ArticleFrontiers in neuroscience2017
CSPα, a Molecular Co-chaperone Essential for Short and Long-Term Synaptic Maintenance.
Article in Frontiers in neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Synaptic vesicles that store monoamines and glutamate differ in protein composition.Science advances · 2026Article
- DNAJC5 facilitates the proliferation and migration of lung adenocarcinoma cells by augmenting EGFR trafficking.Communications biology · 2025Article
- α-Synuclein pathology as a target in neurodegenerative diseases.Nature reviews. Neurology · 2025Review
- Cysteine string protein α and a link between rare and common neurodegenerative dementias.NPJ dementia · 2025Review
- Regulation of proteostasis by sleep through autophagy inLife science alliance · 2024Article
- Cysteine string protein alpha accumulates with early pre-synaptic dysfunction in Alzheimer's disease.Brain communications · 2022Article
- Cysteine String Protein Controls Two Routes of Export for Misfolded Huntingtin.Frontiers in neuroscience · 2021Article
- AeLife · 2019Article
- LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.Molecular systems biology · 2018Article
- Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cysteine string protein α (CSPα) is a vesicle protein located in the presynaptic terminal of most synapses. CSPα is an essential molecular co-chaperone that facilitates the correct folding of proteins and the assembly of the exocytic machinery. The absence of this protein leads to altered neurotransmitter release and neurodegeneration in multiple model systems, from flies to mice. In humans, CSPα mutations are associated with the development of neuronal ceroid lipofuscinosis (NCL), a neurodegenerative disease characterized by intracellular accumulation of lysosomal material. Here, we review the physiological role of CSPα and the pathology resulting from the homozygous deletion of the gene or its mutations. In addition, we investigate whether long-term moderate reduction of the protein produces motor dysfunction. We found that 1-year-old CSPα heterozygous mice display a reduced ability to sustain motor unit recruitment during repetitive stimulation, which indicates that physiological levels of CSPα are required for normal neuromuscular responses in mice and, likely, in humans.
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