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Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR

Nature Communications, ISSN: 2041-1723, Vol: 12, Issue: 1, Page: 7158
2021
  • 19
    Citations
  • 0
    Usage
  • 46
    Captures
  • 1
    Mentions
  • 393
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    19
  • Captures
    46
  • Mentions
    1
    • News Mentions
      1
      • News
        1
  • Social Media
    393
    • Shares, Likes & Comments
      393
      • Facebook
        393

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Article Description

β-arrestins (βarrs) play multifaceted roles in the function of G protein-coupled receptors (GPCRs). βarrs typically interact with phosphorylated C-terminal tail (C tail) and transmembrane core (TM core) of GPCRs. However, the effects of the C tail- and TM core-mediated interactions on the conformational activation of βarrs have remained elusive. Here, we show the conformational changes for βarr activation upon the C tail- and TM core-mediated interactions with a prototypical GPCR by nuclear magnetic resonance (NMR) spectroscopy. Our NMR analyses demonstrated that while the C tail-mediated interaction alone induces partial activation, in which βarr exists in equilibrium between basal and activated conformations, the TM core- and the C tail-mediated interactions together completely shift the equilibrium toward the activated conformation. The conformation-selective antibody, Fab30, promotes partially activated βarr into the activated-like conformation. This plasticity of βarr conformation in complex with GPCRs engaged in different binding modes may explain the multifunctionality of βarrs.

Bibliographic Details

Shiraishi, Yutaro; Kofuku, Yutaka; Ueda, Takumi; Pandey, Shubhi; Dwivedi-Agnihotri, Hemlata; Shukla, Arun K; Shimada, Ichio

Springer Science and Business Media LLC

Chemistry; Biochemistry, Genetics and Molecular Biology; Multidisciplinary; Physics and Astronomy

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