@article{TEXTUAL,
      recid = {9904},
      author = {Sarikhani, Mohsen and Mishra, Sneha and Maity, Sangeeta  and Kotyada, Chaithanya and Wolfgeher, Donald and Gupta,  Mahesh P. and Singh, Mahavir and Sundaresan, Nagalingam R.},
      title = {SIRT2 deacetylase regulates the activity of GSK3 isoforms  independent of inhibitory phosphorylation},
      journal = {eLife},
      address = {2018-03-05},
      number = {TEXTUAL},
      abstract = {Glycogen synthase kinase 3 (GSK3) is a critical regulator  of diverse cellular functions involved in the maintenance  of structure and function. Enzymatic activity of GSK3 is  inhibited by N-terminal serine phosphorylation. However,  alternate post-translational mechanism(s) responsible for  GSK3 inactivation are not characterized. Here, we report  that GSK3a and GSK3β are acetylated at Lys246 and Lys183,  respectively. Molecular modeling and/or molecular dynamics  simulations indicate that acetylation of GSK3 isoforms  would hinder both the adenosine binding and prevent stable  interactions of the negatively charged phosphates. We found  that SIRT2 deacetylates GSK3β, and thus enhances its  binding to ATP. Interestingly, the reduced activity of  GSK3β is associated with lysine acetylation, but not with  phosphorylation at Ser9 in hearts of SIRT2-deficient mice.  Moreover, GSK3 is required for the anti-hypertrophic  function of SIRT2 in cardiomyocytes. Overall, our study  identified lysine acetylation as a novel post-translational  modification regulating GSK3 activity.},
      url = {http://knowledge.uchicago.edu/record/9904},
}