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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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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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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.
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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
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Updated: Jun 27, 2025

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
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Sortase-Modified Cholera Toxoids Show Specific Golgi Localization.

Darren C Machin1, Daniel J Williamson1, Peter Fisher2

  • 1School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

Toxins
|April 26, 2024
PubMed
Summary
This summary is machine-generated.

Researchers modified cholera toxoid for cell biology. The B5 pentamer variant specifically localized to the Golgi, suggesting new live-cell imaging applications beyond neuronal tracing.

Keywords:
Golgi bodycellular imagingcholera toxinprotein labelingsortase

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Molecular Biology

Background:

  • Cholera toxoid is a recognized tool for cellular tracing in neuroscience and cell biology.
  • Existing applications include neuronal tracing and labeling of lipid rafts in fixed cells.

Purpose of the Study:

  • To generate site-specific N-terminally modified variants of cholera toxoid using a sortase labeling approach.
  • To investigate the cellular localization of these modified toxoid variants (A2-B5 heterohexamer and B5 pentamer) in mammalian cells.

Main Methods:

  • Employing a sortase labeling strategy to create N-terminally modified cholera toxoid variants.
  • Utilizing endocytosis assays in GM1-positive mammalian cells.
  • Confocal microscopy to determine subcellular localization of the toxoid variants.

Main Results:

  • Both heterohexameric and pentameric cholera toxoid variants were endocytosed by GM1-positive cells.
  • The heterohexameric toxoid primarily localized to the endoplasmic reticulum (ER).
  • The B5 pentamer exhibited unexpected and specific localization within the medial/trans-Golgi apparatus.

Conclusions:

  • Site-specific labeling of cholera toxoid variants enables distinct subcellular localization studies.
  • The B5 pentamer's Golgi localization opens new avenues for its use in live-cell imaging.
  • This work expands the utility of cholera toxoid beyond fixed-cell applications and neuronal tracing.