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Related Concept Videos

Golgi Apparatus01:09

Golgi Apparatus

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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
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Golgi Apparatus01:49

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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
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Transport Across the Golgi01:26

Transport Across the Golgi

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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Overview of Protein Sorting and Transport01:45

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Nuclear Protein Sorting01:34

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Related Experiment Video

Updated: Jan 15, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

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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.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|October 15, 2025
PubMed
Summary
This summary is machine-generated.

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.

Keywords:
GBF1golgi sortingmechanosensingstiffnesstrafficking

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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.