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. Author manuscript; available in PMC: 2020 Jul 30.
Published in final edited form as: Adv Cancer Res. 2020 Feb 5;145:139–156. doi: 10.1016/bs.acr.2020.01.001

Fig. 2.

Fig. 2

Structural representation of β-arrestin indicating some of the interaction interfaces. A potential mechanism underlying the multi-functionality of β-arrestins is their ability to interact with a large number of cellular partners. As some of the interaction interfaces are quite distinct from each other, it offers a framework to modulate selected β-arrestin functions by targeting the protein-protein interaction. This image is adopted from and modified based on a previous publication from our laboratory Ghosh, E., Srivastava, A., Baidya, M., Kumari, P., Dwivedi, H., Nidhi, K., et al. (2017). A synthetic intrabody-based selective and generic inhibitor of GPCR endocytosis. Nature Nanotechnology, 12, 1190–1198.