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Expression and localization of RGS9-2/G 5/R7BP complex in vivo is set by dynamic control of its constitutive degradation by cellular cysteine proteases

Academic Article
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Overview

authors

  • Anderson, G. R.
  • Lujan, R.
  • Semenov, A.
  • Pravetoni, M.
  • Posokhova, E. N.
  • Song, J. H.
  • Uversky, V.
  • Chen, C. K.
  • Wickman, K.
  • Martemyanov, Kirill

publication date

  • December 2007

journal

  • Journal of Neuroscience  Journal

abstract

  • A member of regulator of G-protein signaling family, RGS9-2, is an essential modulator of signaling through neuronal dopamine and opioid G-protein-coupled receptors. Recent findings indicate that the abundance of RGS9-2 determines sensitivity of signaling in the locomotor and reward systems in the striatum. In this study we report the mechanism that sets the concentration of RGS9-2 in vivo, thus controlling G-protein signaling sensitivity in the region. We found that RGS9-2 possesses specific degradation determinants which target it for constitutive destruction by lysosomal cysteine proteases. Shielding of these determinants by the binding partner R7 binding-protein (R7BP) controls RGS9-2 expression at the posttranslational level. In addition, binding to R7BP in neurons targets RGS9-2 to the specific intracellular compartment, the postsynaptic density. Implementation of this mechanism throughout ontogenetic development ensures expression of RGS9-2/type 5 G-protein beta subunit/R7BP complexes at postsynaptic sites in unison with increased signaling demands at mature synapses.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cell Membrane
  • Corpus Striatum
  • Cysteine Endopeptidases
  • Gene Expression Regulation, Enzymologic
  • Lysosomes
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • RGS Proteins
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Research

keywords

  • G-protein
  • RGS proteins
  • intracellular targeting
  • protein degradation
  • signal transduction
  • striatum
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Identity

International Standard Serial Number (ISSN)

  • 0270-6474

Digital Object Identifier (DOI)

  • 10.1523/jneurosci.3884-07.2007

PubMed ID

  • 18094251
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Additional Document Info

start page

  • 14117

end page

  • 14127

volume

  • 27

issue

  • 51

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