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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Related Experiment Video

Updated: Feb 11, 2026

The Microscopy-Based Assay to Study and Analyze the Recycling Endosomes using SNARE Trafficking
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The Microscopy-Based Assay to Study and Analyze the Recycling Endosomes using SNARE Trafficking

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SNARE zippering.

Xiaochu Lou1, Yeon-Kyun Shin2

  • 1Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A.

Bioscience Reports
|May 8, 2016
PubMed
Summary

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediate membrane fusion. This review highlights recent progress in understanding SNARE zippering pathways, focusing on the regulatory role of the half-zippered intermediate.

Keywords:
Munc18-1SNAREcoiled coilcomplexinfour-helix bundlenanodiscsynaptotagmin 1

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Related Experiment Videos

Last Updated: Feb 11, 2026

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • SNARE proteins are essential for intracellular membrane fusion.
  • They function by zippering cognate proteins from separate membranes.
  • The stable, post-fusion state is well-characterized, but the zippering pathway remains unclear.

Purpose of the Study:

  • To review recent advancements in understanding the SNARE zippering pathway.
  • To emphasize the significance of the half-zippered intermediate in SNARE complex formation.
  • To explore the regulatory role of auxiliary factors on this intermediate.

Main Methods:

  • Literature review of recent biochemical and biophysical studies.
  • Analysis of data pertaining to SNARE complex assembly dynamics.
  • Focus on intermediate states during SNARE zippering.

Main Results:

  • Recent studies provide new insights into the dynamic pathway of SNARE zippering.
  • The half-zippered intermediate is identified as a crucial regulatory point.
  • Auxiliary factors likely modulate membrane fusion by interacting with this intermediate.

Conclusions:

  • Understanding the SNARE zippering pathway is key to deciphering membrane fusion regulation.
  • The half-zippered intermediate represents a critical regulatory hub.
  • Further research into auxiliary factor interactions with this intermediate is warranted.