Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation

Abstract Api5, is a known anti-apoptotic and nuclear protein that is responsible for inhibiting cell death in serum-starved conditions. The only known post-translational modification of Api5 is acetylation at lysine 251 (K251). K251 acetylation of Api5 is responsible for maintaining its stability wh...

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Autores principales:	Virender Kumar Sharma, Mayurika Lahiri
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8dd02fb26ae54f6cadf2d5b862f5c9e0
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spelling	oai:doaj.org-article:8dd02fb26ae54f6cadf2d5b862f5c9e02021-12-02T18:50:44ZInterplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation10.1038/s41598-021-95941-42045-2322https://doaj.org/article/8dd02fb26ae54f6cadf2d5b862f5c9e02021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-95941-4https://doaj.org/toc/2045-2322Abstract Api5, is a known anti-apoptotic and nuclear protein that is responsible for inhibiting cell death in serum-starved conditions. The only known post-translational modification of Api5 is acetylation at lysine 251 (K251). K251 acetylation of Api5 is responsible for maintaining its stability while the de-acetylated form of Api5 is unstable. This study aimed to find out the enzymes regulating acetylation and deacetylation of Api5 and the effect of acetylation on its function. Our studies suggest that acetylation of Api5 at lysine 251 is mediated by p300 histone acetyltransferase while de-acetylation is carried out by HDAC1. Inhibition of acetylation by p300 leads to a reduction in Api5 levels while inhibition of deacetylation by HDAC1 results in increased levels of Api5. This dynamic switch between acetylation and deacetylation regulates the localisation of Api5 in the cell. This study also demonstrates that the regulation of acetylation and deacetylation of Api5 is an essential factor for the progression of the cell cycle.Virender Kumar SharmaMayurika LahiriNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Virender Kumar Sharma Mayurika Lahiri Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation
description	Abstract Api5, is a known anti-apoptotic and nuclear protein that is responsible for inhibiting cell death in serum-starved conditions. The only known post-translational modification of Api5 is acetylation at lysine 251 (K251). K251 acetylation of Api5 is responsible for maintaining its stability while the de-acetylated form of Api5 is unstable. This study aimed to find out the enzymes regulating acetylation and deacetylation of Api5 and the effect of acetylation on its function. Our studies suggest that acetylation of Api5 at lysine 251 is mediated by p300 histone acetyltransferase while de-acetylation is carried out by HDAC1. Inhibition of acetylation by p300 leads to a reduction in Api5 levels while inhibition of deacetylation by HDAC1 results in increased levels of Api5. This dynamic switch between acetylation and deacetylation regulates the localisation of Api5 in the cell. This study also demonstrates that the regulation of acetylation and deacetylation of Api5 is an essential factor for the progression of the cell cycle.
format	article
author	Virender Kumar Sharma Mayurika Lahiri
author_facet	Virender Kumar Sharma Mayurika Lahiri
author_sort	Virender Kumar Sharma
title	Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation
title_short	Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation
title_full	Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation
title_fullStr	Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation
title_full_unstemmed	Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation
title_sort	interplay between p300 and hdac1 regulate acetylation and stability of api5 to regulate cell proliferation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/8dd02fb26ae54f6cadf2d5b862f5c9e0
work_keys_str_mv	AT virenderkumarsharma interplaybetweenp300andhdac1regulateacetylationandstabilityofapi5toregulatecellproliferation AT mayurikalahiri interplaybetweenp300andhdac1regulateacetylationandstabilityofapi5toregulatecellproliferation
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Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation

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