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Conformational Sensors and Domain Swapping Reveal Structural and Functional Differences between β-Arrestin Isoforms

  • Eshan Ghosh
  • , Hemlata Dwivedi
  • , Mithu Baidya
  • , Ashish Srivastava
  • , Punita Kumari
  • , Tomek Stepniewski
  • , Hee Ryung Kim
  • , Mi Hye Lee
  • , Jaana van Gastel
  • , Madhu Chaturvedi
  • , Debarati Roy
  • , Shubhi Pandey
  • , Jagannath Maharana
  • , Ramon Guixà-González
  • , Louis M. Luttrell
  • , Ka Young Chung
  • , Somnath Dutta
  • , Jana Selent
  • , Arun K. Shukla
  • Indian Institute of Technology Kanpur
  • Pompeu Fabra University
  • Sungkyunkwan University
  • Medical University of South Carolina
  • Flanders Institute for Biotechnology
  • University of Antwerp
  • Autonomous University of Barcelona
  • Department of Veterans Affairs
  • Indian Institute of Science Bangalore

Research output: Contribution to journalArticlepeer-review

Abstract

Ghosh et al. discover structural differences between β-arrestin isoforms (β-arrestin 1 and 2), which are universal regulators of signaling and trafficking of G-protein-coupled receptors (GPCRs). These findings have direct implications for understanding the regulatory and signaling paradigms of GPCRs and designing novel therapeutics targeting this important class of receptors.

Original languageEnglish
Pages (from-to)3287-3299.e6
JournalCell Reports
Volume28
Issue number13
DOIs
StatePublished - 24 Sep 2019

Keywords

  • GPCRs
  • antibody fragments
  • biased agonism
  • biosensors
  • cellular signaling
  • desensitization
  • electron microscopy
  • negative staining
  • β-arrestins

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