ERK1/2 regulates SIRT2 deacetylase activity.

SIRT2 is a mammalian member of the Sirtuin family of NAD-dependent protein deacetylases. The function of SIRT2 can be modulated by post-translational modification. However, the precise molecular signaling mechanisms of SIRT2 and extracellular signal-regulated kinase (ERK)1/2 have not been correlated. We investigated the potential regulation of SIRT2 function by ERK1/2. ERK activation by the over-expression of constitutively active MEK increased protein levels and enhanced the stability of SIRT2. In contrast, U0126, an inhibitor of mitogen-activated kinase kinase, suppressed SIRT2 protein level. ERK1/2 interacted with SIRT2 exogenously and endogenously. Deacetylase activity of SIRT2 was up-regulated in an ERK1/2-mediated manner. These results suggest that ERK1/2 regulates SIRT2 by increasing the protein levels, stability and activity of SIRT2. Copyright © 2013 Elsevier Inc. All rights reserved.

Citation

You Hee Choi, Hangun Kim, Sung Ho Lee, Yun-Hye Jin, Kwang Youl Lee. ERK1/2 regulates SIRT2 deacetylase activity. Biochemical and biophysical research communications. 2013 Jul 26;437(2):245-9

PMID: 23806683

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