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STIM2 promotes store-operated calcium entry via enhancing recruitment of STIM1 to the ER-PM junctions

 

Store-operated calcium entry (SOCE) is a process that mediates Ca2+ signals to regulate physiological functions in various cell types. This process occurs in endoplasmic reticulum- plasma membrane (ER-PM) junctions and is activated by the interaction of channel Orai1, localized in PM, and Ca2+-sensing protein STIM1, localized in ER. Ong et al. found STIM2 promotes STIM1 recruitment in ER-PM junctions at low stimulus intensities, results in the enhancement of SOCE. The article was published on Science Signaling.

 

The deletion of STMI2 decreased fluid secretion and SOCE activation, in mouse salivary glands and salivary acinar cells, respectively. Moreover, the knockdown of STIM2 in human embryonic kidney (HEK) 293 cells reduces agonist-induced Ca2+ signaling compared with control cells. By further investigation, they found the absence of five arboxylterminal amino acid residues of STIM2 disrupts its effect on recruitment of STIM1 at low concentrations of agonist, meanwhile, the coexpression of STIM2 together with STIM1 lacking the polybasic region leads to co-clustering of both proteins. In conclusion, STIM2 promotes STIM1 recruitment in ER-PM junctions at low stimulus intensities, therefore, leads to the interaction of STIM1 and Orail1, finally enhances SOCE activation.

 

Reference:
Sci Signal. 2015 Jan 13;8(359):ra3.