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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...

Clathrin Coated Vesicles

Clathrin Coated Vesicles

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...

COP Coated Vesicles

COP Coated Vesicles

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 different...

Feedback Regulation of Calcium Concentration

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

Vesicular Tubular Clusters

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...

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Related Experiment Video

Updated: Jun 22, 2026

Measuring Fast Calcium Fluxes in Cardiomyocytes

Measuring Fast Calcium Fluxes in Cardiomyocytes

Published on: November 29, 2011

Cavin fever: regulating caveolae.

Nature Cell Biology

|July 2, 2009

Summary

The study identifies SDPR as a novel regulator of caveolae biogenesis. Overexpression of SDPR influences caveolae size and promotes the formation of tubules involved in Shiga toxin transport.

Area of Science:

Cell Biology
Membrane Biology
Biochemistry

Background:

Caveolae are flask-shaped invaginations of the plasma membrane involved in cellular processes.
The biogenesis and regulation of caveolae are not fully understood.
Shiga toxin utilizes caveolae for cellular entry.

Discussion:

SDPR (Secretion Downstream Positive Regulator) emerges as a key player in caveolae formation.
SDPR overexpression leads to larger caveolae and the development of caveolae-derived tubules.
These tubules are implicated in the transport of Shiga toxin within cells.

Key Insights:

SDPR acts as a novel regulator of caveolae biogenesis.
The protein influences the size and morphology of caveolae.

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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca²⁺ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

Related Experiment Videos

Last Updated: Jun 22, 2026

Measuring Fast Calcium Fluxes in Cardiomyocytes

Measuring Fast Calcium Fluxes in Cardiomyocytes

Published on: November 29, 2011

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca²⁺ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

SDPR is potentially involved in membrane curvature induction during caveolae formation.

Outlook:

Further research into SDPR's mechanism could reveal new therapeutic targets for toxin-mediated diseases.
Investigating SDPR's role in membrane curvature may elucidate fundamental principles of organelle biogenesis.
Understanding SDPR's function could impact strategies for modulating cellular uptake pathways.