SIRT1 and p300/CBP regulate the reversible acetylation of serine-threonine kinase NDR2

Nuclear Dbf2-related kinase 2 (NDR2) is a highly conserved kinase that belongs to the NDR/LATS serine-threonine kinase family. NDR2 is involved in many cellular processes as a kinase or a scaffolding protein. As a known kinase, NDR2 requires self-phosphorylation and trans-phosphorylation to become f...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2019-10, Vol.518 (2), p.396-401
Main Authors: Tang, Yunlan, Yu, Wei
Format: Article
Language:English
Subjects:
Acetylation
HDACs
NDR2
p300/CBP
SIRT1
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Summary:Nuclear Dbf2-related kinase 2 (NDR2) is a highly conserved kinase that belongs to the NDR/LATS serine-threonine kinase family. NDR2 is involved in many cellular processes as a kinase or a scaffolding protein. As a known kinase, NDR2 requires self-phosphorylation and trans-phosphorylation to become fully active. However, beside phosphorylation, little is known about other posttranslational modifications of NDR2. In this study, we found that NDR2 can be specially acetylated at K463 in cells. In addition, SIRT1 acts as the major deacetylase for NDR2, while p300 and CBP function as specific acetyltransferases for NDR2. Interestingly, in SIRT1 deficient cells HDAC6 and HDAC1/2 can deacetylate NDR2, which provides a novel insight in deacetylation regulation. Our results demonstrate that NDR2 is a reversible acetylated kinase regulated by SIRT1 and p300/CBP. •Acetylation of NDR2 can be accumulated by NAM treatment.•SIRT1 is the major deacetylase for NDR2.•HDAC1/2 and HDAC6 can deacetylate NDR2 only in the condition of SIRT1 deficiency.•P300/CBP are specific acetyltransferases for NDR2.•K463 is the major acetylated site in NDR2.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2019.08.069