Yoo Jung Choi's research while affiliated with The University of Western Ontario and other places
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Publications (3)
Stromal interaction molecule-1 (STIM1) is a type-I transmembrane protein located on the endoplasmic reticulum (ER) and plasma membranes (PM). ER-resident STIM1 regulates the activity of PM Orai1 channels in a process known as store operated calcium (Ca²⁺) entry which is the principal Ca²⁺ signaling process that drives the immune response. STIM1 und...
A major intracellular calcium (Ca(2+)) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca(2+) entry (SOCE). SOCE is the process by which endoplasmic reticulum (ER)-stored Ca(2+) depletion leads to activation of plasma membrane Ca(2+) channels to provide a sustained increase in cytosolic Ca(2+) levels that media...
Citations
... This cell surface targeting is mediated by N-glycosylation of Asn131 and Asn171 [1,2,66,[79][80][81]. Both these Asn residues are located within the EF-SAM domain, and recent solution NMR approaches have shed light into the structural mechanisms of regulation via modifications at these sites [82,83]. Site-selective covalent attachment of glucose at Asn131 and Asn171 in isolated STIM1 EF-SAM resulted in a reduced Ca 2+ binding affinity, concomitant loss in stability and enhanced oligomerization propensity of the domain; moreover, the two simultaneous modifications were found to cause structural changes which pervaded through the EF-SAM core [82]. ...
... core α8 helix, in the EF-SAM domain, resulting in enhanced Ca 2+ influx through CRAC channels 19 , whether deglycosylation enzyme is involved or further modification of STIM1 glycosylation remains elusive. There remains an important gap in understanding the mechanisms by which Glu II regulates STIM1 activation even after two decades. ...
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