c-Met, and IGF-1R in a p110α-independent manner. Cancer cells expressing these...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 34507989
DOI: 10.1073/pnas.2101751118
PMCID: PMC8449365

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