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Association of neuronal calcium channels with modular adaptor proteins

Academic Article
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Overview

authors

  • Maximov, Anton
  • Sudhof, T. C.
  • Bezprozvanny, I.

publication date

  • August 1999

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Presynaptic voltage-gated calcium (Ca(2+)) channels mediate Ca(2+) influx into the presynaptic terminal that triggers synaptic vesicle fusion and neurotransmitter release. The immediate proximity of Ca(2+) 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 Ca(2+) channel pore-forming alpha(1B) subunit with the modular adaptor proteins Mint1 and CASK. The carboxyl termini of alpha(1B) bind to the first PDZ domain of Mint1 (Mint1-1). The proline-rich region present in the carboxyl termini of alpha(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 (alpha(1B)) and P/Q-type (alpha(1A)) Ca(2+) channels, but not in R-type (alpha(1E)) or L-type (alpha(1C)) Ca(2+) channels. Our results directly link presynaptic Ca(2+) 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.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Brain
  • COS Cells
  • Calcium
  • Calcium Channels
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Carrier Proteins
  • Cell Adhesion
  • Exocytosis
  • Guanylate Kinase
  • Ligands
  • Membrane Proteins
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Nucleoside-Phosphate Kinase
  • Protein Binding
  • Rats
  • Signal Transduction
  • Synaptic Transmission
  • Yeasts
  • src Homology Domains
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.274.35.24453

PubMed ID

  • 10455105
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Additional Document Info

start page

  • 24453

end page

  • 24456

volume

  • 274

issue

  • 35

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