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Conformational Sensors and Domain Swapping Reveal Structural and Functional Differences between β-Arrestin Isoforms / Ghosh, Eshan (Indian Institute of Technology, Kanpur) ; Dwivedi, Hemlata (Indian Institute of Technology, Kanpur) ; Baidya, Mithu (Indian Institute of Technology, Kanpur) ; Srivastava, Ashish (Indian Institute of Technology, Kanpur) ; Kumari, Punita (Indian Institute of Technology, Kanpur) ; Stepniewski, Tomek (Universitat Pompeu Fabra. Departament de Ciències Experimentals i de la Salut) ; Kim, Hee Ryung (Sungkyunkwan University, South Korea) ; Lee, Mi-Hye (Medical University of South Carolina) ; van Gastel, Jana (University of Antwerp) ; Chaturvedi, Madhu (Indian Institute of Technology, Kanpur) ; Roy, Debarati (Indian Institute of Technology, Kanpur) ; Pandey, Shubhi (Indian Institute of Technology, Kanpur) ; Maharana, Jagannath (Indian Institute of Technology, Kanpur) ; Guixà González, Ramon (Universitat Autònoma de Barcelona. Laboratori de Medicina Computacional) ; Luttrell, Louis M. (Medical University of South Carolina) ; Chung, Ka Young (Sungkyunkwan University, South Korea) ; Dutta, Somnath (Indian Institute of Sciences, Bangalore) ; Selent, Jana (Universitat Pompeu Fabra. Departament de Ciències Experimentals i de la Salut) ; Shukla, Arun K. (Indian Institute of Technology, Kanpur)
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.
2019 - DOI (Digital Object Identifier)

10.1016/j.celrep.2019.08.053
Cell reports, Vol. 28 Núm. 13 (24 2019) , p. 3287-3299.e6

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