MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation

Batlle et al. identify the presence of coiled-coil (CC) domains that overlap with polyQ tracts in human proteins containing prion-like domains (PrLDs). They demonstrate that human MED15 Mediator complex subunit forms homodimers in solution mediated by coiled-coil interactions and that MED15CC aggreg...

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Autores principales:	Cristina Batlle, Isabel Calvo, Valentin Iglesias, Cian J. Lynch, Marcos Gil-Garcia, Manuel Serrano, Salvador Ventura
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/2517a586465644e7b440718bfabfa5ee
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spelling	oai:doaj.org-article:2517a586465644e7b440718bfabfa5ee2021-12-02T17:04:04ZMED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation10.1038/s42003-021-01930-82399-3642https://doaj.org/article/2517a586465644e7b440718bfabfa5ee2021-03-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01930-8https://doaj.org/toc/2399-3642Batlle et al. identify the presence of coiled-coil (CC) domains that overlap with polyQ tracts in human proteins containing prion-like domains (PrLDs). They demonstrate that human MED15 Mediator complex subunit forms homodimers in solution mediated by coiled-coil interactions and that MED15CC aggregates into amyloid fibrils.Cristina BatlleIsabel CalvoValentin IglesiasCian J. LynchMarcos Gil-GarciaManuel SerranoSalvador VenturaNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Cristina Batlle Isabel Calvo Valentin Iglesias Cian J. Lynch Marcos Gil-Garcia Manuel Serrano Salvador Ventura MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
description	Batlle et al. identify the presence of coiled-coil (CC) domains that overlap with polyQ tracts in human proteins containing prion-like domains (PrLDs). They demonstrate that human MED15 Mediator complex subunit forms homodimers in solution mediated by coiled-coil interactions and that MED15CC aggregates into amyloid fibrils.
format	article
author	Cristina Batlle Isabel Calvo Valentin Iglesias Cian J. Lynch Marcos Gil-Garcia Manuel Serrano Salvador Ventura
author_facet	Cristina Batlle Isabel Calvo Valentin Iglesias Cian J. Lynch Marcos Gil-Garcia Manuel Serrano Salvador Ventura
author_sort	Cristina Batlle
title	MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
title_short	MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
title_full	MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
title_fullStr	MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
title_full_unstemmed	MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
title_sort	med15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2517a586465644e7b440718bfabfa5ee
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MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation

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