Calmodulin dissociates the STIM1-Orai1 complex and STIM1 oligomers.
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ABSTRACT:
SUBMITTER: Li X
PROVIDER: S-EPMC5648805 | biostudies-literature | 2017 Oct
REPOSITORIES: biostudies-literature
Publications
Calmodulin dissociates the STIM1-Orai1 complex and STIM1 oligomers.
Li Xin X Wu Guangyan G Yang Yin Y Fu Shijuan S Liu Xiaofen X Kang Huimin H Yang Xue X Su Xun-Cheng XC Shen Yuequan Y
Nature communications 20171019 1
Store-operated calcium entry (SOCE) is a major pathway for calcium ions influx into cells and has a critical role in various cell functions. Here we demonstrate that calcium-bound calmodulin (Ca<sup>2+</sup>-CaM) binds to the core region of activated STIM1. This interaction facilitates slow Ca<sup>2+</sup>-dependent inactivation after Orai1 channel activation by wild-type STIM1 or a constitutively active STIM1 mutant. We define the CaM-binding site in STIM1, which is adjacent to the STIM1-Orai1 ...[more]
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