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Related Concept Videos

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Electron Transport Chain: Complex III and IV01:43

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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Complexes with Interchangeable Parts01:57

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The Erv41-Erv46 complex serves as a retrograde receptor to retrieve misfolded secretory proteins that have escaped from the ER.

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Related Experiment Video

Updated: Dec 31, 2025

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
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Twenty-five years after coat protein complex II.

Charles Barlowe1

  • 1Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.

Molecular Biology of the Cell
|December 31, 2019
PubMed
Summary

Researchers discovered the coat protein complex II (COPII) in 1994 through collaborative efforts. This perspective reviews the discovery and ongoing research into COPII vesicle budding mechanisms.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Vesicular transport is crucial for eukaryotic cell function.
  • Coat proteins mediate the formation of transport vesicles.
  • The discovery of coat protein complex II (COPII) was a significant advancement.

Purpose of the Study:

  • To recount the historical events leading to the discovery of COPII.
  • To review the progress in understanding COPII vesicle budding mechanisms.
  • To provide a perspective on the significance of COPII in cell biology.

Main Methods:

  • Historical review of research publications.
  • Analysis of collaborative research networks.
  • Synthesis of experimental findings on COPII function.

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Main Results:

  • The discovery of COPII in 1994 resulted from a convergence of ideas and collaborative research.
  • Significant progress has been made in elucidating the molecular components and functions of COPII.
  • Understanding COPII budding mechanisms has advanced considerably.

Conclusions:

  • The discovery of COPII revolutionized the understanding of intracellular transport.
  • Continued research on COPII is essential for unraveling the complexities of vesicle formation and trafficking.
  • COPII plays a vital role in maintaining cellular homeostasis and function.