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Related Concept Videos

Feedback Inhibition00:46

Feedback Inhibition

Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

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Related Experiment Video

Updated: May 15, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)
16:33

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)

Published on: February 18, 2013

Profiling and inhibiting reversible palmitoylation.

Jeannie L Hernandez1, Jaimeen D Majmudar, Brent R Martin

  • 1Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

Current Opinion in Chemical Biology
|January 5, 2013
PubMed
Summary
This summary is machine-generated.

Protein palmitoylation, a key modification for protein function, is dynamically regulated by enzymes called protein thioesterases. New tools are emerging to study this process and develop drugs targeting oncogenic proteins.

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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
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Last Updated: May 15, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)
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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
08:28

Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins

Published on: March 29, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein palmitoylation is a reversible posttranslational modification involving the attachment of fatty acids to cysteine residues.
  • This modification is crucial for the membrane localization, structural organization, and functional activity of numerous proteins.
  • Palmitoylation levels are tightly regulated through both spontaneous deacylation and enzymatic removal by protein thioesterases.

Purpose of the Study:

  • To highlight the regulatory role of protein thioesterases in controlling palmitoylation dynamics.
  • To emphasize the importance of thioesterases in organizing oncogenic proteins like Ras GTPases.
  • To introduce novel tools for investigating enzyme-mediated regulation of palmitoylation.

Main Methods:

  • Utilizing bioorthogonal pulse-chase labeling techniques to track palmitoylation.
  • Developing and employing new inhibitors and chemical probes.
  • Applying advanced proteomics methodologies.

Main Results:

  • Demonstrated the critical role of protein thioesterases in regulating palmitoylation.
  • Showcased the involvement of thioesterases in the spatial control of oncogenic proteins.
  • Highlighted the potential of new tools to dissect enzymatic regulation of palmitoylation.

Conclusions:

  • Protein thioesterases are key enzymes controlling dynamic protein palmitoylation.
  • Understanding palmitoylation regulation offers new avenues for therapeutic interventions, particularly for cancer.
  • Emerging chemical biology tools will significantly advance research in this field.