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The Structural Basis of Arrestin Functions pp 255–271Cite as

Monofunctional Elements of Multi-functional Proteins

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Abstract

Arrestins can act as activators or molecular scaffolds for various effectors, including MAPK signaling cascades, clathrin and AP2, E3 ubiquitin ligases, and phosphatases. Current investigations have focused on isolating the regions of arrestin that interact with effectors in an attempt to understand the role of arrestin in mediating downstream signaling pathways. The interactions of arrestins with some of their binding partners has recently been tested using monofunctional elements, which only have a particular function of a protein, and range from peptide fragments to separated domains. These elements can be used to recapitulate protein-protein interactions, and have been applied successfully in elucidation of the structural basis of the interactions of arrestin with receptors, clathrin, AP2, kinases, and several other effector proteins.

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Notes

  1. 1.

    This chapter uses the systematic names of the arrestin proteins: arrestin-1 (historic name S-antigen, visual or rod arrestin), arrestin-2 (β-arrestin or β-arrestin1), arrestin-3 (β-arrestin2), and arrestin-4 (cone or X-arrestin).

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Acknowledgements

This work was supported by NIH grants to VVG (GM077561, GM109955, EY011500), EVG (NS065868, DA030103) and TMI (GM095633, GM120569). NAP was supported by T32 GM007628 and the American Heart Association (16PRE30180007).

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  1. Department of Pharmacology, Vanderbilt University, Nashville, TN, 46795, USA

    Nicole A. Perry, T. M. Iverson, Eugenia V. Gurevich & Vsevolod V. Gurevich

  2. Department of Chemistry, Tennessee Technological University, Cookeville, TN, 38505, USA

    Xuanzhi Zhan

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    Vsevolod V. Gurevich

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Perry, N.A., Zhan, X., Iverson, T.M., Gurevich, E.V., Gurevich, V.V. (2017). Monofunctional Elements of Multi-functional Proteins. In: Gurevich, V. (eds) The Structural Basis of Arrestin Functions. Springer, Cham. https://doi.org/10.1007/978-3-319-57553-7_18

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