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Related Concept Videos

Clathrin Coated Vesicles01:12

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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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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Transport Across the Golgi01:26

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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Cargo Loading onto Kinesin Powered Molecular Shuttles
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Galectins CLIC cargo inside.

Pamela Stanley1

  • 1Department of Cell Biology, Albert Einstein College of Medicine, New York, 10461, USA.

Nature Cell Biology
|May 31, 2014
PubMed
Summary
This summary is machine-generated.

Galectin-3 regulates clathrin-independent endocytosis by forming specialized carriers (CLICs). This protein binds cargo and lipids, driving membrane changes essential for cellular uptake.

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Area of Science:

  • Cell biology
  • Molecular mechanisms of endocytosis

Background:

  • Clathrin-independent endocytosis is a key cellular process for removing cell surface proteins.
  • The precise mechanisms governing clathrin-independent endocytosis remain largely unknown.

Purpose of the Study:

  • To investigate the role of Galectin-3 in regulating clathrin-independent endocytosis.
  • To elucidate the molecular mechanisms by which Galectin-3 influences clathrin-independent carrier (CLIC) formation.

Main Methods:

  • Investigated the interaction of Galectin-3 with glycosylated cargo proteins.
  • Examined Galectin-3's interaction with membrane glycosphingolipids.
  • Observed the effects of Galectin-3 on membrane deformation and CLIC biogenesis.

Main Results:

  • Galectin-3 was identified as a regulator of a specific subpopulation of clathrin-independent carriers (CLICs).
  • Galectin-3 directly binds to glycosylated proteins destined for endocytosis.
  • Galectin-3 interacts with membrane glycosphingolipids, inducing membrane curvature and facilitating CLIC formation.

Conclusions:

  • Galectin-3 plays a crucial role in the biogenesis of CLICs, a pathway of clathrin-independent endocytosis.
  • The dual interaction of Galectin-3 with cargo proteins and membrane lipids provides a mechanism for initiating endocytic events.