Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29

VARP is bound to endosomes and functions as a protein:protein interaction platform. Here, the authors present the NMR structure of the complex between the retromer subunit VPS29 and a VARP Zn-fingernail microdomain that is structurally distinct from Zn-fingers and further show that mutations, which...

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Autores principales:	Harriet Crawley-Snowdon, Ji-Chun Yang, Nathan R. Zaccai, Luther J. Davis, Lena Wartosch, Emily K. Herman, Nicholas A. Bright, James S. Swarbrick, Brett M. Collins, Lauren P. Jackson, Matthew N. J. Seaman, J. Paul Luzio, Joel B. Dacks, David Neuhaus, David J. Owen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5179c14a82ba4080bfd7a8f14df6270f
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spelling	oai:doaj.org-article:5179c14a82ba4080bfd7a8f14df6270f2021-12-02T18:07:53ZMechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS2910.1038/s41467-020-18773-22041-1723https://doaj.org/article/5179c14a82ba4080bfd7a8f14df6270f2020-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18773-2https://doaj.org/toc/2041-1723VARP is bound to endosomes and functions as a protein:protein interaction platform. Here, the authors present the NMR structure of the complex between the retromer subunit VPS29 and a VARP Zn-fingernail microdomain that is structurally distinct from Zn-fingers and further show that mutations, which abolish VPS29:VARP binding, inhibit trafficking from endosomes to the cell surface.Harriet Crawley-SnowdonJi-Chun YangNathan R. ZaccaiLuther J. DavisLena WartoschEmily K. HermanNicholas A. BrightJames S. SwarbrickBrett M. CollinsLauren P. JacksonMatthew N. J. SeamanJ. Paul LuzioJoel B. DacksDavid NeuhausDavid J. OwenNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Harriet Crawley-Snowdon Ji-Chun Yang Nathan R. Zaccai Luther J. Davis Lena Wartosch Emily K. Herman Nicholas A. Bright James S. Swarbrick Brett M. Collins Lauren P. Jackson Matthew N. J. Seaman J. Paul Luzio Joel B. Dacks David Neuhaus David J. Owen Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
description	VARP is bound to endosomes and functions as a protein:protein interaction platform. Here, the authors present the NMR structure of the complex between the retromer subunit VPS29 and a VARP Zn-fingernail microdomain that is structurally distinct from Zn-fingers and further show that mutations, which abolish VPS29:VARP binding, inhibit trafficking from endosomes to the cell surface.
format	article
author	Harriet Crawley-Snowdon Ji-Chun Yang Nathan R. Zaccai Luther J. Davis Lena Wartosch Emily K. Herman Nicholas A. Bright James S. Swarbrick Brett M. Collins Lauren P. Jackson Matthew N. J. Seaman J. Paul Luzio Joel B. Dacks David Neuhaus David J. Owen
author_facet	Harriet Crawley-Snowdon Ji-Chun Yang Nathan R. Zaccai Luther J. Davis Lena Wartosch Emily K. Herman Nicholas A. Bright James S. Swarbrick Brett M. Collins Lauren P. Jackson Matthew N. J. Seaman J. Paul Luzio Joel B. Dacks David Neuhaus David J. Owen
author_sort	Harriet Crawley-Snowdon
title	Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
title_short	Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
title_full	Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
title_fullStr	Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
title_full_unstemmed	Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29
title_sort	mechanism and evolution of the zn-fingernail required for interaction of varp with vps29
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/5179c14a82ba4080bfd7a8f14df6270f
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Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29

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