Fatty Acylation of Proteins

Beta-cell hypersensitivity to glucose following 24-h exposure of rat islets to fatty acids

“…A similar conclusion regarding the causative role of hexokinase was recently reported in abstract form based on the use of oleate in transformed beta-cells [28]. Possible mechanisms based on known modulatory effects of fatty acids include acylation [29], increased gene transcription [30], increased production of long chain-CoA products, or a direct effect of fatty acid metabolites on the enzyme activity. Regarding the latter, an inhibitory effect of long chain acyl-CoA esters has been reported for glucokinase [31,32], phosphofructokinase [33], and glucose 6-phosphatase [34]: we are not aware of any reports of stimulation of a glycolytic enzyme such as that noted in this study.…”

Dynamic Palmitoylation Links Cytosol-Membrane Shuttling of Acyl-protein Thioesterase-1 and Acyl-protein Thioesterase-2 with That of Proto-oncogene H-Ras Product and Growth-associated Protein-43

“…Post-translational modifications such as phosphorylation, glycosylation, ubiquitination, and lipidation play critical roles in regulating the function of many proteins (1). Post-translational lipid modifications of proteins facilitate membrane localization, protein-protein interaction, cell signaling, subcellular trafficking, and vesicular transport (1)(2)(3)(4)(5)(6)(7)(8).…”

“…Post-translational lipid modifications of proteins facilitate membrane localization, protein-protein interaction, cell signaling, subcellular trafficking, and vesicular transport (1)(2)(3)(4)(5)(6)(7)(8). Some of the common lipid modifications of proteins include N-myristoylation, palmitoylation, and prenylation, which occur in the cytoplasmic face of the cell membrane (1,5,6). Among these, palmitoylation (also called S-acylation) is the only reversible lipid modification in which a 16-carbon fatty acid (predominantly palmitate) is attached to cysteine residues of polypeptides via thioester linkage (4,6).…”

Association of Serine in Position 1124 of Hantaan Virus Glycoprotein With Virulence in Mice

“…Veit et al (1991) showed that mutagenesis from cysteine to serine of the acylation sites severely inhibits palmitoylation but that it does not impair haemagglutinin-induced polykaryon formation. In the case of HV it is predicted that two residues, a serine and a cysteine in positions 1124 and 1127 of G2, are palmitoylated, because palmitic acid is linked either to serine/threonine residues via oxyester bonds (Stoffel et al, 1983) or to cysteine residues through thioester linkage (Schmidt, 1989). Our preliminary experiments suggest that the G2 protein of HV is palmitoylated (Isegawa et at., unpublished data).…”