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Updated: May 13, 2025

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

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

Published on: March 29, 2020

Engineered depalmitoylases enable selective manipulation of protein localization and function.

Srinidhi Jayaraman¹, Audrey Kochiss¹, Thy-Lan Alcalay²

¹Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, USA.

Nature Communications

|April 13, 2025

Summary

Scientists developed new tools to precisely control protein palmitoylation, a key cellular process. This breakthrough allows for targeted manipulation of protein function, offering new avenues for understanding and treating diseases like cancer and neurodegenerative disorders.

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

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

Published on: February 18, 2013

Area of Science:

Biochemistry
Cell Biology
Neuroscience

Background:

S-palmitoylation is a crucial reversible post-translational modification regulating protein localization, stability, and function.
Dysregulated protein palmitoylation is implicated in various human diseases, including cancers and neurodevelopmental/neurodegenerative disorders.
Precise temporal and subcellular control over protein palmitoylation is needed for physiological studies and therapeutic development.

Purpose of the Study:

To develop novel chemogenetic and optogenetic tools for precise manipulation of protein palmitoylation.
To demonstrate the programmability and versatility of these tools for selective depalmitoylation.

Main Methods:

Engineered depalmitoylases were developed for chemogenetic and optogenetic induction.
The system was tested for selective depalmitoylation in specific organelles and of individual protein complexes.
The methodology was applied to investigate neuronal excitability.

Main Results:

Demonstrated programmable and selective depalmitoylation in live cells.
Showcased control over depalmitoylation triggered by cell-signaling events.
Revealed bidirectional tuning of neuronal excitability using distinct depalmitoylases.

Conclusions:

The developed strategy offers a versatile and powerful method for manipulating protein palmitoylation.
This approach provides valuable insights into protein palmitoylation regulation in various physiological contexts.
The tools enable precise control for both basic research and potential therapeutic applications.