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...
| Autores: | , , , , , , , , , , , , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2019 |
| País: | España |
| Institución: | Universitat Autònoma de Barcelona |
| Repositorio: | Dipòsit Digital de Documents de la UAB |
| Idioma: | inglés |
| OAI Identifier: | oai:ddd.uab.cat:224183 |
| Acceso en línea: | https://ddd.uab.cat/record/224183 https://dx.doi.org/urn:doi:10.1016/j.celrep.2019.08.053 |
| Access Level: | acceso abierto |
| Palabra clave: | GPCRs β-arrestins Cellular signaling Antibody fragments Biosensors Biased agonism Desensitization Negative staining Electron microscopy |
| Sumario: | 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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