Techniques: Profiling protein palmitoylation

2011 ◽  
Author(s):  
Katrin Legg
Keyword(s):  
Protein Palmitoylation

scholarly journals A metabolic modeling approach reveals promising therapeutic targets and antiviral drugs to combat COVID-19

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Fernando Santos-Beneit ◽  
Vytautas Raškevičius ◽  
Vytenis A. Skeberdis ◽  
Sergio Bordel
Keyword(s):  
Literature Search ◽  
Metabolic Modeling ◽  
Bioactive Molecules ◽  
Flux Balance ◽  
Triacsin C ◽  
Protein Palmitoylation ◽  
Positive Sense ◽  
Different Types ◽  
Balance Analysis ◽  
Docking Calculations

AbstractIn this study we have developed a method based on Flux Balance Analysis to identify human metabolic enzymes which can be targeted for therapeutic intervention against COVID-19. A literature search was carried out in order to identify suitable inhibitors of these enzymes, which were confirmed by docking calculations. In total, 10 targets and 12 bioactive molecules have been predicted. Among the most promising molecules we identified Triacsin C, which inhibits ACSL3, and which has been shown to be very effective against different viruses, including positive-sense single-stranded RNA viruses. Similarly, we also identified the drug Celgosivir, which has been successfully tested in cells infected with different types of viruses such as Dengue, Zika, Hepatitis C and Influenza. Finally, other drugs targeting enzymes of lipid metabolism, carbohydrate metabolism or protein palmitoylation (such as Propylthiouracil, 2-Bromopalmitate, Lipofermata, Tunicamycin, Benzyl Isothiocyanate, Tipifarnib and Lonafarnib) are also proposed.

scholarly journals Selenoprotein K and Protein Palmitoylation

2015 ◽  
Vol 23 (10) ◽  
pp. 854-862 ◽  
Author(s):  
Gregory J. Fredericks ◽  
Peter R. Hoffmann
Keyword(s):  
Protein Palmitoylation ◽  
Selenoprotein K

scholarly journals Modulation of insulin secretion from normal rat islets by inhibitors of the post-translational modifications of GTP-binding proteins

1993 ◽  
Vol 295 (1) ◽  
pp. 31-40 ◽  
Author(s):  
S A Metz ◽  
M E Rabaglia ◽  
J B Stock ◽  
A Kowluru
Keyword(s):  
Insulin Secretion ◽  
Insulin Release ◽  
Binding Proteins ◽  
Mevalonic Acid ◽  
Post Translational Modifications ◽  
Gtp Binding Proteins ◽  
Carboxyl Methylation ◽  
Gtp Binding ◽  
Protein Palmitoylation ◽  
Normal Rat

Many GTP-binding proteins (GBPs) are modified by mevalonic acid (MVA)-dependent isoprenylation, carboxyl methylation or palmitoylation. The effects of inhibitors of these processes on insulin release were studied. Intact pancreatic islets were shown to synthesize and metabolize MVA and to prenylate several candidate proteins. Culture with lovastatin (to inhibit synthesis of endogenous MVA) caused the accumulation in the cytosol of low-M(r) GBPs (labelled by the [alpha-32P]GTP overlay technique), suggesting a disturbance of membrane association. Concomitantly, lovastatin pretreatment reduced glucose-induced insulin release by about 50%; co-provision of 100-200 microM MVA totally prevented this effect. Perillic acid, a purported inhibitor of the prenylation of small GBPs, also markedly reduced glucose-induced insulin secretion. Furthermore, both N-acetyl-S-trans, trans-farnesyl-L-cysteine (AFC), which inhibited the base-labile carboxyl methylation of GBPs in islets or in transformed beta-cells, and cerulenic acid, an inhibitor of protein palmitoylation, also reduced nutrient-induced secretion; an inactive analogue of AFC (which did not inhibit carboxyl methylation in islets) had no effect on secretion. In contrast with nutrients, the effects of agonists that induce secretion by directly activating distal components in signal transduction (such as a phorbol ester or mastoparan) were either unaffected or enhanced by lovastatin or AFC. These data are compatible with the hypothesis that post-translational modifications are required for one or more stimulatory GBPs to promote proximal step(s) in fuel-induced insulin secretion, whereas one or more inhibitory GBPs might reduce secretion at a more distal locus.

New Insights into the Mechanisms of Protein Palmitoylation†

Biochemistry ◽  
2003 ◽  
Vol 42 (15) ◽  
pp. 4311-4320 ◽  
Author(s):  
Maurine E. Linder ◽  
Robert J. Deschenes
Keyword(s):  
Protein Palmitoylation

Multiple roles for protein palmitoylation in plants

2008 ◽  
Vol 13 (6) ◽  
pp. 295-302 ◽  
Author(s):  
Piers A. Hemsley ◽  
Claire S. Grierson
Keyword(s):  
Multiple Roles ◽  
Protein Palmitoylation

scholarly journals The intracellular dynamic of protein palmitoylation

2010 ◽  
Vol 191 (7) ◽  
pp. 1229-1238 ◽  
Author(s):  
Christine Salaun ◽  
Jennifer Greaves ◽  
Luke H. Chamberlain
Keyword(s):  
Posttranslational Modifications ◽  
Posttranslational Modification ◽  
Mammalian Cells ◽  
Protein Functionality ◽  
Peripheral Membrane Proteins ◽  
Protein Palmitoylation ◽  
Thioester Bond ◽  
Intracellular Sorting ◽  
Intracellular Dynamic ◽  
Insight Into

S-palmitoylation describes the reversible attachment of fatty acids (predominantly palmitate) onto cysteine residues via a labile thioester bond. This posttranslational modification impacts protein functionality by regulating membrane interactions, intracellular sorting, stability, and membrane micropatterning. Several recent findings have provided a tantalizing insight into the regulation and spatiotemporal dynamics of protein palmitoylation. In mammalian cells, the Golgi has emerged as a possible super-reaction center for the palmitoylation of peripheral membrane proteins, whereas palmitoylation reactions on post-Golgi compartments contribute to the regulation of specific substrates. In addition to palmitoylating and depalmitoylating enzymes, intracellular palmitoylation dynamics may also be controlled through interplay with distinct posttranslational modifications, such as phosphorylation and nitrosylation.

scholarly journals Regulation of the Cardiac Sodium/Calcium Exchanger by Protein Palmitoylation

2014 ◽  
Vol 106 (2) ◽  
pp. 581a
Author(s):  
Louise Reilly ◽  
Donald W. Hilgemann ◽  
Michael L.J. Ashford ◽  
William Fuller
Keyword(s):  
Sodium Calcium Exchanger ◽  
Sodium Calcium ◽  
Protein Palmitoylation
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