Regulation of Orai1/STIM1 Function by S-Acylation
نویسندگان
چکیده
منابع مشابه
Ion channel regulation by protein S-acylation
Protein S-acylation, the reversible covalent fatty-acid modification of cysteine residues, has emerged as a dynamic posttranslational modification (PTM) that controls the diversity, life cycle, and physiological function of numerous ligand- and voltage-gated ion channels. S-acylation is enzymatically mediated by a diverse family of acyltransferases (zDHHCs) and is reversed by acylthioesterases....
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چکیده ندارد.
15 صفحه اولThe physiology of protein S-acylation.
Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto intracellular cysteine residues of soluble and tr...
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Introduction The aminopropyl groups in spermidine and spermine are obtained from S-adenosylmethionine (AdoMet) after its decarboxylation by the action of the enzyme S-adenosylmethionine decarboxylase (AcloMetDC) [ 1,2]. Once decarboxylated, AdoMet no longer serves as a methyl donor. AdoMetDC is, therefore, not only critical for polyamine biosynthesis but plays a key role in determining the disp...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2020
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2019.11.2292