BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization

BMI1, a core element of the polycomb repressive complex 1, is suggested to have oncogenic activity in a variety of cancers. Here, the authors report the structure of BMI1 bound to the protein PHC2, identify BMI1 homo-oligomerization interfaces, and analyse the role of BMI1 protein-protein interactio...

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Autores principales:	Felicia Gray, Hyo Je Cho, Shirish Shukla, Shihan He, Ashley Harris, Bohdan Boytsov, Łukasz Jaremko, Mariusz Jaremko, Borries Demeler, Elizabeth R. Lawlor, Jolanta Grembecka, Tomasz Cierpicki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/73f8f5efb05f424ba5d871afa61e0222
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spelling	oai:doaj.org-article:73f8f5efb05f424ba5d871afa61e02222021-12-02T16:50:12ZBMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization10.1038/ncomms133432041-1723https://doaj.org/article/73f8f5efb05f424ba5d871afa61e02222016-11-01T00:00:00Zhttps://doi.org/10.1038/ncomms13343https://doaj.org/toc/2041-1723BMI1, a core element of the polycomb repressive complex 1, is suggested to have oncogenic activity in a variety of cancers. Here, the authors report the structure of BMI1 bound to the protein PHC2, identify BMI1 homo-oligomerization interfaces, and analyse the role of BMI1 protein-protein interactions in PRC1 function.Felicia GrayHyo Je ChoShirish ShuklaShihan HeAshley HarrisBohdan BoytsovŁukasz JaremkoMariusz JaremkoBorries DemelerElizabeth R. LawlorJolanta GrembeckaTomasz CierpickiNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Felicia Gray Hyo Je Cho Shirish Shukla Shihan He Ashley Harris Bohdan Boytsov Łukasz Jaremko Mariusz Jaremko Borries Demeler Elizabeth R. Lawlor Jolanta Grembecka Tomasz Cierpicki BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization
description	BMI1, a core element of the polycomb repressive complex 1, is suggested to have oncogenic activity in a variety of cancers. Here, the authors report the structure of BMI1 bound to the protein PHC2, identify BMI1 homo-oligomerization interfaces, and analyse the role of BMI1 protein-protein interactions in PRC1 function.
format	article
author	Felicia Gray Hyo Je Cho Shirish Shukla Shihan He Ashley Harris Bohdan Boytsov Łukasz Jaremko Mariusz Jaremko Borries Demeler Elizabeth R. Lawlor Jolanta Grembecka Tomasz Cierpicki
author_facet	Felicia Gray Hyo Je Cho Shirish Shukla Shihan He Ashley Harris Bohdan Boytsov Łukasz Jaremko Mariusz Jaremko Borries Demeler Elizabeth R. Lawlor Jolanta Grembecka Tomasz Cierpicki
author_sort	Felicia Gray
title	BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization
title_short	BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization
title_full	BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization
title_fullStr	BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization
title_full_unstemmed	BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization
title_sort	bmi1 regulates prc1 architecture and activity through homo- and hetero-oligomerization
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/73f8f5efb05f424ba5d871afa61e0222
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BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization

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