The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation

While the biological roles of ubiquitin chains are well studied, little is known about the functions of SUMO polymers. Here, the authors identify poly-SUMOylation substrates and provide evidence that SUMO polymers regulate the accumulation of CCAN subunits at chromatin and centromeres.

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Autores principales:	Frauke Liebelt, Nicolette S. Jansen, Sumit Kumar, Ekaterina Gracheva, Laura A. Claessens, Matty Verlaan-de Vries, Edwin Willemstein, Alfred C. O. Vertegaal
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8d573a3ede6f4566ad9972c15b4cb8c0
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spelling	oai:doaj.org-article:8d573a3ede6f4566ad9972c15b4cb8c02021-12-02T14:39:37ZThe poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation10.1038/s41467-019-11773-x2041-1723https://doaj.org/article/8d573a3ede6f4566ad9972c15b4cb8c02019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11773-xhttps://doaj.org/toc/2041-1723While the biological roles of ubiquitin chains are well studied, little is known about the functions of SUMO polymers. Here, the authors identify poly-SUMOylation substrates and provide evidence that SUMO polymers regulate the accumulation of CCAN subunits at chromatin and centromeres.Frauke LiebeltNicolette S. JansenSumit KumarEkaterina GrachevaLaura A. ClaessensMatty Verlaan-de VriesEdwin WillemsteinAlfred C. O. VertegaalNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-18 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Frauke Liebelt Nicolette S. Jansen Sumit Kumar Ekaterina Gracheva Laura A. Claessens Matty Verlaan-de Vries Edwin Willemstein Alfred C. O. Vertegaal The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
description	While the biological roles of ubiquitin chains are well studied, little is known about the functions of SUMO polymers. Here, the authors identify poly-SUMOylation substrates and provide evidence that SUMO polymers regulate the accumulation of CCAN subunits at chromatin and centromeres.
format	article
author	Frauke Liebelt Nicolette S. Jansen Sumit Kumar Ekaterina Gracheva Laura A. Claessens Matty Verlaan-de Vries Edwin Willemstein Alfred C. O. Vertegaal
author_facet	Frauke Liebelt Nicolette S. Jansen Sumit Kumar Ekaterina Gracheva Laura A. Claessens Matty Verlaan-de Vries Edwin Willemstein Alfred C. O. Vertegaal
author_sort	Frauke Liebelt
title	The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
title_short	The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
title_full	The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
title_fullStr	The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
title_full_unstemmed	The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
title_sort	poly-sumo2/3 protease senp6 enables assembly of the constitutive centromere-associated network by group desumoylation
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/8d573a3ede6f4566ad9972c15b4cb8c0
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The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation

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