Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies

Auxin-mediated recruitment of AUX/IAAs by the F-box protein TIR1 prompts rapid AUX/IAA ubiquitylation and degradation. By resolving auxin receptor topology, the authors show that intrinsically disordered regions near the degrons of two Aux/IAA proteins reinforce complex assembly and position Aux/IAA...

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Autores principales:	Michael Niemeyer, Elena Moreno Castillo, Christian H. Ihling, Claudio Iacobucci, Verona Wilde, Antje Hellmuth, Wolfgang Hoehenwarter, Sophia L. Samodelov, Matias D. Zurbriggen, Panagiotis L. Kastritis, Andrea Sinz, Luz Irina A. Calderón Villalobos
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/083d3139070748c996146102b870ffe1
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spelling	oai:doaj.org-article:083d3139070748c996146102b870ffe12021-12-02T14:40:53ZFlexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies10.1038/s41467-020-16147-22041-1723https://doaj.org/article/083d3139070748c996146102b870ffe12020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16147-2https://doaj.org/toc/2041-1723Auxin-mediated recruitment of AUX/IAAs by the F-box protein TIR1 prompts rapid AUX/IAA ubiquitylation and degradation. By resolving auxin receptor topology, the authors show that intrinsically disordered regions near the degrons of two Aux/IAA proteins reinforce complex assembly and position Aux/IAAs for ubiquitylation.Michael NiemeyerElena Moreno CastilloChristian H. IhlingClaudio IacobucciVerona WildeAntje HellmuthWolfgang HoehenwarterSophia L. SamodelovMatias D. ZurbriggenPanagiotis L. KastritisAndrea SinzLuz Irina A. Calderón VillalobosNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-18 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Michael Niemeyer Elena Moreno Castillo Christian H. Ihling Claudio Iacobucci Verona Wilde Antje Hellmuth Wolfgang Hoehenwarter Sophia L. Samodelov Matias D. Zurbriggen Panagiotis L. Kastritis Andrea Sinz Luz Irina A. Calderón Villalobos Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies
description	Auxin-mediated recruitment of AUX/IAAs by the F-box protein TIR1 prompts rapid AUX/IAA ubiquitylation and degradation. By resolving auxin receptor topology, the authors show that intrinsically disordered regions near the degrons of two Aux/IAA proteins reinforce complex assembly and position Aux/IAAs for ubiquitylation.
format	article
author	Michael Niemeyer Elena Moreno Castillo Christian H. Ihling Claudio Iacobucci Verona Wilde Antje Hellmuth Wolfgang Hoehenwarter Sophia L. Samodelov Matias D. Zurbriggen Panagiotis L. Kastritis Andrea Sinz Luz Irina A. Calderón Villalobos
author_facet	Michael Niemeyer Elena Moreno Castillo Christian H. Ihling Claudio Iacobucci Verona Wilde Antje Hellmuth Wolfgang Hoehenwarter Sophia L. Samodelov Matias D. Zurbriggen Panagiotis L. Kastritis Andrea Sinz Luz Irina A. Calderón Villalobos
author_sort	Michael Niemeyer
title	Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies
title_short	Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies
title_full	Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies
title_fullStr	Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies
title_full_unstemmed	Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies
title_sort	flexibility of intrinsically disordered degrons in aux/iaa proteins reinforces auxin co-receptor assemblies
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/083d3139070748c996146102b870ffe1
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Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies

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