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Characterizing The Structural, Biophysical And Functional Effects Of S-Glutathionylation On Stim1 Ca2+ Sensing, Christian Michael Sirko
Characterizing The Structural, Biophysical And Functional Effects Of S-Glutathionylation On Stim1 Ca2+ Sensing, Christian Michael Sirko
Electronic Thesis and Dissertation Repository
Stromal interaction molecule 1 (STIM1) is an endo/sarcoplasmic reticulum (ER/SR) calcium (Ca2+) sensing protein that initiates cytoplasmic Ca2+ influx via store-operated calcium entry (SOCE). STIM1, in conjunction with Orai, a plasma membrane (PM) protein, function as mediators of SOCE through the formation of calcium-release activated calcium (CRAC) channels. S-Glutathionylation of STIM1 at Cys56 has been shown to evoke constitutive Ca2+ entry in DT40 cells, however no studies have carefully investigated the biophysical and structural effects of this covalent modification to the luminal domain, which are critical for understanding the molecular mechanism underlying the regulation of …
Excess No Stabilizes The Luminal Domain Of Stim2 In A Cys-Specific Manner Thereby Regulating Basal Calcium Homeostasis And Store-Operated Calcium Entry, Matthew Novello
Excess No Stabilizes The Luminal Domain Of Stim2 In A Cys-Specific Manner Thereby Regulating Basal Calcium Homeostasis And Store-Operated Calcium Entry, Matthew Novello
Electronic Thesis and Dissertation Repository
Stromal-interaction molecule 2 (STIM2) is an endoplasmic reticulum (ER) membrane-inserted Ca2+-sensing protein which, together with the plasma membrane Ca2+ channel Orai1, regulates basal Ca2+ homeostasis and store-operated Ca2+ entry (SOCE). Recent evidence suggests that S-nitrosylation, which is the covalent attachment of a nitric oxide (NO) moiety to a cysteine thiol, can attenuate the function of the paralog STIM1 protein. Compared to STIM1, STIM2 also functions as a basal Ca2+ homeostatic feedback regulator. Therefore, the objective of my study was to evaluate the susceptibility of STIM2 to S-nitrosylation and the effects that this …
S-Nitrosylation Suppresses Stromal Interaction Molecule-1 Activation And Ameliorates Cardiomyocyte Hypertrophy, Jinhui Zhu
Electronic Thesis and Dissertation Repository
Stromal interaction molecule 1 (STIM1) is an endo/sarcoplasmic reticulum (ER/SR) calcium (Ca2+) sensor that activates store-operated Ca2+ entry (SOCE) following Ca2+ depletion. SOCE-induced elevation of cytosolic Ca2+ stimulates the calcineurin/nuclear factor of activated T cells (NFAT) pathway, which upregulates pro-hypertrophic gene transcription. Nitric oxide (NO) regulates protein functions by S-nitrosylation, but how NO regulates SOCE in inhibiting cardiac hypertrophy is unclear. I hypothesize that NO stabilizes and inhibits STIM1 via S-nitrosylation and mitigates cardiomyocyte hypertrophy. STIM1 residues Cys49 and Cys56 were susceptible to S-nitrosylation by S-nitrosoglutathione (GSNO) and sodium nitroprusside (SNP), …