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TRIC-A shapes oscillatory Ca2+ signals by interaction with STIM1/Orai1 complexes.

PLoS Biol. 2020 Apr 24;18(4):e3000700. eCollection 2020 Apr
Niroj Shrestha 1 , Bernadett Bacsa 1 , Hwei Ling Ong 2 , Susanne Scheruebel 1 , Helmut Bischof 3 , Roland Malli 3 , Indu Suresh Ambudkar 2 , Klaus Groschner 1
Niroj Shrestha 1 , Bernadett Bacsa 1 , Hwei Ling Ong 2 , Susanne Scheruebel 1 , Helmut Bischof 3 , Roland Malli 3 , Indu Suresh Ambudkar 2 , Klaus Groschner 1
+ et al

[No authors listed]

Author information
  • 1 Gottfried Schatz Research Center-Biophysics, Medical University of Graz, Graz, Austria.
  • 2 Secretory Physiology Section, NIDCR, NIH, Bethesda, Maryland, United States of America.
  • 3 Gottfried Schatz Research Center-Molecular Biology and Biochemistry, Medical University of Graz, Graz, Austria.

摘要


Trimeric intracellular cation (TRIC) channels have been proposed to modulate Ca2+ release from the endoplasmic reticulum (ER) and determine oscillatory Ca2+ signals. Here, we report that TRIC-A-mediated amplitude and frequency modulation of ryanodine receptor 2 (RyR2)-mediated Ca2+ oscillations and inositol 1,4,5-triphosphate receptor (IP3R)-induced cytosolic signals is based on attenuating store-operated Ca2+ entry (SOCE). Further, TRIC-A-dependent delay in ER Ca2+ store refilling contributes to shaping the pattern of Ca2+ oscillations. Upon ER Ca2+ depletion, TRIC-A clusters with stromal interaction molecule 1 (STIM1) and Ca2+-release-activated Ca2+ channel 1 (Orai1) within ER-plasma membrane (PM) junctions and impairs assembly of the STIM1/Orai1 complex, causing a decrease in Orai1-mediated Ca2+ current and SOCE. Together, our findings demonstrate that TRIC-A is a negative regulator of STIM1/Orai1 function. Thus, aberrant SOCE could contribute to muscle disorders associated with loss of TRIC-A.