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Decoding transcriptomic signatures of Cysteine String Protein alpha-mediated synapse maintenance.

Na Wang1, Biqing Zhu2, Mary Alice Allnutt1,3

  • 1Departments of Neurology and Neuroscience, Yale University, New Haven, CT, USA.

Biorxiv : the Preprint Server for Biology
|October 24, 2023
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Summary

Synapse maintenance is crucial for brain function and neurodegeneration. Loss of cysteine string protein alpha (CSPα) impairs synapse maintenance, leading to synaptic repression and increased autophagy.

Keywords:
CSPαNeurexin1-Neuroligin 1autophagosomechaperonesynapse loss

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Synapse maintenance is vital for functional neural circuits, and its decline is a hallmark of neurodegenerative diseases.
  • Cysteine string protein alpha (CSPα), encoded by the Dnajc5 gene, is a synaptic vesicle chaperone essential for synapse maintenance and implicated in neurodegeneration.

Approach:

  • Single nucleus transcriptomics was employed on the cortex of young CSPα knockout (KO) mice and littermate controls.
  • Differential gene expression and gene ontology analyses identified unique transcriptional signatures in neurons and glial cells of CSPα KO brains.
  • Electron microscopy visualized synaptic alterations and autophagosomes, while cell-cell interaction imputation revealed changes in neuron-glia communication.

Key Points:

  • Neurons in CSPα KO brains exhibited repressed synaptic pathways and upregulated autophagy-related genes.
  • Alterations in synapses, particularly inhibitory ones, and autophagosomes were confirmed via electron microscopy.
  • Neuron-glia interactions were increased in CSPα KO mice, mediated by synaptogenic adhesion molecules like Neurexin1-Neuroligin 1.

Conclusions:

  • CSPα deficiency leads to distinct cellular and molecular transcriptional changes in the cortex.
  • The study provides novel insights into the mechanisms of synapse maintenance and neurodegeneration.
  • Enhanced neuron-glia communication may represent a compensatory mechanism for impaired synapse maintenance.