Life Sciences Commons^™

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 …

Structure And Function Of Stomatin-Like Protein 2, Safee Mian

Electronic Thesis and Dissertation Repository

Stomatin-like protein 2 (SLP-2), a member of the SPFH superfamily, is a mitochondrial inner membrane protein required for optimal mitochondrial respiration. SLP-2 binds to the important mitochondrial phospholipid cardiolipin (CL) and has been proposed to mediate formation of CL-enriched microdomains that would foster respiratory chain supercomplex (RCS) formation and stability. However, little is known about how SLP-2 structure facilitates its cellular function. The goal of this thesis was to elucidate if and how SLP-2 oligomerizes and by what means does it bind CL.

Biophysical analysis of the expressed SLP-2 SPFH domain, either with or without flanking residues, indicates it to …