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The Structural Basis of Arrestin Functions pp 119–132Cite as

Localization of Conformational Dynamics of Arrestins by HDX-MS

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Abstract

Arrestins are a family of multifunctional adapter proteins that were originally discovered by their ability to desensitize G protein-coupled receptors (GPCRs ). Besides desensitization of GPCRs, arrestins regulate various signaling molecules, such as mitogen-activated protein kinase (MAPK) signaling pathway proteins and ubiquitination pathway proteins. To have such diverse functions, arrestins are structurally dynamic. In this chapter, we will discuss the structural dynamics of arrestins revealed by hydrogen/deuterium exchange mass spectrometry (HDX-MS).

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Authors and Affiliations

  1. School of Pharmacy, Sungkyunkwan University, Suwon, 16419, Republic of Korea

    Ji Young Park, Hee Ryung Kim & Ka Young Chung

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  1. Ji Young Park
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  2. Hee Ryung Kim
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  3. Ka Young Chung
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Correspondence to Ka Young Chung .

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  1. Department of Pharmacology, Vanderbilt University, Nashville, Tennessee, USA

    Vsevolod V. Gurevich

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Park, J.Y., Kim, H.R., Chung, K.Y. (2017). Localization of Conformational Dynamics of Arrestins by HDX-MS. In: Gurevich, V. (eds) The Structural Basis of Arrestin Functions. Springer, Cham. https://doi.org/10.1007/978-3-319-57553-7_9

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