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The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins
Open accessAbstract
C1q-like genes (C1ql1-C1ql4) encode small, secreted proteins that are expressed in differential patterns in the brain but whose receptors and functions remain unknown. BAI3 protein, in contrast, is a member of the cell-adhesion class of G protein-coupled receptors that are expressed at high levels in the brain but whose ligands have thus far escaped identification. Using a biochemical approach, we show that all four C1ql proteins bind to the extracellular thrombospondin-repeat domain of BAI3 with high affinity, and that this binding is mediated by the globular C1q domains of the C1ql proteins. Moreover, we demonstrate that addition of submicromolar concentrations of C1ql proteins to cultured neurons causes a significant decrease in synapse density, and that this decrease was prevented by simultaneous addition of the thrombospondin-repeat fragment of BAI3, which binds to C1ql proteins. Our data suggest that C1ql proteins are secreted signaling molecules that bind to BAI3 and act, at least in part, to regulate synapse formation and/or maintenance.
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“Both the ADGRB3 receptor (BAI3) and kainate receptors are bound postsynaptically by C1ql proteins, regulating synaptogenesis in the case of ADGRB3 binding and postsynaptic recruitment in the case of kainate receptors (Sigoillot et al., 2015;Matsuda et al., 2016;Bolliger et al., 2011;Yuzaki, 2017;Martinelli et al., 2016).”
From Glutamate receptors in domestication and modern human evolution (2020) · cites this paper as Bolliger et al., 2011
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Metadata
- Authors
- Bolliger, M. F., Martinelli, D. C., & Südhof, T. C.
- Affiliations
- Stanford University (US)
- Department of Molecular and Cellular Physiology and
- Howard Hughes Medical Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-01-24
- Volume
- 108
- Issue
- 6
- Pages
- 2534-2539
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3038708
- OpenAlex
- W1994852479
- Cited by
- 189
- References
- 46
- Citations by year
- 2026: 15 · 2025: 12 · 2024: 19 · 2023: 13 · 2022: 12 · 2021: 14 · 2020: 13 · 2019: 13 · 2018: 9 · 2017: 12 · 2016: 15 · 2015: 9 · 2014: 5 · 2013: 14 · 2012: 8
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Mental Health (MH052804, R37MH052804)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- BAI3, ligand-receptor interactions, synaptogenesis, synapse maintenance, neurons, brain
- MeSH terms
- Animals, Brain, Cell Adhesion, Humans, Membrane Proteins, Nerve Tissue Proteins, Protein Binding, Synapses, Protein Structure, Tertiary, Tumor Necrosis Factors, Mice, HEK293 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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