Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii

Transient receptor potential (TRP) channels are ubiquitous occurring cation-selective sensory ion channels that respond to various stimuli. Here the authors characterize crTRP1 from the alga Chlamydomonas reinhardtii, present its 3.5 Å cryo-EM structure and show that crTRP1 opens in response to incr...

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Autores principales:	Luke L. McGoldrick, Appu K. Singh, Lusine Demirkhanyan, Ting-Yu Lin, Ryan G. Casner, Eleonora Zakharian, Alexander I. Sobolevsky
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/63a0a3a8fc3a440ba91ed9cb0c51a78f
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spelling	oai:doaj.org-article:63a0a3a8fc3a440ba91ed9cb0c51a78f2021-12-02T16:58:18ZStructure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii10.1038/s41467-019-12121-92041-1723https://doaj.org/article/63a0a3a8fc3a440ba91ed9cb0c51a78f2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12121-9https://doaj.org/toc/2041-1723Transient receptor potential (TRP) channels are ubiquitous occurring cation-selective sensory ion channels that respond to various stimuli. Here the authors characterize crTRP1 from the alga Chlamydomonas reinhardtii, present its 3.5 Å cryo-EM structure and show that crTRP1 opens in response to increased temperature and is positively regulated by the membrane lipid PIP2.Luke L. McGoldrickAppu K. SinghLusine DemirkhanyanTing-Yu LinRyan G. CasnerEleonora ZakharianAlexander I. SobolevskyNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Luke L. McGoldrick Appu K. Singh Lusine Demirkhanyan Ting-Yu Lin Ryan G. Casner Eleonora Zakharian Alexander I. Sobolevsky Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii
description	Transient receptor potential (TRP) channels are ubiquitous occurring cation-selective sensory ion channels that respond to various stimuli. Here the authors characterize crTRP1 from the alga Chlamydomonas reinhardtii, present its 3.5 Å cryo-EM structure and show that crTRP1 opens in response to increased temperature and is positively regulated by the membrane lipid PIP2.
format	article
author	Luke L. McGoldrick Appu K. Singh Lusine Demirkhanyan Ting-Yu Lin Ryan G. Casner Eleonora Zakharian Alexander I. Sobolevsky
author_facet	Luke L. McGoldrick Appu K. Singh Lusine Demirkhanyan Ting-Yu Lin Ryan G. Casner Eleonora Zakharian Alexander I. Sobolevsky
author_sort	Luke L. McGoldrick
title	Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii
title_short	Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii
title_full	Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii
title_fullStr	Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii
title_full_unstemmed	Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii
title_sort	structure of the thermo-sensitive trp channel trp1 from the alga chlamydomonas reinhardtii
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/63a0a3a8fc3a440ba91ed9cb0c51a78f
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Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii

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