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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Related Experiment Video

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In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
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Syntaxin1A lateral diffusion reveals transient and local SNARE interactions.

Claire Ribrault1, Jürgen Reingruber, Maja Petković

  • 1Biologie Cellulaire de la Synapse, Institut de Biologie de l'Ecole Normale Supérieure, Institut National de la Santé et de la Recherche Médicale Unité 1024-CNRS 8197, F-75005 Paris, France.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|December 2, 2011
PubMed
Summary

Presynaptic membrane protein syntaxin1A exhibits diffusive motion compatible with vesicle docking. Its mobility changes with exocytotic complex formation, explained by a reaction-diffusion model.

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Published on: August 24, 2016

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Last Updated: May 27, 2026

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
06:45

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal

Published on: January 14, 2018

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biophysics

Background:

  • Vesicle docking at the synapse requires stable protein interactions.
  • Membrane proteins normally exhibit diffusive motion.
  • The compatibility of protein diffusion with vesicle docking and membrane remodeling is unclear.

Purpose of the Study:

  • To investigate the motion of syntaxin1A, a presynaptic membrane protein crucial for exocytosis.
  • To understand how syntaxin1A's mobility relates to vesicle docking and plasma membrane dynamics.

Main Methods:

  • Studied syntaxin1A motion at population and single-molecule levels.
  • Utilized primary cultures of rat spinal cord neurons.
  • Developed a reaction-diffusion model.

Main Results:

  • Syntaxin1A rapidly exchanges between synaptic and extrasynaptic membrane regions.
  • Changes in syntaxin1A mobility correlate with exocytotic complex formation.
  • A reaction-diffusion model successfully reconciles observed diffusive properties.

Conclusions:

  • Syntaxin1A's diffusive motion is compatible with synaptic vesicle docking.
  • Interactions forming the exocytotic complex transiently stabilize syntaxin1A at the synapse.
  • The study describes syntaxin1A's diffusive behavior and interaction kinetics.