1 Ocak 2018 Dergi makalesi Açık Erişim

Vural, Ali; Fadillioglu, Ersin; Kelesoglu, Fatih; Ma, Dzwokai; Lanier, Stephen M.

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{
  "@context": "https://schema.org/", 
  "@id": 29387, 
  "@type": "ScholarlyArticle", 
  "creator": [
    {
      "@type": "Person", 
      "affiliation": "Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA", 
      "name": "Vural, Ali"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Med Univ South Carolina, Dept Cell & Mol Pharmacol & Expt Therapeut, Charleston, SC 29425 USA", 
      "name": "Fadillioglu, Ersin"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Med Univ South Carolina, Dept Cell & Mol Pharmacol & Expt Therapeut, Charleston, SC 29425 USA", 
      "name": "Kelesoglu, Fatih"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Univ Calif Santa Barbara, Dept Mol Cellular & Dev Biol, Neurosci Res Inst, Santa Barbara, CA 93106 USA", 
      "name": "Ma, Dzwokai"
    }, 
    {
      "@type": "Person", 
      "name": "Lanier, Stephen M."
    }
  ], 
  "datePublished": "2018-01-01", 
  "description": "Activator of G-protein signaling 3 (AGS3, also known as GPSM1) exhibits broad functional diversity and oscillates among different subcellular compartments in a regulated manner. AGS3 consists of a tetratricopeptide repeat (TPR) domain and a G-protein regulatory (GPR) domain. Here, we tested the hypothesis that phosphorylation of the AGS3 GPR domain regulates its subcellular distribution and functionality. In contrast to the cortical and/or diffuse non-homogeneous distribution of wild-type (WT) AGS3, an AGS3 construct lacking all 24 potential phosphorylation sites in the GPR domain localized to cytosolic puncta. This change in localization was revealed to be dependent upon phosphorylation of a single threonine amino acid (T602). The punctate distribution of AGS3-T602A was rescued by co-expression of G alpha(i) and G alpha(o) but not G alpha(s) or G alpha(q). Following treatment with alkaline phosphatase, both AGS3-T602A and WT AGS3 exhibited a gel shift in SDS-PAGE as compared to untreated WT AGS3, consistent with a loss of protein phosphorylation. The punctate distribution of AGS3-T602A was lost in an AGS3-A602T conversion mutant, but was still present upon T602 mutation to glutamate or aspartate. These results implicate dynamic phosphorylation as a discrete mechanism to regulate the subcellular distribution of AGS3 and associated functionality.", 
  "headline": "Role of G-proteins and phosphorylation in the distribution of AGS3 to cell puncta", 
  "identifier": 29387, 
  "image": "https://aperta.ulakbim.gov.tr/static/img/logo/aperta_logo_with_icon.svg", 
  "license": "http://www.opendefinition.org/licenses/cc-by", 
  "name": "Role of G-proteins and phosphorylation in the distribution of AGS3 to cell puncta", 
  "url": "https://aperta.ulakbim.gov.tr/record/29387"
}