Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2

Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2

In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade. Here, the authors solve the cryo-EM structure of an osmosensitive channel from Arabidopsis OSCA1.2 in its inactivated state.

Bibliographic Details
Main Authors: Xin Liu, Jiawei Wang, Linfeng Sun
Format: Article
Language:English
Published: Nature Publishing Group 2018-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-07564-5
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spelling doaj-5d3100442c5f47adb2abc76235c01da02021-05-11T09:37:50ZengNature Publishing GroupNature Communications2041-17232018-11-01911910.1038/s41467-018-07564-5Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2Xin Liu0Jiawei Wang1Linfeng Sun2Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of ChinaState Key Laboratory of Membrane Biology, Beijing Advanced Innovation Centre for Structural Biology, School of Life Sciences, Tsinghua UniversityHefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of ChinaIn plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade. Here, the authors solve the cryo-EM structure of an osmosensitive channel from Arabidopsis OSCA1.2 in its inactivated state.https://doi.org/10.1038/s41467-018-07564-5
collection DOAJ
language English
format Article
sources DOAJ
author Xin Liu
Jiawei Wang
Linfeng Sun
spellingShingle Xin Liu
Jiawei Wang
Linfeng Sun
Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
Nature Communications
author_facet Xin Liu
Jiawei Wang
Linfeng Sun
author_sort Xin Liu
title Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
title_short Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
title_full Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
title_fullStr Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
title_full_unstemmed Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2
title_sort structure of the hyperosmolality-gated calcium-permeable channel osca1.2
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-11-01
description In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade. Here, the authors solve the cryo-EM structure of an osmosensitive channel from Arabidopsis OSCA1.2 in its inactivated state.
url https://doi.org/10.1038/s41467-018-07564-5
work_keys_str_mv AT xinliu structureofthehyperosmolalitygatedcalciumpermeablechannelosca12
AT jiaweiwang structureofthehyperosmolalitygatedcalciumpermeablechannelosca12
AT linfengsun structureofthehyperosmolalitygatedcalciumpermeablechannelosca12
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