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Article

Physical association of PDK1 with AKT1 is sufficient for pathway activation independent of membrane localization and phosphatidylinositol 3 kinase.

PloS one - 26 Mar 2010

Ding Zhiyong, Liang Jiyong, Li Jin, Lu Yiling, Ariyaratna Vathsala, Lu Zhimin, Davies Michael A, Westwick John K, Mills Gordon B

Abstract excerpt

Frequent activation of the AKT serine-threonine kinase in cancer confers resistance to therapy. AKT is activated by a multi-step process involving phosphatidylinositide (PtdIns) phosphate-mediated recruitment of AKT and its upstream kinases, including 3-Phosphoinositide-dependent kinase 1 (PDK1), to the inner surface of the cell membrane. PDK1 in the appropriate context phosphorylates AKT at threonine 308 (T308)...

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Share to Fluorescent Dyes
Share to Gene Expression Regulation, Enzymologic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Phosphatidylinositol 3-Kinases

Share to Proto-Oncogene Proteins c-akt

Share to Pyruvate Dehydrogenase Acetyl-Transferring Kinase

Share to RNA, Small Interfering

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 20361045
DOI: 10.1371/journal.pone.0009910
PMCID: PMC2845649

Genes

AKT1
PDK1

Variants

Provenance

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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