NOK/STYK1 interacts with GSK-3β and mediates Ser9 phosphorylation through activated Akt

NOK (also known as STYK1) has been identified as an oncogene. However, its biochemical and biological activities as a molecular regulator are poorly defined. In the present study, we report that NOK overexpression led to enhanced phosphorylation of GSK-3 beta at its Ser9 residue via Akt phosphorylation at Thr308. NOK could make complexes with both Akt and GSK-3 beta. Moreover, the expression levels of NOK, p-Akt(Thr308) and p-GSK-3 beta(Ser9) were positively correlated in cancerous and non-cancerous breast cell lines. Thus, our data identified a novel functional molecular complex formed by NOK, Akt and GSK-3 beta that may relay a NOK-directed tumourigenic cascade. Structured summary of protein interactions: GSK3B physically interacts with NOK and Akt by anti tag coimmunoprecipitation (View interaction). GSK3B physically interacts with NOK by anti tag coimmunoprecipitation (View interaction). (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.