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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Online Access: | https://doi.org/10.1038/s41598-021-95941-4 |
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doaj-8dd02fb26ae54f6cadf2d5b862f5c9e02021-08-15T11:26:54ZengNature Publishing GroupScientific Reports2045-23222021-08-0111111610.1038/s41598-021-95941-4Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferationVirender Kumar Sharma0Mayurika Lahiri1Department of Biology, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchAbstract 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.https://doi.org/10.1038/s41598-021-95941-4 |
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DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Virender Kumar Sharma Mayurika Lahiri |
spellingShingle |
Virender Kumar Sharma Mayurika Lahiri Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation Scientific Reports |
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 Publishing Group |
series |
Scientific Reports |
issn |
2045-2322 |
publishDate |
2021-08-01 |
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. |
url |
https://doi.org/10.1038/s41598-021-95941-4 |
work_keys_str_mv |
AT virenderkumarsharma interplaybetweenp300andhdac1regulateacetylationandstabilityofapi5toregulatecellproliferation AT mayurikalahiri interplaybetweenp300andhdac1regulateacetylationandstabilityofapi5toregulatecellproliferation |
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