Ca2+/Calmodulin Binding to STIM1 Hydrophobic Residues Facilitates Slow Ca2+-Dependent Inactivation of the Orai1 Channel | Zendy

Rajesh Bhardwaj | Zendy; Bartłomiej Augustynek | Zendy; Ebru Ercan-Herbst | Zendy; Palanivel Kandasamy | Zendy; Matthias Seedorf | Zendy; Christine Peinelt | Zendy; Matthias A. Hediger | Zendy

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Ca2+/Calmodulin Binding to STIM1 Hydrophobic Residues Facilitates Slow Ca2+-Dependent Inactivation of the Orai1 Channel

Author(s) -

Rajesh Bhardwaj,

Bartłomiej Augustynek,

Ebru Ercan-Herbst,

Palanivel Kandasamy,

Matthias Seedorf,

Christine Peinelt,

Matthias A. Hediger

Publication year - 2020

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.33594/000000218

Subject(s) - orai1 , stim1 , calmodulin , chemistry , microbiology and biotechnology , patch clamp , biophysics , hek 293 cells , gating , biochemistry , endoplasmic reticulum , biology , receptor , enzyme

Store-operated Ca 2+ entry (SOCE) through plasma membrane Ca 2+ channel Orai1 is essential for many cellular processes. SOCE, activated by ER Ca 2+ store-depletion, relies on the gating function of STIM1 Orai1-activating region SOAR of the ER-anchored Ca 2+ -sensing protein STIM1. Electrophysiologically, SOCE is characterized as Ca 2+ release-activated Ca 2+ current (I CRAC ). A major regulatory mechanism that prevents deleterious Ca 2+ overload is the slow Ca 2+ -dependent inactivation (SCDI) of I CRAC . Several studies have suggested a role of Ca 2+ /calmodulin (Ca 2+ /CaM) in triggering SCDI. However, a direct contribution of STIM1 in regulating Ca 2+ /CaM-mediated SCDI of I CRAC is as yet unclear.

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