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Related Concept Videos

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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.
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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Related Experiment Video

Updated: May 7, 2026

Osmotic Avoidance in Caenorhabditis elegans: Synaptic Function of Two Genes, Orthologues of Human NRXN1 and NLGN1, as Candidates for Autism
11:20

Osmotic Avoidance in Caenorhabditis elegans: Synaptic Function of Two Genes, Orthologues of Human NRXN1 and NLGN1, as Candidates for Autism

Published on: December 11, 2009

Neurexins.

Carsten Reissner, Fabian Runkel, Markus Missler

    Genome Biology
    |October 3, 2013
    PubMed
    Summary
    This summary is machine-generated.

    Neurexins are cell adhesion proteins crucial for synapse function and neurotransmission. Genetic variations in neurexin genes are linked to neurological disorders like autism and schizophrenia.

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    Related Experiment Videos

    Last Updated: May 7, 2026

    Osmotic Avoidance in Caenorhabditis elegans: Synaptic Function of Two Genes, Orthologues of Human NRXN1 and NLGN1, as Candidates for Autism
    11:20

    Osmotic Avoidance in Caenorhabditis elegans: Synaptic Function of Two Genes, Orthologues of Human NRXN1 and NLGN1, as Candidates for Autism

    Published on: December 11, 2009

    Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors
    07:51

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    Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
    04:47

    Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

    Published on: May 22, 2020

    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Genetics

    Background:

    • Neurexins are a family of cell adhesion proteins with homologs across species.
    • In mammals, neurexin genes produce alpha- and beta-neurexins, with extensive alternative splicing creating numerous variants.
    • Neurexins are primarily located at the presynaptic terminal, playing key roles in neuronal function.

    Purpose of the Study:

    • To summarize the structural diversity and functional significance of neurexins.
    • To highlight the role of neurexins in forming trans-synaptic complexes.
    • To discuss the implications of neurexin gene mutations in neurological diseases.

    Main Methods:

    • Review of existing literature on neurexin structure and function.
    • Analysis of alternative splicing mechanisms in neurexin gene expression.
    • Examination of studies linking neurexin variations to human diseases.

    Main Results:

    • Neurexin proteins exhibit significant structural diversity due to alternative splicing.
    • Neurexins mediate synaptic function through interactions with postsynaptic partners like neuroligins.
    • Mutations and copy-number variations in neurexin genes are associated with autism and schizophrenia.

    Conclusions:

    • Neurexins are essential for proper synaptic formation and neurotransmission.
    • The variability of neurexins contributes to the complexity of synaptic function.
    • Dysregulation of neurexin pathways may underlie the pathogenesis of certain neurodevelopmental and psychiatric disorders.