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Functional studies of single-site variants in the calmodulin-binding domain of rc3/neurogranin in xenopus oocytes

Academic Article
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Overview

authors

  • Watson, J. B.
  • Margulies, J. E.
  • Coulter, P. M.
  • Gerendasy, D. D.
  • Sutcliffe, J. Gregor
  • Cohen, R. W.

publication date

  • November 1996

journal

  • Neuroscience Letters  Journal

abstract

  • Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine36 -->alanine (Ser36-->Ala), serine36-->glycine (Ser36-->Gly), and phenylalanine37-->tryptophan (Phe37-->Trp), which bind calmodulin but are deficient in protein kinase C (PKC) phosphorylation, display serotonin-evoked Ca(2+)-dependent Cl- currents in oocytes similar to control oocytes. A serine36-->aspartate (Ser36-->Asp) variant, which does not bind calmodulin and mimics the PKC-phosphorylated state of RC3, significantly enhances serotonin-evoked currents in a manner similar to wild-type. The results suggest that RC3 not only regulates the availability of free calmodulin in a dendritic spine but also, when phosphorylated, independently stimulates G-protein coupled second messenger pathways that generate inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) and intracellular Ca2+.

subject areas

  • Amino Acid Sequence
  • Animals
  • Calmodulin
  • Calmodulin-Binding Proteins
  • Chlorides
  • Electric Conductivity
  • Female
  • Genetic Variation
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Neurogranin
  • Oocytes
  • Patch-Clamp Techniques
  • Serotonin
  • Xenopus laevis
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Research

keywords

  • 'IQ' motif
  • calmodulin-binding mutants
  • dendritic protein
  • long term potentiation-associated protein
  • protein kinase C substrate
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Identity

International Standard Serial Number (ISSN)

  • 0304-3940

Digital Object Identifier (DOI)

  • 10.1016/s0304-3940(96)13203-1

PubMed ID

  • 8971810
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Additional Document Info

start page

  • 183

end page

  • 186

volume

  • 219

issue

  • 3

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