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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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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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The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
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Related Experiment Video

Updated: Apr 21, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Published on: October 20, 2014

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Regulating dynamin dynamics during endocytosis.

Anna C Sundborger1, Jenny E Hinshaw1

  • 1Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases NIH, Bethesda, MD, 20892 USA.

F1000Prime Reports
|November 7, 2014
PubMed
Summary

Dynamin protein is crucial for cell membrane scission during endocytosis. Its interactions with other proteins facilitate dynamin

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Dynamin, a large GTPase, is essential for plasma membrane fission during clathrin-mediated endocytosis.
  • Dynamin polymerizes on budding membrane necks and undergoes GTP-dependent conformational changes for membrane fission.
  • The precise in vivo mechanism of dynamin-mediated fission remains incompletely understood.

Purpose of the Study:

  • To elucidate the in vivo mechanisms of dynamin-mediated plasma membrane fission.
  • To understand the role of dynamin's C-terminal proline-rich domain (PRD) in protein interactions.
  • To investigate how dynamin-binding partners regulate dynamin's function in endocytosis.

Main Methods:

  • Investigated protein-protein interactions mediated by dynamin's PRD.

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

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  • Focused on the roles of intersectin, amphiphysin, and endophilin in dynamin function.
  • Analyzed the regulation of dynamin assembly and GTPase activity at clathrin-coated pits.
  • Main Results:

    • Dynamin interactions are mediated by its PRD binding to SH3 domains.
    • Intersectin, amphiphysin, and endophilin are key dynamin-binding partners in endocytosis.
    • These partners regulate dynamin recruitment, assembly, and GTPase activity for efficient membrane fission.

    Conclusions:

    • Dynamin-binding partners play critical, sequential roles in dynamin-mediated membrane fission.
    • These interactions are vital for the proper functioning of clathrin-mediated endocytosis.
    • Understanding these mechanisms provides insight into cellular membrane dynamics.