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Calmodulin dissociates the STIM1-Orai1 complex and STIM1 oligomers

Xin Li, Guangyan Wu, Yin Yang, Shijuan Fu, Xiaofen Liu, Huimin Kang, Xue Yang (), Xun-Cheng Su () and Yuequan Shen ()
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Xin Li: Nankai University
Guangyan Wu: Nankai University
Yin Yang: Nankai University
Shijuan Fu: Nankai University
Xiaofen Liu: Nankai University
Huimin Kang: Nankai University
Xue Yang: Nankai University
Xun-Cheng Su: Nankai University
Yuequan Shen: Nankai University

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract 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 (Ca2+-CaM) binds to the core region of activated STIM1. This interaction facilitates slow Ca2+-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 coupling region. The binding of Ca2+-CaM to activated STIM1 disrupts the STIM1–Orai1 complex and also disassembles STIM1 oligomer. Based on these results we propose a model for the calcium-bound CaM-regulated deactivation of SOCE.

Date: 2017
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DOI: 10.1038/s41467-017-01135-w

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