Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel

Hetero-oligomeric TRP-like channels such as PKD1L3/PKD2L1 play crucial roles in a range of physiological and pathophysiological processes. Here, the authors present the cryo-EM structures of a minimal functional murine PKD1L3/PKD2L1 complex in the absence and presence of calcium and further supporte...

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Main Authors:	Qiang Su, Mengying Chen, Yan Wang, Bin Li, Dan Jing, Xiechao Zhan, Yong Yu, Yigong Shi
Format:	article
Language:	EN
Published:	Nature Portfolio 2021
Subjects:	Science Q
Online Access:	https://doaj.org/article/a58b79945a0d42c5b08a86652fb5596b
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spelling	oai:doaj.org-article:a58b79945a0d42c5b08a86652fb5596b2021-12-02T18:50:44ZStructural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel10.1038/s41467-021-25216-z2041-1723https://doaj.org/article/a58b79945a0d42c5b08a86652fb5596b2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25216-zhttps://doaj.org/toc/2041-1723Hetero-oligomeric TRP-like channels such as PKD1L3/PKD2L1 play crucial roles in a range of physiological and pathophysiological processes. Here, the authors present the cryo-EM structures of a minimal functional murine PKD1L3/PKD2L1 complex in the absence and presence of calcium and further supported through structure-guided mutagenic studies, they discuss the mechanism of calcium-induced channel activation.Qiang SuMengying ChenYan WangBin LiDan JingXiechao ZhanYong YuYigong ShiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Qiang Su Mengying Chen Yan Wang Bin Li Dan Jing Xiechao Zhan Yong Yu Yigong Shi Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
description	Hetero-oligomeric TRP-like channels such as PKD1L3/PKD2L1 play crucial roles in a range of physiological and pathophysiological processes. Here, the authors present the cryo-EM structures of a minimal functional murine PKD1L3/PKD2L1 complex in the absence and presence of calcium and further supported through structure-guided mutagenic studies, they discuss the mechanism of calcium-induced channel activation.
format	article
author	Qiang Su Mengying Chen Yan Wang Bin Li Dan Jing Xiechao Zhan Yong Yu Yigong Shi
author_facet	Qiang Su Mengying Chen Yan Wang Bin Li Dan Jing Xiechao Zhan Yong Yu Yigong Shi
author_sort	Qiang Su
title	Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_short	Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_full	Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_fullStr	Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_full_unstemmed	Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_sort	structural basis for ca2+ activation of the heteromeric pkd1l3/pkd2l1 channel
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a58b79945a0d42c5b08a86652fb5596b
work_keys_str_mv	AT qiangsu structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT mengyingchen structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT yanwang structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT binli structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT danjing structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT xiechaozhan structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT yongyu structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel AT yigongshi structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
_version_	1718377523052544000

Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel

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