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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.
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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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Multi-pass Transmembrane Proteins and β-barrels01:09

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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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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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Synaptobrevin Transmembrane Domain Dimerization Studied by Multiscale Molecular Dynamics Simulations.

Jing Han1, Kristyna Pluhackova1, Tsjerk A Wassenaar1

  • 1Computational Biology, Department of Biology, Friedrich-Alexander Universität Erlangen-Nürnberg, Erlangen, Germany.

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|August 20, 2015
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Summary

Synaptic vesicle fusion involves SNARE proteins. This study reveals how synaptobrevin-2 transmembrane domains dimerize, explaining fusion activity and oligomerization through specific TM sequence interactions.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Neuroscience

Background:

  • Synaptic vesicle fusion is critical for neurotransmission, mediated by the SNARE complex.
  • The transmembrane (TM) domains of SNARE proteins, including synaptobrevin-2 (sybII), are involved in membrane fusion.
  • The precise role of sybII TM domain dimerization in fusion remains unclear.

Purpose of the Study:

  • To investigate the homodimerization of the sybII TM domain using computational simulations.
  • To explore the impact of specific TM mutations on sybII dimerization and its relationship to fusogenic activity.

Main Methods:

  • Coarse-grained and atomistic molecular simulations were employed.
  • Modeling focused on wild-type sybII TM domain and selected mutants.
  • Analysis of dimerization interfaces and association kinetics.

Main Results:

  • Wild-type sybII TM domain forms a stable, right-handed dimer with specific interfaces, explaining higher-order oligomerization.
  • Two novel binding interfaces were identified for wild-type sybII.
  • A fusion-inactive poly-Leu mutant exhibited only one dimerization interface and reduced association kinetics compared to wild-type.

Conclusions:

  • TM sequence specificity dictates sybII aggregation and dimerization in membranes.
  • Differences in dimerization interfaces and kinetics between wild-type and mutant sybII correlate with fusogenic activity.
  • This study provides molecular insights into SNARE protein function during synaptic vesicle fusion.