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Related Concept Videos

Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Regulation of Food Intake01:30

Regulation of Food Intake

Short-term regulation of food intake primarily involves neural signals from the gastrointestinal (GI) tract, blood nutrient levels, and GI tract hormones. Communication between the gut and brain via vagal nerve fibers plays a significant role in evaluating the contents of the gut. Clinical studies have shown that protein ingestion produces a more prolonged response in these nerve fibers compared to an equivalent amount of glucose. Additionally, the activation of stretch receptors caused by GI...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Regulation of Hormone Secretion01:19

Regulation of Hormone Secretion

Regulation of hormone secretion is a finely tuned orchestration driven by various types of stimuli, encompassing neural, humoral, and hormonal signals. Environmental cues instigate neural stimuli, where action potentials traverse nerve fibers to reach their designated targets. An illustrative scenario is the body's response to stress, wherein the sympathetic nervous system releases epinephrine from the adrenal glands, inducing the well-known 'fight or flight' reaction.
Humoral stimuli,...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...

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Related Experiment Video

Updated: May 25, 2026

Ex Vivo Release of Calcitonin Gene-Related Peptide from the Trigeminovascular System in Rodents
08:39

Ex Vivo Release of Calcitonin Gene-Related Peptide from the Trigeminovascular System in Rodents

Published on: May 16, 2022

RIC-7 promotes neuropeptide secretion.

Yingsong Hao1, Zhitao Hu, Derek Sieburth

  • 1Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts, United States of America.

Plos Genetics
|January 26, 2012
PubMed
Summary
This summary is machine-generated.

Researchers discovered RIC-7, a protein crucial for neuropeptide secretion in C. elegans. This protein specifically regulates dense-core vesicle release, offering new insights into neuronal communication.

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Brain Membrane Fractionation: An Ex Vivo Approach to Assess Subsynaptic Protein Localization
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Brain Membrane Fractionation: An Ex Vivo Approach to Assess Subsynaptic Protein Localization

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Related Experiment Videos

Last Updated: May 25, 2026

Ex Vivo Release of Calcitonin Gene-Related Peptide from the Trigeminovascular System in Rodents
08:39

Ex Vivo Release of Calcitonin Gene-Related Peptide from the Trigeminovascular System in Rodents

Published on: May 16, 2022

Brain Membrane Fractionation: An Ex Vivo Approach to Assess Subsynaptic Protein Localization
09:49

Brain Membrane Fractionation: An Ex Vivo Approach to Assess Subsynaptic Protein Localization

Published on: May 12, 2017

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Neurotransmitter and neuropeptide secretion relies on distinct organelles: synaptic vesicles (SVs) and dense-core vesicles (DCVs).
  • Factors differentially regulating SV and DCV secretion remain largely unknown.

Purpose of the Study:

  • To identify novel proteins involved in the differential regulation of SV and DCV secretion.
  • To characterize the function of the novel protein RIC-7 in neuropeptide secretion.

Main Methods:

  • Utilized Caenorhabditis elegans as a model organism.
  • Performed imaging, electrophysiology, and behavioral analyses on ric-7 mutants.
  • Investigated the localization and expression of RIC-7 in neurons.

Main Results:

  • Identified RIC-7 as a novel protein essential for neuropeptide secretion in C. elegans.
  • RIC-7 is expressed in all neurons and localizes to presynaptic terminals.
  • ric-7 mutants exhibit normal acetylcholine release but significantly decreased neuropeptide release.

Conclusions:

  • RIC-7 plays a critical role in promoting dense-core vesicle (DCV)-mediated secretion.
  • This finding sheds light on the specific mechanisms regulating neuropeptide release distinct from neurotransmitter release.