Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5

Legionella pneumophila replicates in a Legionella-containing vacuole (LCV). Here the authors present the structure of the Legionella effector RidL N-terminal domain and reveal how RidL contributes to the subversion of retrograde trafficking by binding to the retromer coat complex subunit Vps29, whic...

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Autores principales:	Kevin Bärlocher, Cedric A. J. Hutter, A. Leoni Swart, Bernhard Steiner, Amanda Welin, Michael Hohl, François Letourneur, Markus A. Seeger, Hubert Hilbi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/148a39307e6a423aa3dcf97540bed38e
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spelling	oai:doaj.org-article:148a39307e6a423aa3dcf97540bed38e2021-12-02T16:51:52ZStructural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D510.1038/s41467-017-01512-52041-1723https://doaj.org/article/148a39307e6a423aa3dcf97540bed38e2017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01512-5https://doaj.org/toc/2041-1723Legionella pneumophila replicates in a Legionella-containing vacuole (LCV). Here the authors present the structure of the Legionella effector RidL N-terminal domain and reveal how RidL contributes to the subversion of retrograde trafficking by binding to the retromer coat complex subunit Vps29, which leads to a displacement of the regulator TBC1D5.Kevin BärlocherCedric A. J. HutterA. Leoni SwartBernhard SteinerAmanda WelinMichael HohlFrançois LetourneurMarkus A. SeegerHubert HilbiNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kevin Bärlocher Cedric A. J. Hutter A. Leoni Swart Bernhard Steiner Amanda Welin Michael Hohl François Letourneur Markus A. Seeger Hubert Hilbi Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5
description	Legionella pneumophila replicates in a Legionella-containing vacuole (LCV). Here the authors present the structure of the Legionella effector RidL N-terminal domain and reveal how RidL contributes to the subversion of retrograde trafficking by binding to the retromer coat complex subunit Vps29, which leads to a displacement of the regulator TBC1D5.
format	article
author	Kevin Bärlocher Cedric A. J. Hutter A. Leoni Swart Bernhard Steiner Amanda Welin Michael Hohl François Letourneur Markus A. Seeger Hubert Hilbi
author_facet	Kevin Bärlocher Cedric A. J. Hutter A. Leoni Swart Bernhard Steiner Amanda Welin Michael Hohl François Letourneur Markus A. Seeger Hubert Hilbi
author_sort	Kevin Bärlocher
title	Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5
title_short	Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5
title_full	Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5
title_fullStr	Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5
title_full_unstemmed	Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5
title_sort	structural insights into legionella ridl-vps29 retromer subunit interaction reveal displacement of the regulator tbc1d5
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/148a39307e6a423aa3dcf97540bed38e
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Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5

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