SIRT2 regulates oxidative stress-induced cell death through deacetylation of c-Jun NH₂-terminal kinase.

ABSTRACT: c-Jun NH₂-terminal kinases (JNKs) are responsive to stress stimuli and their activation regulate key cellular functions, including cell survival, growth, differentiation and aging. Previous studies demonstrate that activation of JNK requires dual phosphorylation by the mitogen-activated protein kinase kinases. However, other post-translational mechanisms involved in regulating the activity of JNK have been poorly understood. In this work, we studied the functional significance of reversible lysine acetylation in regulating the kinase activity of JNK. We found that the acetyl transferase p300 binds to, acetylates and inhibits kinase activity of JNK. Using tandem mass spectrometry, molecular modelling and molecular dynamics simulations, we found that acetylation of JNK at Lys153 w

SUBMITTER: Sarikhani M 

PROVIDER: S-EPMC6143545 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature