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Updated: Jan 30, 2026
13:08
Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
11.4K
Cycling molecular assemblies for Golgi imaging and disruption.
Weiyi Tan1, Qiuxin Zhang1, Zhiyu Liu1
1Department of Chemistry, Brandeis University, Waltham, MA, USA.
Nature Communications
|January 28, 2026
Summary
Researchers developed cycling molecular assemblies (CyMA) for rapid Golgi imaging and cell-selective disruption. This novel approach utilizes self-assembling peptides for precise organelle targeting and functional interference.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Imaging
Background:
- The Golgi apparatus is crucial for protein processing and transport.
- Challenges exist in real-time Golgi imaging and targeted functional disruption.
Purpose of the Study:
- To develop a method for rapid Golgi apparatus imaging.
- To achieve cell-selective interference with Golgi functions.
Main Methods:
- Utilized acetylated amphiphilic thiopeptides as precursors for cycling molecular assemblies (CyMA).
- Exploited intracellular thioesterases and Golgi-resident palmitoyl acyltransferases for peptide modification and self-assembly.
- Engineered CyMA with a biphenyl motif to disrupt Golgi functions.
Main Results:
- Developed CyMA, dynamic nanostructures that enable near-instantaneous Golgi imaging via reversible S-acylation.
- Demonstrated cell-selective disruption of Golgi functions including protein modification, trafficking, and secretion.
- Achieved Golgi disruption leading to cell death by promoting CyMA accumulation.
Conclusions:
- Dynamic supramolecular assembly offers a versatile strategy for Golgi-targeting.
- CyMA enables pleiotropic interference with Golgi functions.
- This approach may be adapted for targeting other organelles using alternative enzyme switches.
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