Stress-induced Changes in the S-palmitoylation and S-nitrosylation of Synaptic Proteins.

ABSTRACT: The precise regulation of synaptic integrity is critical for neuronal network connectivity and proper brain function. Essential aspects of the activity and localization of synaptic proteins are regulated by posttranslational modifications. S-palmitoylation is a reversible covalent modification of the cysteine with palmitate. It modulates affinity of the protein for cell membranes and membranous compartments. Intracellular palmitoylation dynamics are regulated by crosstalk with other posttranslational modifications, such as S-nitrosylation. S-nitrosylation is a covalent modification of cysteine thiol by nitric oxide and can modulate protein functions. Therefore, simultaneous identification of endogenous site-specific proteomes of both cysteine modifications under certain biological conditio

SUBMITTER: Zareba-Koziol M 

PROVIDER: S-EPMC6773552 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature