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Identification of Novel Interacting Partners of Sirtuin6

SIRT6 is a member of the Sirtuin family of histone deacetylases that has been implicated in inflammatory, aging and metabolic pathways. Some of its actions have been suggested to be via physical interaction with NFκB and HIF1α and transcriptional regulation through its histone deacetylase activity....

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Autores principales: Polyakova, Oxana, Borman, Satty, Grimley, Rachel, Vamathevan, Jessica, Hayes, Brian, Solari, Roberto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3519869/
https://www.ncbi.nlm.nih.gov/pubmed/23240041
http://dx.doi.org/10.1371/journal.pone.0051555
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author Polyakova, Oxana
Borman, Satty
Grimley, Rachel
Vamathevan, Jessica
Hayes, Brian
Solari, Roberto
author_facet Polyakova, Oxana
Borman, Satty
Grimley, Rachel
Vamathevan, Jessica
Hayes, Brian
Solari, Roberto
author_sort Polyakova, Oxana
collection PubMed
description SIRT6 is a member of the Sirtuin family of histone deacetylases that has been implicated in inflammatory, aging and metabolic pathways. Some of its actions have been suggested to be via physical interaction with NFκB and HIF1α and transcriptional regulation through its histone deacetylase activity. Our previous studies have investigated the histone deacetylase activity of SIRT6 and explored its ability to regulate the transcriptional responses to an inflammatory stimulus such as TNFα. In order to develop a greater understanding of SIRT6 function we have sought to identify SIRT6 interacting proteins by both yeast-2-hybrid and co-immunoprecipitation studies. We report a number of interacting partners which strengthen previous findings that SIRT6 functions in base excision repair (BER), and novel interactors which suggest a role in nucleosome and chromatin remodeling, the cell cycle and NFκB biology.
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spelling pubmed-35198692012-12-13 Identification of Novel Interacting Partners of Sirtuin6 Polyakova, Oxana Borman, Satty Grimley, Rachel Vamathevan, Jessica Hayes, Brian Solari, Roberto PLoS One Research Article SIRT6 is a member of the Sirtuin family of histone deacetylases that has been implicated in inflammatory, aging and metabolic pathways. Some of its actions have been suggested to be via physical interaction with NFκB and HIF1α and transcriptional regulation through its histone deacetylase activity. Our previous studies have investigated the histone deacetylase activity of SIRT6 and explored its ability to regulate the transcriptional responses to an inflammatory stimulus such as TNFα. In order to develop a greater understanding of SIRT6 function we have sought to identify SIRT6 interacting proteins by both yeast-2-hybrid and co-immunoprecipitation studies. We report a number of interacting partners which strengthen previous findings that SIRT6 functions in base excision repair (BER), and novel interactors which suggest a role in nucleosome and chromatin remodeling, the cell cycle and NFκB biology. Public Library of Science 2012-12-11 /pmc/articles/PMC3519869/ /pubmed/23240041 http://dx.doi.org/10.1371/journal.pone.0051555 Text en © 2012 Polyakova et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Polyakova, Oxana
Borman, Satty
Grimley, Rachel
Vamathevan, Jessica
Hayes, Brian
Solari, Roberto
Identification of Novel Interacting Partners of Sirtuin6
title Identification of Novel Interacting Partners of Sirtuin6
title_full Identification of Novel Interacting Partners of Sirtuin6
title_fullStr Identification of Novel Interacting Partners of Sirtuin6
title_full_unstemmed Identification of Novel Interacting Partners of Sirtuin6
title_short Identification of Novel Interacting Partners of Sirtuin6
title_sort identification of novel interacting partners of sirtuin6
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3519869/
https://www.ncbi.nlm.nih.gov/pubmed/23240041
http://dx.doi.org/10.1371/journal.pone.0051555
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