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Updated: May 10, 2026
13:08
Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Stapled Golgi cisternae remain in place as cargo passes through the stack.
Gregory Lavieu1, Hong Zheng, James E Rothman
1Department of Cell Biology , Yale University School of Medicine , New Haven , United States.
Elife
|June 12, 2013
Summary
Researchers developed membrane staples that form plaques in the Golgi. These staples remain static, unlike soluble aggregates, revealing a new Golgi transport mechanism called Rim Progression.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The secretory pathway ensures proper protein folding and transport.
- Golgi apparatus is crucial for protein modification and sorting.
- Understanding protein dynamics within the Golgi is key to cell function.
Purpose of the Study:
- To investigate the behavior of membrane-tethered protein aggregates within the Golgi apparatus.
- To explore the mechanisms governing protein trafficking and localization in the Golgi.
- To identify novel pathways involved in Golgi dynamics.
Main Methods:
- Design and synthesis of membrane-tethered FM domain aggregates ('staples').
- Utilizing a disaggregating drug to control protein aggregation and transit.
- Live-cell imaging and electron microscopy to observe staple localization and movement within the Golgi.
Main Results:
- Membrane staples, once formed, remain localized to the cis-Golgi face.
- Soluble FM-aggregates exhibit different trafficking behavior, moving through the Golgi.
- Staples reside in static Golgi cisternae, while soluble aggregates are found in mobile Golgi rims.
Conclusions:
- Membrane staples and soluble aggregates have distinct intracellular fates.
- The Golgi cisternae are relatively static concerning membrane staple localization.
- A novel Golgi transport mechanism, 'Rim Progression', is proposed for mobile Golgi rims.
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