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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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Self-citationStructural diversity of G protein-coupled receptors and significance for drug discovery
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BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module
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Self-citationUemura, T., Lee, S.-J., Yasumura, M., Takeuchi, T., Yoshida, T., Ra, M., Taguchi, R., Sakimura, K., & Mishina, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.035 · Cited by 496
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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
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