Keys to the Kingdom: GPCR phosphorylation patterns direct β-arrestin.

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  • Author(s): Premont RT;Premont RT;Premont RT
  • Source:
    EMBO reports [EMBO Rep] 2020 Sep 03; Vol. 21 (9), pp. e51249. Date of Electronic Publication: 2020 Aug 24.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Comment
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Wiley Blackwell Country of Publication: England NLM ID: 100963049 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1469-3178 (Electronic) Linking ISSN: 1469221X NLM ISO Abbreviation: EMBO Rep Subsets: MEDLINE
    • Publication Information:
      Publication: 2014- : London, UK : Wiley Blackwell
      Original Publication: Oxford, UK : Published for EMBO by Oxford University Press, 2000-
    • Subject Terms:
      Arrestins*/genetics ; Arrestins*/metabolism ; MAP Kinase Signaling System*; Phosphorylation ; beta-Arrestin 1 ; beta-Arrestins
    • Abstract:
      The β-arrestin proteins are key regulators of G protein-coupled receptors, serving at least three distinct functions: inhibiting receptor signaling through G proteins, directing receptor trafficking from the cell surface after activation, and transmitting receptor-initiated signals directly. How the two β-arrestin proteins perform these many functions for hundreds of receptor types throughout the body, and specifically how β-arrestin-mediated signaling can be tuned to cellular conditions, remains an open question. Function-based evidence and recent structure-based evidence have suggested that patterns of receptor phosphorylation ("barcodes") may be a critical determinant of β-arrestin action. In this issue of EMBO Reports, Baidya and colleagues (Baidya et al, 2020a) report that specific receptor phosphorylation site clusters ("codes") determine whether β-arrestin 1 acts to promote or inhibit receptor activation of Erk mitogen-activated protein kinases. They provide direct evidence for a functional barcode system by transferring inhibitory and stimulatory codes between receptors, suggesting future work to understand just how code site location in a receptor and its phosphorylation status can lead to very different functions of bound β-arrestin proteins.
      (© 2020 The Author.)
    • Comments:
      Comment on: EMBO Rep. 2020 Sep 3;21(9):e49886. (PMID: 32715625)
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    • Grant Information:
      P01 HL075443 United States HL NHLBI NIH HHS; R01 DK113159 United States DK NIDDK NIH HHS; P01 HL075443 United States GF NIH HHS; R01 DK113159 United States GF NIH HHS
    • Accession Number:
      0 (Arrestins)
      0 (beta-Arrestin 1)
      0 (beta-Arrestins)
    • Publication Date:
      Date Created: 20200826 Date Completed: 20210121 Latest Revision: 20210904
    • Publication Date:
      20221213
    • Accession Number:
      PMC7507377
    • Accession Number:
      10.15252/embr.202051249
    • Accession Number:
      32840039