1991
DOI: 10.1016/0006-291x(91)91859-b
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Insulin stimulates fatty acid acylation of adipocyte proteins

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Cited by 21 publications
(10 citation statements)
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“…Another potential mechanism is the direct interaction of palmitate with specific motifs on phosphatases or substrates, which may subsequently protect the phosphorylated site from dephosphorylation. Spontaneous or insulininducible palmitoylation of specific proteins susceptible to such modifications may also pro-vide this protection [Quesnel and Silvius, 1994;Jochen et al, 1991]. Careful biochemical studies must be done to confirm direct inhibition of PTPase activity by palmitate and determine the precise mechanism of inhibition.…”
Section: Discussionmentioning
confidence: 99%
“…Another potential mechanism is the direct interaction of palmitate with specific motifs on phosphatases or substrates, which may subsequently protect the phosphorylated site from dephosphorylation. Spontaneous or insulininducible palmitoylation of specific proteins susceptible to such modifications may also pro-vide this protection [Quesnel and Silvius, 1994;Jochen et al, 1991]. Careful biochemical studies must be done to confirm direct inhibition of PTPase activity by palmitate and determine the precise mechanism of inhibition.…”
Section: Discussionmentioning
confidence: 99%
“…Unlike other lipid modifications of proteins, such as myristoylation, isoprenylation and addition of glycosyl-phosphatidylinositol, palmitic acid turns over with a much shorter half-life than that of the protein (Staufenbiel and Lazarides, 1986;Magee et al, 1987;Sefton and Buss, 1987;Schultz et al, 1988;Skene and Virag, 1989). This rapid turnover and the variation of palmitoylation levels with extracellular stimuli Oxford University Press (Huang, 1989;James and Olson, 1989;Jochen et al, 1991) strongly suggest that addition or removal of palmitate regulates the activity of proteins.…”
Section: Introductionmentioning
confidence: 99%
“…In the majority of the cases, the chemically bound acyl chains turn over much faster than the protein backbone, implying that palmitoylation is a regulatory modification. In fact, fatty acylation of this and other types of proteins has been shown to be modulated by physiological (7)(8)(9) or pharmacological stimuli (10 -14). To date, the metabolic features of palmitoylation have only been studied by labeling cultured cells with [ 3 H]palmitic acid, and the half-life of the palmitate has been estimated from the disappearance of the protein-bound radioactivity after isotopic dilution with the unlabeled fatty acid.…”
mentioning
confidence: 99%