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Related Concept Videos

Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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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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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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Fusion of Secretory Vesicles with the Plasma Membrane01:26

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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.
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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COP Coated Vesicles00:59

COP Coated Vesicles

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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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Related Experiment Video

Updated: May 6, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Multiple neuropeptides derived from a common precursor are differentially packaged and transported.

J M Fisher1, W Sossin, R Newcomb

  • 1Department of Biological Sciences, Stanford University, California 94305.

Cell
|September 9, 1988
PubMed
Summary

The egg-laying hormone (ELH) prohormone yields peptides that control egg-laying behavior in Aplysia. These peptides are sorted into distinct vesicles through a process involving early cleavage and Golgi sorting, regulating their levels and localization.

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Area of Science:

  • Neurobiology
  • Molecular Biology
  • Cell Biology

Background:

  • The egg-laying hormone (ELH) prohormone in Aplysia is a precursor to multiple bioactive peptides.
  • These peptides are known to regulate complex behaviors such as egg-laying.

Purpose of the Study:

  • To investigate the intracellular processing and sorting mechanisms of peptides derived from the ELH prohormone.
  • To understand how these mechanisms influence the localization and steady-state levels of individual peptides within neurons.

Main Methods:

  • Quantitative immunocytochemistry was employed to visualize and quantify peptide distribution.
  • Experiments focused on proteolytic cleavage and trans-Golgi sorting pathways.

Main Results:

  • ELH prohormone processing generates at least nine distinct peptides.
  • Peptides are sorted into specific vesicle classes, suggesting regulated intracellular trafficking.
  • Amino-terminal peptides (e.g., bag cell peptides) have lower steady-state levels than carboxy-terminal peptides (e.g., ELH).

Conclusions:

  • Intracellular packaging and routing mechanisms play a critical role in determining the differential localization and abundance of peptides derived from a single prohormone.
  • These processes are essential for regulating neuronal function and behavior in Aplysia.