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Overview of Secretory Vesicles

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...

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...

ER Retrieval Pathway

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

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...

Directing Proteins to the Rough Endoplasmic Reticulum

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...

Clathrin Coated Vesicles

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...

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Related Experiment Video

Updated: Jun 6, 2026

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Published on: October 23, 2016

Charting the secretory pathway in a simple eukaryote.

Randy Schekman¹

¹Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California-Berkeley, Berkeley, CA 94720, USA. schekman@berkeley.edu

Molecular Biology of the Cell

|November 17, 2010

Summary

This summary is machine-generated.

This study elucidates the conserved protein transport pathway in eukaryotic cells using yeast secretion mutants. Key findings reveal essential Sec proteins involved in endoplasmic reticulum translocation and vesicle budding.

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

George Palade's foundational work established the ultrastructural basis for understanding protein secretion and membrane assembly in eukaryotic cells.
The research builds upon this legacy by investigating the molecular mechanisms of protein transport pathways.
The study focuses on dissecting these pathways using complementary genetic and biochemical approaches.

Discussion:

The research utilized Saccharomyces cerevisiae (yeast) secretion mutants to identify and characterize essential genes (SEC genes) involved in the secretory pathway.
Cytological analysis of single and double mutants, alongside molecular cloning, confirmed the conserved nature of the yeast secretory pathway across eukaryotes.
A key focus was on understanding the roles of specific Sec proteins in protein translocation and vesicle formation.

Key Insights:

Established that yeast employs a secretory pathway conserved across all eukaryotic organisms.
Identified Sec61 as the polypeptide translocation channel in the endoplasmic reticulum membrane.
Characterized the COPII protein complex responsible for capturing cargo proteins into transport vesicles budding from the ER.

Outlook:

Further biochemical characterization of Sec proteins and their interactions.
Exploring the regulation of protein transport in response to cellular needs.
Investigating potential therapeutic targets within the protein secretion pathway for diseases.