Biochemical and cellular evidence demonstrating AKT-1 as a binding partner for resveratrol targeting protein NQO2.

ABSTRACT:

Background

AKT plays an important role in the control of cell proliferation and survival. Aberrant activation of AKT frequently occurs in human cancers making it an attractive drug targets and leading to the synthesis of numerous AKT inhibitors as therapeutic candidates. Less is known regarding proteins that control AKT. We recently reported that quinone reductase 2 (NQO2) inhibited AKT activity, by unknown mechanisms.

Methodology/principal findings

In this study, molecular modeling was used to query interaction between NQO2 and AKT. We found that pleckstrin homology (PH) and kinase domains of AKT bind to chains A and B of NQO2. Pull-down and deletion assays revealed that PH domain of AKT is essential for interaction with NQO2. Modeling analysis further revealed that kinase

SUBMITTER: Hsieh TC 

PROVIDER: S-EPMC4072751 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature