Differential effects of acyl-CoA binding protein on enzymatic and non-enzymatic thioacylation of protein and peptide substrates

Dunphy, Julianne T.; Schroeder, H; Leventis, Rania; Greentree, Wendy K.; Knudsen, Jens; Silvius, John R.; Linder, Maurine E.

doi:10.1016/s1388-1981(00)00060-3

Cited by 43 publications

(30 citation statements)

References 47 publications

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“…Attempts at biochemical characterization and cloning of palmitoyltransferases has been hampered by their integral association with membranes and because of their inherent instability in vitro (Berthiaume and Resh, 1995;Dunphy et al, 1996Dunphy et al, , 2000. In agreement, native and recombinant GODZ was found to copurify with membranes.…”

Section: Discussionmentioning

confidence: 87%

The γ2 Subunit of GABA_AReceptors Is a Substrate for Palmitoylation by GODZ

et al. 2004

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The neurotransmitter GABA activates heteropentameric GABA A receptors, which are composed mostly of ␣, ␤, and ␥2 subunits. Regulated membrane trafficking and subcellular targeting of GABA A receptors is important for determining the efficacy of GABAergic inhibitory function. Of special interest is the ␥2 subunit, which is mostly dispensable for assembly and membrane insertion of functional receptors but essential for accumulation of GABA A receptors at synapses. In a search for novel receptor trafficking proteins, we have used the SOS-recruitment system and isolated a Golgi-specific DHHC zinc finger protein (GODZ) as a novel ␥2 subunit-interacting protein.GODZ is a member of the superfamily of DHHC cysteine-rich domain (DHHC-CRD) polytopic membrane proteins shown recently in yeast to represent palmitoyltransferases. GODZ mRNA is found in many tissues; however, in brain the protein is detected in neurons only and highly concentrated and asymmetrically distributed in the Golgi complex. GODZ interacts with a cysteine-rich 14-amino acid domain conserved specifically in the large cytoplasmic loop of ␥1-3 subunits but not in other GABA A receptor subunits. Coexpression of GODZ and GABA A receptors in heterologous cells results in palmitoylation of the ␥2 subunit in a cytoplasmic loop domain-dependent manner. Neuronal GABA A receptors are similarly palmitoylated. Thus, GODZ-mediated palmitoylation represents a novel posttranslational modification that is selective for ␥ subunit-containing GABA A receptor subtypes, a mechanism that is likely to be important for regulated trafficking of these receptors in the secretory pathway.

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Section: Discussionmentioning

confidence: 87%

The γ2 Subunit of GABA_AReceptors Is a Substrate for Palmitoylation by GODZ

et al. 2004

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“…Because most studies of chemical acylation have not included ACBP and have extended the concentration of activated fatty acids even into the millimolar range, their results must be interpreted with great caution. Upon the inclusion of ACBP, chemical acylation of peptides and proteins has been shown to be eliminated; this buffering does not affect DHHC-PAT activity (86,96,98) and the effect on self-palmitoylating proteins has generally not been studied. Cytosolic H3 modification including acetylation or methylation by early acting enzymes prior to chromatin incorporation has been demonstrated (99, 100) and given the ER and perinuclear localization of multiple DHHCPATs (101), it is possible H3 variants are modified before nuclear incorporation, during nuclear breakdown or possibly at the periphery of the nucleus during specific regulatory events (supplemental Fig.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters Reveals S-Acylation of Histone H3 Variants

Wilson

Raghavan

Yang

et al. 2011

Molecular & Cellular Proteomics

129

156

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“…), and it has only recently been established that an enzymatic activity (protein Sacyltransferase) is likely to represent the predominant mechanism for thioacylation (29). Because it is a reversible modification with dynamic cycles of acylation and deacylation, it is capable of playing a role in signal transduction.…”

Section: Discussionmentioning

confidence: 99%

The Effects of Cerulenin, an Inhibitor of Protein Acylation, on the Two Phases of Glucose-Stimulated Insulin Secretion

et al. 2002

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The potential role of protein acylation in the control of biphasic insulin secretion has been studied in isolated rat pancreatic islets. The protein acylation inhibitor cerulenin inhibited both phases of glucose-stimulated insulin secretion. However, it did not affect the secretory response to a depolarizing concentration of KCl in either the absence or presence of diazoxide. Therefore, cerulenin has no deleterious effect on the L-type Ca 2؉ channels or subsequent events in Ca 2؉ stimulus-secretion coupling. Advantage was taken of this to study the effect of cerulenin on the K ATP channel-independent pathway of glucose signaling. In the presence of KCl and diazoxide, cerulenin powerfully inhibited the augmentation of insulin release by glucose and palmitate. Similar inhibition of the augmentation of release by glucose and palmitate was seen under Ca 2؉ -free conditions in the presence of 12-O-tetradecanoylphorbol-13-acetate and forskolin. As neither glucose oxidation nor the effect of glucose to inhibit fatty acid oxidation is affected by cerulenin, these data suggest that protein acylation is involved in the K ATP channel-independent pathway of glucose signaling. Diabetes 51 (Suppl. 1): S91-S95, 2002

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Differential effects of acyl-CoA binding protein on enzymatic and non-enzymatic thioacylation of protein and peptide substrates

Cited by 43 publications

References 47 publications

The γ2 Subunit of GABA_AReceptors Is a Substrate for Palmitoylation by GODZ

The γ2 Subunit of GABA_AReceptors Is a Substrate for Palmitoylation by GODZ

Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters Reveals S-Acylation of Histone H3 Variants

The Effects of Cerulenin, an Inhibitor of Protein Acylation, on the Two Phases of Glucose-Stimulated Insulin Secretion

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Differential effects of acyl-CoA binding protein on enzymatic and non-enzymatic thioacylation of protein and peptide substrates

Cited by 43 publications

References 47 publications

The γ2 Subunit of GABAAReceptors Is a Substrate for Palmitoylation by GODZ

The γ2 Subunit of GABAAReceptors Is a Substrate for Palmitoylation by GODZ

Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters Reveals S-Acylation of Histone H3 Variants

The Effects of Cerulenin, an Inhibitor of Protein Acylation, on the Two Phases of Glucose-Stimulated Insulin Secretion

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The γ2 Subunit of GABA_AReceptors Is a Substrate for Palmitoylation by GODZ

The γ2 Subunit of GABA_AReceptors Is a Substrate for Palmitoylation by GODZ