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Biochem Biophys Res Commun. 2013 Nov 29;441(4):799-804. doi: 10.1016/j.bbrc.2013.10.133. Epub 2013 Nov 5.

SIRT1 negatively regulates the protein stability of HIPK2.

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  • 1Department of Molecular Biology, Sejong University, Seoul 143-747, Republic of Korea.

Abstract

In the present study, we investigated whether a histone deacetylase sirtuin 1 (SIRT1) can regulate the protein stability of homeodomain-interacting protein kinase 2 (HIPK2). We observed the evidence of molecular interaction between SIRT1 and HIPK2. Interestingly, overexpression or pharmacological activation of SIRT1 promoted ubiquitination and the proteasomal degradation of HIPK2 whereas inhibition of SIRT1 activity increased the protein level of HIPK2. Furthermore, a SIRT1 activator decreased the level of HIPK2 acetylation whereas an inhibitor increased the acetylation level. These results suggest that SIRT1 may deacetylate and promote the ubiquitination and subsequent proteasomal degradation of HIPK2.

Copyright © 2013 Elsevier Inc. All rights reserved.

KEYWORDS:

Deacetylation; HIPK2; Proteasomal degradation; SIRT1; Ubiquitination

PMID:
24211575
[PubMed - indexed for MEDLINE]
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