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Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis.

Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL
Biochemistry 41 3321-8 (2002)
Cited: 119 times
EuropePMC logo PMID: 11876640

Abstract

Arrestin binding to activated, phosphorylated G protein-coupled receptors (GPCRs) represents a critical step in regulation of light- and hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and terminating signaling events. Using a combination of X-ray crystallography, molecular modeling, mutagenesis, and binding analysis, we reveal structural features of arrestin-2 that may enable simultaneous binding to phosphorylated receptor, SH3 domains, phosphoinositides, and beta-adaptin. The structure of full-length arrestin-2 thus provides a uniquely oriented scaffold for assembly of multiple, diverse molecules involved in GPCR signal transduction.

Reviews - 1jsy mentioned but not cited (5)

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  5. New Structural Perspectives in G Protein-Coupled Receptor-Mediated Src Family Kinase Activation. Berndt S, Liebscher I. Int J Mol Sci 22 6489 (2021)

Articles - 1jsy mentioned but not cited (15)

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  11. Crystal Structure of β-Arrestin 2 in Complex with CXCR7 Phosphopeptide. Min K, Yoon HJ, Park JY, Baidya M, Dwivedi-Agnihotri H, Maharana J, Chaturvedi M, Chung KY, Shukla AK, Lee HH. Structure 28 1014-1023.e4 (2020)
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Reviews citing this publication (36)

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  32. MicroRNAs Regulating Cytoskeleton Dynamics, Endocytosis, and Cell Motility-A Link Between Neurodegeneration and Cancer? Gerasymchuk D, Hubiernatorova A, Domanskyi A. Front Neurol 11 549006 (2020)
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