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Related Concept Videos

Clathrin Coated Vesicles01:12

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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COP Coated Vesicles00:59

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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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Membrane Domains01:18

Membrane Domains

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
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Vesicular Tubular Clusters01:45

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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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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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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...
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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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A Mimic of the Tumor Microenvironment: A Simple Method for Generating Enriched Cell Populations and Investigating Intercellular Communication
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Cavin 1 function does not follow caveolar morphology.

Tobias Timmel1, Séverine Kunz1, Franziska Seifert2

  • 1Muscle Research Unit, Experimental and Clinical Research Center, Charité Medical Faculty and Max Delbrück Center for Molecular Medicine Berlin, Berlin, Germany; and.

American Journal of Physiology. Cell Physiology
|April 24, 2015
PubMed
Summary
This summary is machine-generated.

Caveolae, vital for cell function, may not perform their roles solely based on structure. Research shows that even with normal caveolae, cellular functions can be impaired, suggesting alternative mechanisms at play.

Keywords:
caveolaecaveolincavin 1/polymerase I and transcript release factorelectron microscopyfluorescein-activated cell sorting

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Area of Science:

  • Cell Biology
  • Membrane Biology
  • Molecular Medicine

Background:

  • Caveolae are small invaginations of the plasma membrane implicated in cellular processes like endocytosis and signal transduction.
  • Caveolin 3 (CAV3) and polymerase I and transcript release factor (PTRF) are crucial for caveolae formation, particularly in muscle cells.
  • The precise function of caveolae and their role in various cellular pathways remain incompletely understood.

Purpose of the Study:

  • To investigate the morphological and functional aspects of caveolae in the context of mutations affecting key structural proteins.
  • To determine if the presence of morphologically normal caveolae is sufficient for proper cellular function.
  • To explore the relationship between caveolae structure and their role in specific cellular processes, such as toxin uptake.

Main Methods:

  • Morphological analysis of caveolae using electron microscopy in myotubes from patients with CAV3 mutations.
  • Functional analysis of caveolae using cholera toxin B uptake assays in PTRF-deficient fibroblasts.
  • Rescue experiments involving PTRF transfection in PTRF-deficient fibroblasts.

Main Results:

  • CAV3-deficient myotubes exhibited normal caveolae shape and number, despite presenting a clinical picture of caveolinopathy.
  • PTRF-deficient fibroblasts, lacking caveolae, showed altered cholera toxin B uptake compared to normal fibroblasts.
  • Restoration of caveolae by PTRF transfection did not normalize cholera toxin B uptake in the deficient fibroblasts.

Conclusions:

  • The physical presence of caveolae does not guarantee their functional integrity.
  • Cellular functions attributed to caveolae may be regulated by mechanisms independent of caveolae structure.
  • Further research is needed to elucidate the precise molecular mechanisms underlying caveolae function.