Structural basis for PtdInsP2-mediated human TRPML1 regulation

Transient receptor potential mucolipin 1 (TRPML1) is a lysosomal channel which maintains the low pH and calcium levels for lysosomal function. Here authors use structural biology and electrophysiology to show how lipids bind and allosterically activate TRPML1.

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Detalles Bibliográficos
Autores principales:	Michael Fine, Philip Schmiege, Xiaochun Li
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3d5601d34f4f4819b821e2d7b34bcf07
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spelling	oai:doaj.org-article:3d5601d34f4f4819b821e2d7b34bcf072021-12-02T17:32:31ZStructural basis for PtdInsP2-mediated human TRPML1 regulation10.1038/s41467-018-06493-72041-1723https://doaj.org/article/3d5601d34f4f4819b821e2d7b34bcf072018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06493-7https://doaj.org/toc/2041-1723Transient receptor potential mucolipin 1 (TRPML1) is a lysosomal channel which maintains the low pH and calcium levels for lysosomal function. Here authors use structural biology and electrophysiology to show how lipids bind and allosterically activate TRPML1.Michael FinePhilip SchmiegeXiaochun LiNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-8 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Michael Fine Philip Schmiege Xiaochun Li Structural basis for PtdInsP2-mediated human TRPML1 regulation
description	Transient receptor potential mucolipin 1 (TRPML1) is a lysosomal channel which maintains the low pH and calcium levels for lysosomal function. Here authors use structural biology and electrophysiology to show how lipids bind and allosterically activate TRPML1.
format	article
author	Michael Fine Philip Schmiege Xiaochun Li
author_facet	Michael Fine Philip Schmiege Xiaochun Li
author_sort	Michael Fine
title	Structural basis for PtdInsP2-mediated human TRPML1 regulation
title_short	Structural basis for PtdInsP2-mediated human TRPML1 regulation
title_full	Structural basis for PtdInsP2-mediated human TRPML1 regulation
title_fullStr	Structural basis for PtdInsP2-mediated human TRPML1 regulation
title_full_unstemmed	Structural basis for PtdInsP2-mediated human TRPML1 regulation
title_sort	structural basis for ptdinsp2-mediated human trpml1 regulation
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/3d5601d34f4f4819b821e2d7b34bcf07
work_keys_str_mv	AT michaelfine structuralbasisforptdinsp2mediatedhumantrpml1regulation AT philipschmiege structuralbasisforptdinsp2mediatedhumantrpml1regulation AT xiaochunli structuralbasisforptdinsp2mediatedhumantrpml1regulation
_version_	1718380242764038144

Structural basis for PtdInsP2-mediated human TRPML1 regulation

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