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:English
Published: Nature Publishing Group 2021-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-25216-z
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spelling doaj-a58b79945a0d42c5b08a86652fb5596b2021-08-15T11:40:03ZengNature Publishing GroupNature Communications2041-17232021-08-0112111010.1038/s41467-021-25216-zStructural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channelQiang Su0Mengying Chen1Yan Wang2Bin Li3Dan Jing4Xiechao Zhan5Yong Yu6Yigong Shi7Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, School of Medicine, Tsinghua UniversityDepartment of Biological Sciences, St. John’s UniversityDepartment of Biological Sciences, St. John’s UniversityKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityDepartment of Biological Sciences, St. John’s UniversityKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityHetero-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.https://doi.org/10.1038/s41467-021-25216-z
collection DOAJ
language English
format Article
sources DOAJ
author Qiang Su
Mengying Chen
Yan Wang
Bin Li
Dan Jing
Xiechao Zhan
Yong Yu
Yigong Shi
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-08-01
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.
url https://doi.org/10.1038/s41467-021-25216-z
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