SIRT2 deacetylase regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation

SIRT2 deacetylase regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation

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 inactiv...

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Bibliographic Details
Main Authors: Mohsen Sarikhani, Sneha Mishra, Sangeeta Maity, Chaithanya Kotyada, Donald Wolfgeher, Mahesh P Gupta, Mahavir Singh, Nagalingam R Sundaresan
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2018-03-01
Series:eLife
Subjects:
Lysine acetylation
Sirtuins
SIRT2
p300
GSK3α
GSK3β
Online Access:https://elifesciences.org/articles/32952

Internet

https://elifesciences.org/articles/32952

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