ERK1/2 regulates SIRT2 deacetylase activity

被引：23

作者：

Choi, You Hee ^{[1
,2
]}

Kim, Hangun ^{[3
,4
]}

Lee, Sung Ho ^{[1
,2
]}

Jin, Yun-Hye ^{[1
,2
]}

Lee, Kwang Youl ^{[1
,2
]}

机构：

[1] Chonnam Natl Univ, Coll Pharm, Kwangju, South Korea

[2] Chonnam Natl Univ, Res Inst Drug Dev, Kwangju, South Korea

[3] Sunchon Natl Univ, Coll Pharm, Sunchon, South Korea

[4] Sunchon Natl Univ, Res Inst Life & Pharmaceut Sci, Sunchon, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2013年 / 437卷 / 02期

基金：

新加坡国家研究基金会;

关键词：

SIRT2; ERK1/2; Protein level; Stability; Deacetylation; DEPENDENT DEACETYLASES; CELL-DEATH; P53; ACETYLATION; HDAC6; INHIBITION; INTERACTS; TUBULIN; FAMILY; GENE;

D O I：

10.1016/j.bbrc.2013.06.053

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

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. (C) 2013 Elsevier Inc. All rights reserved.

引用

页码：245 / 249

页数：5

共 25 条

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