Calmodulin dissociates the STIM1-Orai1 complex and STIM1 oligomers

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(2+)-CaM) binds to the core region of activated STIM1. This interaction facilitates slow Ca(2+)-dependent...

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Detalles Bibliográficos
Autores principales: Li, Xin, Wu, Guangyan, Yang, Yin, Fu, Shijuan, Liu, Xiaofen, Kang, Huimin, Yang, Xue, Su, Xun-Cheng, Shen, Yuequan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5648805/
https://www.ncbi.nlm.nih.gov/pubmed/29051492
http://dx.doi.org/10.1038/s41467-017-01135-w
Descripción
Sumario: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(2+)-CaM) binds to the core region of activated STIM1. This interaction facilitates slow Ca(2+)-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 Ca(2+)-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.

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