Efficient S-Acylation of Thiourea
نویسندگان
چکیده
منابع مشابه
The 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...
متن کاملS-acylation regulates Kv1.5 channel surface expression.
The number of ion channels expressed on the cell surface shapes the complex electrical response of excitable cells. An imbalance in the ratio of inward and outward conducting channels is unfavorable and often detrimental. For example, over- or underexpression of voltage-gated K(+) (Kv) channels can be cytotoxic and in some cases lead to disease. In this study, we demonstrated a novel role for S...
متن کاملS-acylation by the DHHC protein family.
A family of 23 DHHC (Asp-His-His-Cys) proteins that function as mammalian S-acyltransferases has been identified, reinvigorating the study of protein S-acylation. Recent studies have continued to reveal how S-acylation affects target proteins, and have provided glimpses of how DHHC-substrate specificity might be achieved.
متن کاملIon 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....
متن کاملThe Golgi S-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity and S-acylation activity
S-acylation, the attachment of fatty acids onto cysteine residues, regulates protein trafficking and function and is mediated by a family of zDHHC enzymes. The S-acylation of peripheral membrane proteins has been proposed to occur at the Golgi, catalyzed by an S-acylation machinery that displays little substrate specificity. To advance understanding of how S-acylation of peripheral membrane pro...
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ژورنال
عنوان ژورنال: SynOpen
سال: 2018
ISSN: 2509-9396
DOI: 10.1055/s-0037-1610370