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Related Concept Videos

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.
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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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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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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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Energy to Drive Translocation01:37

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
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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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Related Experiment Video

Updated: Oct 7, 2025

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
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Exploring the Two Coupled Conformational Changes That Activate the Munc18-1/Syntaxin-1 Complex.

Jihong Gong1, Xianping Wang2, Chaoyang Cui1

  • 1Key Laboratory of Cognitive Science, Laboratory of Membrane Ion Channels and Medicine, College of Biomedical Engineering, South-Central University for Nationalities, Wuhan, China.

Frontiers in Molecular Neuroscience
|January 10, 2022
PubMed
Summary
This summary is machine-generated.

Munc13-1's role in SNARE complex assembly is clarified. Opening the syntaxin-1 linker region initiates assembly, allowing Munc18-1 domain 3a extension to template further interactions for calcium-dependent synaptic vesicle exocytosis.

Keywords:
Munc13-1Munc18-1SNARE complexexocytosissynapsesyntaxin-1

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Calcium-dependent synaptic vesicle exocytosis relies on SNARE complex formation.
  • The transition to the SNARE complex is catalyzed by the Munc13-1 MUN domain.
  • This transition involves syntaxin-1 linker opening and Munc18-1 domain 3a extension, but their order is unclear.

Purpose of the Study:

  • To elucidate the relationship and action order of conformational changes in SNARE complex assembly.
  • To investigate the roles of syntaxin-1 linker opening and Munc18-1 domain 3a extension.

Main Methods:

  • Experimental data were analyzed to determine the functional significance of specific protein conformations.
  • The study focused on the interplay between Munc13-1, Munc18-1, and syntaxin-1.

Main Results:

  • An open syntaxin-1 linker conformation can proceed without the MUN NF sequence.
  • An extended Munc18-1 domain 3a can substitute for the syntaxin-1 RI sequence.
  • These findings clarify the sequential events in SNARE complex initiation.

Conclusions:

  • Munc13-1-mediated opening of the syntaxin-1 linker is a crucial initial step for SNARE complex assembly.
  • Munc18-1 domain 3a extension then serves as a template for synaptobrevin-2 and syntaxin-1 association.
  • This provides a refined model for the regulation of synaptic vesicle exocytosis.