Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins

Malvezzi et al. discuss the impact of BRD4 phosphorylation on the formation of dimers and identify the key residues necessary for this dimerization. They also discuss the differential role of monovalent and bivalents bromodomain inhibitors regarding the interaction with these dimers and suggest a ne...

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Autores principales:	Francesca Malvezzi, Christopher J. Stubbs, Thomas A. Jowitt, Ian L. Dale, Xieyang Guo, Jon P. DeGnore, Gianluca Degliesposti, J. Mark Skehel, Andrew J. Bannister, Mark S. McAlister
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/f5b48828673a41eebf428eec72402021
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spelling	oai:doaj.org-article:f5b48828673a41eebf428eec724020212021-11-14T12:12:19ZPhosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins10.1038/s42003-021-02750-62399-3642https://doaj.org/article/f5b48828673a41eebf428eec724020212021-11-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02750-6https://doaj.org/toc/2399-3642Malvezzi et al. discuss the impact of BRD4 phosphorylation on the formation of dimers and identify the key residues necessary for this dimerization. They also discuss the differential role of monovalent and bivalents bromodomain inhibitors regarding the interaction with these dimers and suggest a new model of BRD4 binding to chromatin.Francesca MalvezziChristopher J. StubbsThomas A. JowittIan L. DaleXieyang GuoJon P. DeGnoreGianluca DegliespostiJ. Mark SkehelAndrew J. BannisterMark S. McAlisterNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Francesca Malvezzi Christopher J. Stubbs Thomas A. Jowitt Ian L. Dale Xieyang Guo Jon P. DeGnore Gianluca Degliesposti J. Mark Skehel Andrew J. Bannister Mark S. McAlister Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins
description	Malvezzi et al. discuss the impact of BRD4 phosphorylation on the formation of dimers and identify the key residues necessary for this dimerization. They also discuss the differential role of monovalent and bivalents bromodomain inhibitors regarding the interaction with these dimers and suggest a new model of BRD4 binding to chromatin.
format	article
author	Francesca Malvezzi Christopher J. Stubbs Thomas A. Jowitt Ian L. Dale Xieyang Guo Jon P. DeGnore Gianluca Degliesposti J. Mark Skehel Andrew J. Bannister Mark S. McAlister
author_facet	Francesca Malvezzi Christopher J. Stubbs Thomas A. Jowitt Ian L. Dale Xieyang Guo Jon P. DeGnore Gianluca Degliesposti J. Mark Skehel Andrew J. Bannister Mark S. McAlister
author_sort	Francesca Malvezzi
title	Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins
title_short	Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins
title_full	Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins
title_fullStr	Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins
title_full_unstemmed	Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins
title_sort	phosphorylation-dependent brd4 dimerization and implications for therapeutic inhibition of bet family proteins
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f5b48828673a41eebf428eec72402021
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Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins

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