Disruption of PH-kinase domain interactions leads to oncogenic activation of AKT in human cancers.

doi:10.1073/pnas.1204384109

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Article

Disruption of PH-kinase domain interactions leads to oncogenic activation of AKT in human cancers.

Proceedings of the National Academy of Sciences of the United States of America - 20 Nov 2012

Parikh Chaitali, Janakiraman Vasantharajan, Wu Wen-I, Foo Catherine K, Kljavin Noelyn M, Chaudhuri Subhra, Stawiski Eric, Lee Brian, Lin Jie, Li Hong, Lorenzo Maria N, Yuan Wenlin, Guillory Joseph, Jackson Marlena, Rondon Jesus, Franke Yvonne, Bowman Krista K, Sagolla Meredith, Stinson Jeremy, Wu Thomas D, Wu Jiansheng, Stokoe David, Stern Howard M, Brandhuber Barbara J, Lin Kui, Skelton Nicholas J, Seshagiri Somasekar

Abstract excerpt

The protein kinase v-akt murine thymoma viral oncogene homolog (AKT), a key regulator of cell survival and proliferation, is frequently hyperactivated in human cancers. Intramolecular pleckstrin homology (PH) domain-kinase domain (KD) interactions are important in maintaining AKT in an inactive state. AKT activation proceeds after a conformational change that dislodges the PH from the KD. To understand these...

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PMID: 23134728
DOI: 10.1073/pnas.1204384109
PMCID: PMC3511101

Genes

AKT1

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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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