ERK1/2 regulates SIRT2 deacetylase activity

作者：Choi You Hee; Kim Hangun; Lee Sung Ho; Jin Yun Hye^*; Lee Kwang Youl

来源：Biochemical and Biophysical Research Communications, 2013, 437(2): 245-249.

DOI：10.1016/j.bbrc.2013.06.053

• SIRT2
• ERK1/2
• Protein level
• Stability
• Deacetylation

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.

• 出版日期2013-7-26