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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

11.1K
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.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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SNARE disassembly requires Sec18/NSF side loading.

Yousuf A Khan1,2,3,4, K Ian White5,6,7,8,9, Richard A Pfuetzner5,6,7,8,9

  • 1Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA. yousuf@stanford.edu.

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|July 3, 2025
PubMed
Summary
This summary is machine-generated.

Sec18/NSF (N-ethylmaleimide-sensitive factor) and Sec17/α-SNAP disassemble SNARE protein bundles after cell membrane fusion. New cryo-EM structures reveal Sec18/NSF threads SNAREs through its ATPase rings, enabling side loading and unloading.

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Area of Science:

  • Cell biology
  • Molecular machinery
  • Membrane fusion

Background:

  • SNARE proteins mediate membrane fusion by forming four-helix bundles.
  • Sec18/NSF and Sec17/α-SNAP disassemble these bundles for recycling.
  • Previous models faced topological challenges with SNARE transmembrane domains.

Purpose of the Study:

  • To elucidate the mechanism of SNARE complex disassembly by Sec18/NSF.
  • To resolve the topological constraints of SNARE threading through Sec18/NSF.
  • To visualize Sec18/NSF and Sec17/α-SNAP interactions with SNAREs.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of yeast SNARE complexes.
  • Mass spectrometry to identify protein interactions.
  • Structural analysis under non-hydrolyzing and hydrolyzing conditions.

Main Results:

  • Cryo-EM structures show SNARE Sso1 threaded through Sec18/NSF's D1 and D2 ATPase rings.
  • The N-terminal Habc domain of Sso1 interacts with the D2 ring and remains folded.
  • Structures under hydrolyzing conditions reveal substrate release and ring opening.
  • Sec18/NSF utilizes side loading and unloading for topologically constrained SNAREs.

Conclusions:

  • Sec18/NSF disassembles SNAREs via a side-loading mechanism.
  • The ATPase rings of Sec18/NSF open to accommodate and release SNARE substrates.
  • This mechanism overcomes topological constraints posed by SNARE domains.