Cited by 189Neuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration MechanismsReceptor Mechanisms and Signaling

The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

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Bolliger, Marc F., Martinelli, David C., Südhof, Thomas C.·2011·Proceedings of the National Academy of Sciences

Abstract

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.

    “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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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
Published
2011-01-24
Volume
108
Issue
6
Pages
2534-2539
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
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
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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