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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...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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Septins01:19

Septins

Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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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Updated: Jun 26, 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

A role for the syntaxin N-terminus.

Mary Munson1, Nia J Bryant

  • 1Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. mary.munson@umassmed.edu

The Biochemical Journal
|January 23, 2009
PubMed
Summary
This summary is machine-generated.

Sec1p/Munc18 (SM) proteins regulate syntaxins, essential for membrane fusion. Loss of a specific SM-syntaxin interaction impairs neuromuscular transmission in C. elegans, revealing differential regulation of trafficking steps.

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Last Updated: Jun 26, 2026

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
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Area of Science:

  • Molecular biology
  • Cell biology
  • Neuroscience

Background:

  • Intracellular membrane fusion in eukaryotes relies on SNARE proteins, including syntaxins.
  • Syntaxin function is modulated by regulatory proteins like Sec1p/Munc18 (SM) proteins.
  • Understanding SM-syntaxin interactions is crucial for elucidating regulatory mechanisms.

Discussion:

  • The conserved N-terminal peptide binding mode between syntaxins and SM proteins was investigated.
  • Mutations disrupting this interaction in some SM proteins showed no in vivo effects.
  • Johnson et al. demonstrate a significant impact of disrupting the UNC-18 and UNC-64 interaction on C. elegans neuromuscular function.

Key Insights:

  • Loss of the N-terminal binding interaction between UNC-64 (syntaxin) and UNC-18 (SM protein) severely impairs neuromuscular synaptic transmission in C. elegans.
  • This impairment results in an unco-ordinated behavioral phenotype.
  • Disruption of a second, distinct SM-syntaxin binding mode had no detectable effect on synaptic transmission.

Outlook:

  • These findings suggest differential regulation of membrane trafficking steps despite conserved binding modes.
  • Further research is needed to dissect the specific roles of different SM-syntaxin binding modes.
  • This study highlights the complexity of SNARE-mediated membrane fusion regulation.