Association of neuronal calcium channels with modular adaptor proteins

Anton Maximov, Thomas C. Südhof, Ilya Bezprozvanny

Research output: Contribution to journalArticlepeer-review

260 Scopus citations


Presynaptic voltage-gated calcium (Ca2+) channels mediate Ca2+ influx into the presynaptic terminal that triggers synaptic vesicle fusion and neurotransmitter release. The immediate proximity of Ca2+ channels to the synaptic vesicle release apparatus is critical for rapid and efficient synaptic transmission. In a series of biochemical experiments, we demonstrate a specific association of the cytosolic carboxyl terminus of the N-type Ca2+ channel pore-forming α(1B) subunit with the modular adaptor proteins Mint1 and CASK. The carboxyl termini of α(1B) bind to the first PDZ domain of Mint1 (Mint1-1). The proline-rich region present in the carboxyl termini of α(1B) binds to the SH3 domain of CASK. Mint1-1 is specific for the E/D-X- W-C/S-COOH consensus, which defines a novel class of PDZ domains (class III). The Mint1-1 PDZ domain-binding motif is present only in the 'long' carboxyl- terminal splice variants of N-type (α(1B)) and P/Q-type (α(1A)) Ca2+ channels, but not in R-type (α(1E)) or L-type (α(1C)) Ca2+ channels. Our results directly link presynaptic Ca2+ channels to a macromolecular complex formed by modular adaptor proteins at synaptic junction and advance our understanding of coupling between cell adhesion and synaptic vesicle exocytosis.

Original languageEnglish (US)
Pages (from-to)24453-24456
Number of pages4
JournalJournal of Biological Chemistry
Issue number35
StatePublished - Aug 27 1999

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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