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Association of ca(v)1.3 l-type calcium channels with shank

Academic Article
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Overview

authors

  • Zhang, H.
  • Maximov, Anton
  • Fu, Y.
  • Xu, F.
  • Tang, T. S.
  • Tkatch, T.
  • Surmeier, D. J.
  • Bezprozvanny, I.

publication date

  • February 2005

journal

  • Journal of Neuroscience  Journal

abstract

  • Neurons express multiple types of voltage-gated calcium (Ca2+) channels. Two subtypes of neuronal L-type Ca2+ channels are encoded by CaV1.2 and CaV1.3 pore-forming subunits. Both CaV1.2 and CaV1.3 subunits contain class I PDZ (postsynaptic density-95/Discs large/zona occludens-1) domain-binding consensus at their C termini. In yeast two-hybrid screen of rat brain cDNA library with the C-terminal bait of CaV1.3a (long C-terminal splice variant) L-type Ca2+ channel subunit, we isolated multiple clones of postsynaptic adaptor protein Shank. We demonstrated a specific association of CaV1.3a C termini, but not of CaV1.2 C termini, with Shank PDZ domain in vitro. We further demonstrated that the proline-rich region present in C termini of CaV1.3a subunit binds to Shank Src homology 3 domain. We established that CaV1.3a and Shank localized to postsynaptic locations in cultured rat hippocampal neurons. By expressing epitope-tagged recombinant CaV1.3 subunits in rat hippocampal neuronal cultures, we demonstrated that the presence of Shank-binding motifs in CaV1.3a sequence is both necessary and sufficient for synaptic clustering of CaV1.3 L-type Ca2+ channels. In experiments with dominant-negative peptides and dihydropyridine-resistant CaV1.3a mutants, we demonstrated an importance of Shank-binding motif in CaV1.3a sequence for phosphorylated cAMP response element-binding protein (pCREB) signaling in cultured hippocampal neurons. Our results directly link CaV1.3 neuronal L-type Ca2+ channels to macromolecular signaling complex formed by Shank and other modular adaptor proteins at postsynaptic density and provide novel information about the role played by CaV1.3 L-type Ca2+ channels in pCREB signaling.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Calcium Channels
  • Calcium Channels, L-Type
  • Calcium Signaling
  • Cyclic AMP Response Element-Binding Protein
  • Hippocampus
  • Nerve Tissue Proteins
  • Neurons
  • Oocytes
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Rats
  • Recombinant Fusion Proteins
  • Two-Hybrid System Techniques
  • Xenopus laevis
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Research

keywords

  • CREB
  • PDZ domains
  • calcium channels
  • postsynaptic density
  • protein targeting
  • synapse
  • synaptic plasticity
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Identity

International Standard Serial Number (ISSN)

  • 0270-6474

Digital Object Identifier (DOI)

  • 10.1523/jneurosci.4554-04.2005

PubMed ID

  • 15689539
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Additional Document Info

start page

  • 1037

end page

  • 1049

volume

  • 25

issue

  • 5

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