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Journal of Cellular Physiology, 2023
AbstractPalmitoylation, a critical lipid modification of proteins, is involved in various physiological processes such as altering protein localization, transport, and stability, which perform essential roles in protein function. Palmitoyltransferases are specific enzymes involved in the palmitoylation modification of substrates.
Qian Zheng
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AbstractPalmitoylation, a critical lipid modification of proteins, is involved in various physiological processes such as altering protein localization, transport, and stability, which perform essential roles in protein function. Palmitoyltransferases are specific enzymes involved in the palmitoylation modification of substrates.
Qian Zheng
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Palmitoylation, pathogens and their host
Biochemical Society Transactions, 2013 S-Palmitoylation, the only reversible post-translational lipid modification, confers unique biochemical and functional properties to proteins. Although it has long been known that viral proteins are palmitoylated, recent studies reveal that this modification plays a critical role for pathogens of all kinds and at multiple steps of their life cycle. The
Blanc Mathieu +2 more
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Assays of protein palmitoylation
Methods, 2006Protein palmitoylation plays an important role in the structure and function of a wide array of proteins. Unlike other lipid modifications, protein palmitoylation is highly dynamic and cycles of palmitoylation and depalmitoylation can regulate protein function and localization.
Renaldo C Drisdel, William N Green
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Protein cysteine palmitoylation in immunity and inflammation
FEBS Journal, 2021 Protein cysteine palmitoylation, or S-palmitoylation, has been known for about 40 years and thousands for proteins in humans are known to be modified.
Hening Lin
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Biochemical and Biophysical Research Communications, 1997
Tubulin is a very water soluble protein, yet a significant portion is firmly associated with cell membranes. Because recent work has shown that palmitoylation is a dynamic process that can alter the targeting of proteins to membranes, we tested whether or not tubulin could be palmitoylated to account for its membrane location.
A M, Zambito, J, Wolff
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Tubulin is a very water soluble protein, yet a significant portion is firmly associated with cell membranes. Because recent work has shown that palmitoylation is a dynamic process that can alter the targeting of proteins to membranes, we tested whether or not tubulin could be palmitoylated to account for its membrane location.
A M, Zambito, J, Wolff
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Palmitoylation and palmitoyl-transferases in Plasmodium parasites
Biochemical Society Transactions, 2015Protein post-translational modifications (PTM) are commonly used to regulate biological processes. Protein S-acylation is an enzymatically regulated reversible modification that has been shown to modulate protein localization, activity and membrane binding.
Nicola, Hodson +3 more
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Palmitoylation as a Signal for Delivery
2020The ligands and receptors in immune checkpoint signaling are typically transmembrane proteins, which may be regulated by palmitoylation as a reversible lipid modification. Our recent work demonstrated that palmitoylation reduces the lysosomal degradation of PD-L1 trafficking and may present a new therapeutic target.
Yiting, Wang +3 more
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Protein palmitoylation and subcellular trafficking
Biochimica Et Biophysica Acta - Biomembranes, 2011 Protein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues with the 16-carbon fatty acid palmitate, is the most common acylation of proteins in eukaryotic cells.
Clara Aicart-Ramos +1 more
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Palmitoylation of serotonin receptors
Biochemical Society Transactions, 2013The covalent attachment of palmitic acid to one or more cysteine residues (S-palmitoylation) is a widespread modification of signalling proteins. With the finding that palmitoylation is a dynamic process, it is now widely accepted that repeated cycles of palmitoylation/depalmitoylation could be involved in the regulation of multiple signalling ...
Nataliya, Gorinski, Evgeni, Ponimaskin
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