ArticleThe Biochemical journal2002
Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 83 citations in OpenAlex.
- Cysteine string protein α and a link between rare and common neurodegenerative dementias.NPJ dementia · 2025Review
- Pseudophosphorylation of single residues of the J-domain of DNAJA2 regulates the holding/folding balance of the Hsc70 system.Protein science : a publication of the Protein Society · 2024Article
- Proximity labelling reveals effects of disease-causing mutation on the DNAJC5/cysteine string protein α interactome.The Biochemical journal · 2024Article
- Abnormal triaging of misfolded proteins by adult neuronal ceroid lipofuscinosis-associated DNAJC5/CSPα mutants causes lipofuscin accumulation.Autophagy · 2023Article
- Phosphorylation of cysteine string protein-α up-regulates the frequency of cholinergic wavesVisual neuroscience · 2022Article
- CSPα in neurodegenerative diseases.Frontiers in aging neuroscience · 2022Review
- Safeguarding Lysosomal Homeostasis by DNAJC5/CSPα-Mediated Unconventional Protein Secretion and Endosomal Microautophagy.Frontiers in cell and developmental biology · 2022Review
- Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021Review
- Review
- Autosomal dominant neuronal ceroid lipofuscinosis: Clinical features and molecular basis.Clinical genetics · 2021Review
- Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy.Biochemistry · 2020Review
- The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones.International journal of molecular sciences · 2019Review
- GPCR regulation of secretion.Pharmacology & therapeutics · 2018Review
- DNAJ Proteins in neurodegeneration: essential and protective factors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- The Role of Cysteine String Protein α Phosphorylation at Serine 10 and 34 by Protein Kinase Cγ for Presynaptic Maintenance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo.Scientific reports · 2017Article
- The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Frontiers in neuroscience · 2017Review
- Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch.Structure (London, England : 1993) · 2016Article
- Clinically early-stage CSPα mutation carrier exhibits remarkable terminal stage neuronal pathology with minimal evidence of synaptic loss.Acta neuropathologica communications · 2015Article
- Cysteine string protein (CSP) and its role in preventing neurodegeneration.Seminars in cell & developmental biology · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The secretory vesicle cysteine string proteins (CSPs) are members of the DnaJ family of chaperones, and function at late stages of Ca2+-regulated exocytosis by an unknown mechanism. To determine novel binding partners of CSPs, we employed a pull-down strategy from purified rat brain membrane or cytosolic proteins using recombinant hexahistidine-tagged (His(6)-)CSP. Western blotting of the CSP-binding proteins identified synaptotagmin I to be a putative binding partner. Furthermore, pull-down assays using cAMP-dependent protein kinase (PKA)-phosphorylated CSP recovered significantly less synaptotagmin. Complexes containing CSP and synaptotagmin were immunoprecipitated from rat brain membranes, further suggesting that these proteins interact in vivo. Binding assays in vitro using recombinant proteins confirmed a direct interaction between the two proteins and demonstrated that the PKA-phosphorylated form of CSP binds synaptotagmin with approximately an order of magnitude lower affinity than the non-phosphorylated form. Genetic studies have implicated each of these proteins in the Ca2+-dependency of exocytosis and, since CSP does not bind Ca2+, this novel interaction might explain the Ca2+-dependent actions of CSP.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.