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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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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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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Protein Complex Assembly02:41

Protein Complex Assembly

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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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Protein Translocation Machinery on the ER Membrane01:28

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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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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Interspecies complementation identifies a pathway to assemble SNAREs.

Leonardo A Parra-Rivas1, Mark T Palfreyman1, Thien N Vu1

  • 1Howard Hughes Medical Institute, School of Biological Sciences, University of Utah, Salt Lake City, UT 84112-0840, USA.

Iscience
|June 27, 2022
PubMed
Summary
This summary is machine-generated.

Synaptic membrane fusion relies on Unc18 and SNARE proteins. Key interactions between these proteins, conserved across species, are essential for synaptic transmission and membrane fusion.

Keywords:
Biological sciencesCell biologyFunctional aspects of cell biologyMolecular biologyMolecular neuroscienceNeuroscience

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Unc18 and SNARE proteins are crucial for synaptic membrane fusion.
  • Understanding their functional interactions is key to synaptic transmission.

Purpose of the Study:

  • To investigate the functional interactions within the Unc18-SNARE machinery.
  • To explore the evolutionary conservation of these interactions using interspecies complementation.

Main Methods:

  • Utilized an "interspecies complementation" approach in *Caenorhabditis elegans*.
  • Substituted worm Unc18 and SNARE proteins with yeast homologs.
  • Analyzed synaptic transmission in chimeric worm-yeast systems.

Main Results:

  • Individual yeast protein substitutions failed to rescue synaptic fusion.
  • Synaptic transmission was restored in chimeras requiring specific Habc-Unc18 and Unc18-SNARE motif interfaces.
  • A constitutively open Unc18 form bypassed the Habc-Unc18 interface requirement.

Conclusions:

  • The Habc domain of syntaxin is necessary for Unc18 to adopt an open conformation, which then guides SNARE complex assembly.
  • Synaptic transmission machinery in *C. elegans* can be functionally replaced by yeast proteins, indicating deep evolutionary conservation.