Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release

Sortilin is an endocytosis receptor with a luminal β-propeller domain. Here the authors present the structures of the β-propeller domain at neutral and acidic pH, which reveal that sortilin dimerises and undergoes conformational changes at low pH and further propose a model for low pH-induced ligand...

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Autores principales:	Nadia Leloup, Philip Lössl, Dimphna H. Meijer, Martha Brennich, Albert J. R. Heck, Dominique M. E. Thies-Weesie, Bert J. C. Janssen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6012de2c7ca2445a89156e52dab21cee
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spelling	oai:doaj.org-article:6012de2c7ca2445a89156e52dab21cee2021-12-02T15:37:00ZLow pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release10.1038/s41467-017-01485-52041-1723https://doaj.org/article/6012de2c7ca2445a89156e52dab21cee2017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01485-5https://doaj.org/toc/2041-1723Sortilin is an endocytosis receptor with a luminal β-propeller domain. Here the authors present the structures of the β-propeller domain at neutral and acidic pH, which reveal that sortilin dimerises and undergoes conformational changes at low pH and further propose a model for low pH-induced ligand release by endocytosis receptors.Nadia LeloupPhilip LösslDimphna H. MeijerMartha BrennichAlbert J. R. HeckDominique M. E. Thies-WeesieBert J. C. JanssenNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-16 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nadia Leloup Philip Lössl Dimphna H. Meijer Martha Brennich Albert J. R. Heck Dominique M. E. Thies-Weesie Bert J. C. Janssen Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
description	Sortilin is an endocytosis receptor with a luminal β-propeller domain. Here the authors present the structures of the β-propeller domain at neutral and acidic pH, which reveal that sortilin dimerises and undergoes conformational changes at low pH and further propose a model for low pH-induced ligand release by endocytosis receptors.
format	article
author	Nadia Leloup Philip Lössl Dimphna H. Meijer Martha Brennich Albert J. R. Heck Dominique M. E. Thies-Weesie Bert J. C. Janssen
author_facet	Nadia Leloup Philip Lössl Dimphna H. Meijer Martha Brennich Albert J. R. Heck Dominique M. E. Thies-Weesie Bert J. C. Janssen
author_sort	Nadia Leloup
title	Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
title_short	Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
title_full	Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
title_fullStr	Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
title_full_unstemmed	Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
title_sort	low ph-induced conformational change and dimerization of sortilin triggers endocytosed ligand release
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6012de2c7ca2445a89156e52dab21cee
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Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release

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