| Autor: |
Tsai, Ching-Ju, Marino, Jacopo, Adaixo, Ricardo, Pamulal, Filip, Muehle, Jonas, Maeda, Shoji, Flock, Tilman, Taylorn, Nicholas M. I., Mohammed, Inayatulla, Matile, Hugues, Dawson, Roger J. P., Deupi, Xavier, Stahlberg, Henning, Schertler, Gebhard |
| Popis: |
One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the G beta subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of G beta as scaffold for recruiting G alpha subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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