Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state

DOCK2 is a guanine nucleotide exchange factor (GEF) that activates RHO GTPases and interacts with ELMO1, which stimulates its GEF activity. Here, the authors provide mechanistic insights into how ELMO1 regulates DOCK2 activity by determining the structure of the DOCK2–ELMO1 binary complex representi...

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Autores principales:	Leifu Chang, Jing Yang, Chang Hwa Jo, Andreas Boland, Ziguo Zhang, Stephen H. McLaughlin, Afnan Abu-Thuraia, Ryan C. Killoran, Matthew J. Smith, Jean-Francois Côté, David Barford
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d8a372772f44414b8c28c69fb426524f
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spelling	oai:doaj.org-article:d8a372772f44414b8c28c69fb426524f2021-12-02T16:14:58ZStructure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state10.1038/s41467-020-17271-92041-1723https://doaj.org/article/d8a372772f44414b8c28c69fb426524f2020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17271-9https://doaj.org/toc/2041-1723DOCK2 is a guanine nucleotide exchange factor (GEF) that activates RHO GTPases and interacts with ELMO1, which stimulates its GEF activity. Here, the authors provide mechanistic insights into how ELMO1 regulates DOCK2 activity by determining the structure of the DOCK2–ELMO1 binary complex representing the closed, auto-inhibited state and the DOCK2−ELMO1−RAC1 ternary complex structure, where DOCK2−ELMO1 adopts an open, active conformation.Leifu ChangJing YangChang Hwa JoAndreas BolandZiguo ZhangStephen H. McLaughlinAfnan Abu-ThuraiaRyan C. KilloranMatthew J. SmithJean-Francois CôtéDavid BarfordNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Leifu Chang Jing Yang Chang Hwa Jo Andreas Boland Ziguo Zhang Stephen H. McLaughlin Afnan Abu-Thuraia Ryan C. Killoran Matthew J. Smith Jean-Francois Côté David Barford Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
description	DOCK2 is a guanine nucleotide exchange factor (GEF) that activates RHO GTPases and interacts with ELMO1, which stimulates its GEF activity. Here, the authors provide mechanistic insights into how ELMO1 regulates DOCK2 activity by determining the structure of the DOCK2–ELMO1 binary complex representing the closed, auto-inhibited state and the DOCK2−ELMO1−RAC1 ternary complex structure, where DOCK2−ELMO1 adopts an open, active conformation.
format	article
author	Leifu Chang Jing Yang Chang Hwa Jo Andreas Boland Ziguo Zhang Stephen H. McLaughlin Afnan Abu-Thuraia Ryan C. Killoran Matthew J. Smith Jean-Francois Côté David Barford
author_facet	Leifu Chang Jing Yang Chang Hwa Jo Andreas Boland Ziguo Zhang Stephen H. McLaughlin Afnan Abu-Thuraia Ryan C. Killoran Matthew J. Smith Jean-Francois Côté David Barford
author_sort	Leifu Chang
title	Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
title_short	Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
title_full	Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
title_fullStr	Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
title_full_unstemmed	Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
title_sort	structure of the dock2−elmo1 complex provides insights into regulation of the auto-inhibited state
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/d8a372772f44414b8c28c69fb426524f
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Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state

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