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

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...

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Bibliographic Details
Authors: Ghosh, Eshan|||0000-0003-4532-1329, Dwivedi, Hemlata, Baidya, Mithu, Srivastava, Ashish, Kumari, Punita, Stepniewski, Tomek, Kim, Hee Ryung, Lee, Mi-Hye, van Gastel, Jana, Chaturvedi, Madhu, Roy, Debarati, Pandey, Shubhi, Maharana, Jagannath, Guixà González, Ramon|||0000-0003-0397-9800, Luttrell, Louis M., Chung, Ka Young, Dutta, Somnath, Selent, Jana|||0000-0002-1844-4449, Shukla, Arun K.
Format: article
Publication Date:2019
Country:España
Institution:Universitat Autònoma de Barcelona
Repository:Dipòsit Digital de Documents de la UAB
Language:English
OAI Identifier:oai:ddd.uab.cat:224183
Online Access:https://ddd.uab.cat/record/224183
https://dx.doi.org/urn:doi:10.1016/j.celrep.2019.08.053
Access Level:Open access
Keyword:GPCRs
β-arrestins
Cellular signaling
Antibody fragments
Biosensors
Biased agonism
Desensitization
Negative staining
Electron microscopy
Description
Summary: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.

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