ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000
Cbln3, a novel member of the precerebellin family that binds specifically to Cbln1.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Who cites it
39 citing papers in PubMed, 84 citations in OpenAlex.
- Glutamate Delta 1 Receptor in Synapses, Circuits, and Disease.The European journal of neuroscience · 2026Review
- Integrative multi-omics analysis of druggable genes for therapeutic target identification in polycystic ovary syndrome.Journal of ovarian research · 2025Article
- Promoter demethylation of cerebellin 2 by ten-eleven translocation 3 contributes to peripheral sensitization in trigeminal neuropathic pain of mice.The journal of headache and pain · 2025Article
- Biomarker discovery in progressive supranuclear palsy from human cerebrospinal fluid.Clinical proteomics · 2024Article
- Accurately deciphering spatial domains for spatially resolved transcriptomics with stCluster.Briefings in bioinformatics · 2024Article
- ZEB1 Is Regulated by K811 Acetylation to Promote Stability, NuRD Complex Interactions, EMT, and NSCLC Metastasis.Molecular cancer research : MCR · 2023Article
- Cbln1 Directs Axon Targeting by Corticospinal Neurons Specifically toward Thoraco-Lumbar Spinal Cord.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Extracellular matrix and synapse formation.Bioscience reports · 2023Article
- Spatially aware dimension reduction for spatial transcriptomics.Nature communications · 2022Article
- Transcriptional atlas analysis from multiple tissues reveals the expression specificity patterns in beef cattle.BMC biology · 2022Article
- Functional and Molecular Immune Response of Rainbow Trout (International journal of molecular sciences · 2022Article
- Neurexins and their ligands at inhibitory synapses.Frontiers in synaptic neuroscience · 2022Review
- Molecular self-avoidance in synaptic neurexin complexes.Science advances · 2021Article
- Ultrastructural localization of glutamate delta 1 (GluD1) receptor immunoreactivity in the mouse and monkey striatum.The Journal of comparative neurology · 2021Article
- GNG13 Is a Potential Marker of the State of Health of Alzheimer's Disease Patients' Cerebellum.Journal of molecular neuroscience : MN · 2021Article
- Identification of Novel Candidate Genes and Variants for Hearing Loss and Temporal Bone Anomalies.Genes · 2021Article
- Cbln2 and Cbln4 are expressed in distinct medial habenula-interpeduncular projections and contribute to different behavioral outputs.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Genetic Ablation of All Cerebellins Reveals Synapse Organizer Functions in Multiple Regions Throughout the Brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Shaping Synapses by the Neural Extracellular Matrix.Frontiers in neuroanatomy · 2018Review
- Cerebellins are differentially expressed in selective subsets of neurons throughout the brain.The Journal of comparative neurology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Precerebellin (Cbln1) is the precursor of the brain-specific hexadecapeptide cerebellin. Although cerebellin has properties of a conventional neuropeptide, its function is controversial because Cbln1 has structural features characteristic of circulating atypical collagens. Cbln1 is related to the three subunits of the complement C1q complex. Therefore, we hypothesized that Cbln1 participated in analogous heteromeric complexes with precerebellin-related proteins. Using LexA-Cbln1 as bait in a yeast two-hybrid screen, we isolated a cDNA encoding a novel Cbln1-related protein, designated Cbln3. The gene encoding cbln3 had the same intron-exon structure as cbln1 but mapped to a different mouse chromosome (14). The deduced amino acid sequence of Cbln3 was 55% identical to Cbln1 and also contained a C1q signature domain and signal sequence for secretion. In addition to binding avidly to Cbln3, Cbln1 also formed homomeric complexes. In contrast, Cbln3 homomeric association was weak. These interactions exhibited specificity because C1qB bound to neither Cbln1 nor Cbln3. Like cbln1, cbln3 was expressed in the cerebellum and dorsal cochlear nucleus in which it was detected in granule neurons. Because Cbln1 and Cbln3 are coexpressed in the brain and interact avidly, they may function as a secreted heteromeric complex in vivo.
Indexed as
Identifiers
10964938PMC6772977W2125287331What OpenQuestion holds
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.