Phosphorylation of serine-504 of tNOX (ENOX2) modulates cell proliferation and migration in cancer cells
- Graduate Institute of Biomedical Sciences, National Chung Hsing University, Taichung, 40227, Taiwan, ROC (China)
- School of Dentistry, Chung-Shan Medical University, Taichung 402, Taiwan, ROC (China)
Tumor-associated NADH oxidase (tNOX; ENOX2) is a growth-related protein expressed in transformed cells. Consistent with this function, tNOX knockdown by RNA interference leads to a significant reduction in cell proliferation and migration in HeLa cells, whereas tNOX overexpression confers an aggressive phenotype. Here, for the first time, we report that tNOX is phosphorylated by protein kinase C{delta} (PKC{delta}) both in vitro and in vivo. Replacement of serine-504 with alanine significantly reduces phosphorylation by PKC{delta}. Co-immunoprecipitation experiments reveal an interaction between tNOX and PKC{delta}. Moreover, whereas overexpression of wild-type tNOX in NIH3T3 cells increases cell proliferation and migration, overexpression of the S504A tNOX mutant leads to diminished cell proliferation and migration, reflecting reduced stability of the unphosphorylatable tNOX mutant protein. Collectively, these results suggest that phosphorylation of serine-504 by PKC{delta} modulates the biological function of tNOX.
- OSTI ID:
- 22212285
- Journal Information:
- Experimental Cell Research, Vol. 318, Issue 14; Other Information: Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0014-4827
- Country of Publication:
- United States
- Language:
- English
Similar Records
Knockdown of Trnau1ap inhibits the proliferation and migration of NIH3T3, JEG-3 and Bewo cells via the PI3K/Akt signaling pathway
RNA interference targeting tNOX attenuates cell migration via a mechanism that involves membrane association of Rac