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Updated: Jan 15, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Mechanical Cues Regulate Cargo Sorting and Export at the Golgi
Greta Serafino1, Stefania Forciniti1, Edoardo Scarpa2,3
1Institute of Nanotechnology, National Research Council (CNR-NANOTEC), Lecce, 73100, Italy.
Substrate stiffness enhances conventional secretion by regulating the Src-FAK-AMPK-GBF1 pathway. This mechanical signaling axis controls protein sorting in the Golgi apparatus, impacting cellular secretion and lysosomal degradation.
Area of Science:
- Cell Biology
- Biochemistry
- Mechanobiology
Background:
- The secretory pathway is crucial for protein and lipid transport.
- Regulation of the secretory pathway by mechanical cues is not well understood.
- Understanding mechanical regulation is vital for cellular processes.
Purpose of the Study:
- To investigate how substrate stiffness influences conventional secretion.
- To elucidate the molecular pathway linking mechanical cues to secretion.
- To identify key regulators of mechano-sensitive secretion.
Main Methods:
- Phosphoproteomic analysis to identify mechano-responsive proteins.
- Investigating the roles of Src, FAK, AMPK, and GBF1 in secretion.
- Studying protein trafficking from the Golgi apparatus.
Main Results:
- Substrate stiffness positively regulates conventional secretion.
- A pathway involving Src, FAK, AMPK, and GBF1 was identified.
- GBF1 phosphorylation state dictates post-Golgi cargo sorting.
- AMP-activated protein kinase (AMPK) regulates GBF1 phosphorylation in response to stiffness.
Conclusions:
- Matrix stiffness positively regulates cellular secretion via the Src-FAK-AMPK-GBF1 axis.
- This pathway impacts protein sorting and lysosomal degradation.
- Findings have implications for cancer, fibrosis, and therapeutic strategies.
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