Protein S -palmitoylation in immunity

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Protein S-palmitoylation in cellular differentiation

Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein-protein and membrane-protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in eukaryotes with the potential to coordinate di...

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Protein palmitoylation by a family of DHHC protein S-acyltransferases.

Protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the side chain of cysteine, forming a thioester linkage. This acyl modification is readily reversible, providing a potential regulatory mechanism to mediate protein-membrane interactions and subcellular trafficking of proteins. The mechanism that underlies the transfer of palmitate or other long-chain f...

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Emerging roles for protein S-palmitoylation in Toxoplasma biology.

Post-translational modifications are refined, rapidly responsive and powerful ways to modulate protein function. Among post-translational modifications, acylation is now emerging as a widespread modification exploited by eukaryotes, bacteria and viruses to control biological processes. Protein palmitoylation involves the attachment of palmitic acid, also known as hexadecanoic acid, to cysteine ...

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ژورنال

عنوان ژورنال: Open Biology

سال: 2021

ISSN: 2046-2441

DOI: 10.1098/rsob.200411