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PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression

While reversible histone modifications are linked to an ever-expanding range of biological functions1–5, the demethylases for histone H4 lysine 20 and their potential regulatory roles remain unknown. Here, we report that the PHD and Jumonji C (JmjC) domain-containing protein, PHF8, while utilizing m...

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Autores principales: Liu, Wen, Tanasa, Bogdan, Tyurina, Oksana V., Zhou, Tian Yuan, Gassmann, Reto, Liu, Wei Ting, Ohgi, Kenneth A., Benner, Chris, Garcia-Bassets, Ivan, Aggarwal, Aneel K., Desai, Arshad, Dorrestein, Pieter C., Glass, Christopher K., Rosenfeld, Michael G.
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059551/
https://www.ncbi.nlm.nih.gov/pubmed/20622854
http://dx.doi.org/10.1038/nature09272
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author Liu, Wen
Tanasa, Bogdan
Tyurina, Oksana V.
Zhou, Tian Yuan
Gassmann, Reto
Liu, Wei Ting
Ohgi, Kenneth A.
Benner, Chris
Garcia-Bassets, Ivan
Aggarwal, Aneel K.
Desai, Arshad
Dorrestein, Pieter C.
Glass, Christopher K.
Rosenfeld, Michael G.
author_facet Liu, Wen
Tanasa, Bogdan
Tyurina, Oksana V.
Zhou, Tian Yuan
Gassmann, Reto
Liu, Wei Ting
Ohgi, Kenneth A.
Benner, Chris
Garcia-Bassets, Ivan
Aggarwal, Aneel K.
Desai, Arshad
Dorrestein, Pieter C.
Glass, Christopher K.
Rosenfeld, Michael G.
author_sort Liu, Wen
collection PubMed
description While reversible histone modifications are linked to an ever-expanding range of biological functions1–5, the demethylases for histone H4 lysine 20 and their potential regulatory roles remain unknown. Here, we report that the PHD and Jumonji C (JmjC) domain-containing protein, PHF8, while utilizing multiple substrates, including H3K9me(1/2) and H3K27me(2), also functions as an H4K20me(1) demethylase. PHF8 is recruited to promoters by its PHD domain based on interaction with H3K4me(2/3) and controls G1/S transition in conjunction with E2F1, HCF-1 and Set1A, at least in part, by removing the repressive H4K20me(1) mark from a subset of E2F1-regulated gene promoters. Phosphorylation-dependent PHF8 dismissal from chromatin in prophase is apparently required for the accumulation of H4K20me(1) during early mitosis, which might represent a component of the Condensin II loading process. Accordingly, the HEAT repeat clusters in two non-SMC Condensin II subunits, N-CAPD3 and N-CAPG2, are capable of recognizing H4K20me(1), and ChIP-seq. analysis demonstrate a significant overlap of Condensin II and H4K20me(1) sites in mitotic HeLa cells. Thus, the identification and characterization of the first H4K20me(1) demethylase, PHF8, has revealed an intimate link between this enzyme and two distinct events in cell cycle progression.
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spelling pubmed-30595512011-03-17 PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression Liu, Wen Tanasa, Bogdan Tyurina, Oksana V. Zhou, Tian Yuan Gassmann, Reto Liu, Wei Ting Ohgi, Kenneth A. Benner, Chris Garcia-Bassets, Ivan Aggarwal, Aneel K. Desai, Arshad Dorrestein, Pieter C. Glass, Christopher K. Rosenfeld, Michael G. Nature Article While reversible histone modifications are linked to an ever-expanding range of biological functions1–5, the demethylases for histone H4 lysine 20 and their potential regulatory roles remain unknown. Here, we report that the PHD and Jumonji C (JmjC) domain-containing protein, PHF8, while utilizing multiple substrates, including H3K9me(1/2) and H3K27me(2), also functions as an H4K20me(1) demethylase. PHF8 is recruited to promoters by its PHD domain based on interaction with H3K4me(2/3) and controls G1/S transition in conjunction with E2F1, HCF-1 and Set1A, at least in part, by removing the repressive H4K20me(1) mark from a subset of E2F1-regulated gene promoters. Phosphorylation-dependent PHF8 dismissal from chromatin in prophase is apparently required for the accumulation of H4K20me(1) during early mitosis, which might represent a component of the Condensin II loading process. Accordingly, the HEAT repeat clusters in two non-SMC Condensin II subunits, N-CAPD3 and N-CAPG2, are capable of recognizing H4K20me(1), and ChIP-seq. analysis demonstrate a significant overlap of Condensin II and H4K20me(1) sites in mitotic HeLa cells. Thus, the identification and characterization of the first H4K20me(1) demethylase, PHF8, has revealed an intimate link between this enzyme and two distinct events in cell cycle progression. 2010-07-11 2010-07-22 /pmc/articles/PMC3059551/ /pubmed/20622854 http://dx.doi.org/10.1038/nature09272 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Liu, Wen
Tanasa, Bogdan
Tyurina, Oksana V.
Zhou, Tian Yuan
Gassmann, Reto
Liu, Wei Ting
Ohgi, Kenneth A.
Benner, Chris
Garcia-Bassets, Ivan
Aggarwal, Aneel K.
Desai, Arshad
Dorrestein, Pieter C.
Glass, Christopher K.
Rosenfeld, Michael G.
PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression
title PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression
title_full PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression
title_fullStr PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression
title_full_unstemmed PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression
title_short PHF8 Mediates Histone H4 Lysine 20 Demethylation Events Involved in Cell Cycle Progression
title_sort phf8 mediates histone h4 lysine 20 demethylation events involved in cell cycle progression
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059551/
https://www.ncbi.nlm.nih.gov/pubmed/20622854
http://dx.doi.org/10.1038/nature09272
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