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Related Concept Videos

Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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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.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Insulin Secretory Vesicles01:05

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Insulin secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
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Exocrine Glands: Methods of Secretion01:08

Exocrine Glands: Methods of Secretion

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Exocrine glands are those that release their secretions through ducts. Based on their mode of secretion, they can be classified into merocrine, apocrine, and holocrine.
Merocrine Secretion
Merocrine secretion is the most common type of exocrine secretion. The secretions are enclosed in vesicles and moved to the cell's apical surface, where the contents are released by exocytosis. For example, mucous, a watery secretion rich in the glycoprotein mucin, is a merocrine secretion. The eccrine...
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Pancreatic Juice and Secretion01:26

Pancreatic Juice and Secretion

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Pancreatic juice is a clear fluid produced by the pancreas, containing water, salts, sodium bicarbonate, and enzymes vital for digestion in the small intestine. It helps break down large molecules, facilitating nutrient absorption.
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Related Experiment Video

Updated: Feb 16, 2026

Assessing the Secretory Capacity of Pancreatic Acinar Cells
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Assessing the Secretory Capacity of Pancreatic Acinar Cells

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Multiple Structures Disclose the Secretins' Secrets.

Alain Filloux1, Romé Voulhoux2

  • 1Imperial College London, Department of Life Sciences, MRC-CMBI, London, United Kingdom a.filloux@imperial.ac.uk.

Journal of Bacteriology
|December 22, 2017
PubMed
Summary

Bacterial secretins, essential outer membrane proteins, form ring-shaped structures crucial for protein secretion. Recent cryo-electron microscopy advancements have revealed their atomic organization within type II and type III secretion systems.

Keywords:
GspDT2SSsecretin

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacterial secretins are outer membrane proteins vital for cellular secretion.
  • They form a core component of type II and type III secretion systems (T2SS and T3SS).
  • Secretins assemble into large, ring-shaped homo-oligomers.

Purpose of the Study:

  • To elucidate the precise atomic organization of bacterial secretins.
  • To leverage recent advancements in cryo-electron microscopy for structural determination.

Main Methods:

  • Utilized cryo-electron microscopy (cryo-EM) imaging techniques.
  • Applied advanced image processing to decipher protein structures.

Main Results:

  • The atomic organization of giant, ring-shaped secretin homo-oligomers was recently deciphered.
  • High-resolution structural data was obtained for these complex outer membrane proteins.

Conclusions:

  • Cryo-EM has enabled unprecedented insights into the structure of bacterial secretins.
  • Understanding secretin structure is key to comprehending protein secretion pathways in bacteria.