Related Experiment Video

Updated: Apr 30, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

18.3K

C-terminal AKT phosphorylation by CDK2-cyclin A or mTOR activates AKT

    Cancer Discovery
    |May 6, 2014
    PubMed

    Insights

    Cyclin-dependent kinase 2-cyclin A2 (CDK2-cyclin A2) and the mechanistic target of rapamycin (mTOR) pathway activate AKT. This activation occurs through the phosphorylation of specific C-terminal residues, S477 and T479.

    Area of Science:

    • Molecular Biology
    • Cell Signaling

    Background:

    • The AKT signaling pathway is crucial in regulating cell survival, proliferation, and metabolism.
    • Understanding the upstream regulators of AKT activation is vital for comprehending cellular processes and disease development.

    Purpose of the Study:

    • To elucidate the specific kinases responsible for activating AKT.
    • To identify the phosphorylation sites on AKT involved in its activation by CDK2-cyclin A2 and mTOR.

    Main Methods:

    • Western blotting to detect phosphorylated AKT.
    • Kinase assays to assess the activity of CDK2-cyclin A2 and mTOR.
    • Site-directed mutagenesis to investigate the role of S477 and T479 residues.

    Main Results:

    • CDK2-cyclin A2 was identified as a kinase that phosphorylates AKT.
    • mTOR was also shown to activate AKT.
    • Phosphorylation occurred at the C-terminal serine (S477) and threonine (T479) residues of AKT.

    Conclusions:

    • CDK2-cyclin A2 and mTOR are key activators of AKT.
    • Phosphorylation of S477 and T479 are critical events for AKT activation by these kinases.
    • These findings provide new insights into AKT pathway regulation.

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