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An Asp79Asn mutation of the α2A-adrenoceptor interferes equally with agonist activation of individual Giα-family G protein subtypes

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
462
Issue
3
Identifiers
DOI: 10.1016/s0014-5793(99)01581-1
Keywords
  • G Protein-Coupled Receptor
  • G Protein
  • Adrenaline
  • Gtpase
Disciplines
  • Biology

Abstract

Abstract The quantitative effects of an Asp 79Asn mutation in the porcine α 2A-adrenoceptor on adrenaline-mediated stimulation of the α subunit of individual members of the G i family of G proteins were assessed by measuring GTP turnover number for fusion proteins between the wild type or mutated receptor and pertussis toxin-resistant forms of each of G i1, G i2 and G i3. In each case the receptor mutation limited activation of the G protein to 8–14% of that produced by the wild type receptor. Previous demonstration that in a single cell this mutation selectively interferes with α 2A-adrenoceptor regulation of distinct effector end points transduced by G i family members must therefore reflect differential requirements for amplification or the cellular location of individual, co-expressed, G proteins.

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