An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visua

Chen, Qiuyan; Zhuo, Ya; Sharma, Pankaj; Perez, Ivett; Francis, Derek J.; Chakravarthy, Srinivas; Vishnivetskiy, Sergey A.; Berndt, Sandra; Hanson, Susan M.; Zhan, Xuanzhi; Brooks, Evan K; Altenbach, Christian; Hubbell, Wayne L.; Klug, Candice S.; Iverson, T.M.; Gurevich, Vsevolod V.

doi:10.1016/j.jmb.2020.166790

An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visua

Journal Article · 01 February 2021 · J. Mol. Biol.

DOI:https://doi.org/10.1016/j.jmb.2020.166790· OSTI ID:1770411

Chen, Qiuyan; Zhuo, Ya; Sharma, Pankaj; Perez, Ivett; Francis, Derek J.; Chakravarthy, Srinivas; Vishnivetskiy, Sergey A.; Berndt, Sandra; Hanson, Susan M.; Zhan, Xuanzhi; Brooks, Evan K; Altenbach, Christian; Hubbell, Wayne L.; Klug, Candice S.; Iverson, T.M.; Gurevich, Vsevolod V.

Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: DOE - Office Of Science; National Institutes of Health (NIH)

OSTI ID:: 1770411

Journal Information:: J. Mol. Biol., Vol. 433, Issue (4)

Country of Publication:: United States

Language:: ENGLISH

References (66)

Structural basis of arrestin-3 activation and signaling Chen, Qiuyan; Perry, Nicole A.; Vishnivetskiy, Sergey A. Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/s41467-017-01218-8	journal	November 2017
Duration and Amplitude of the Light-Induced cGMP Hydrolysis in Vertebrate Photoreceptors Are Regulated by Multiple Phosphorylation of Rhodopsin and by Arrestin Binding Wilden, Ursula Biochemistry, Vol. 34, Issue 4 https://doi.org/10.1021/bi00004a040	journal	January 1995
Mechanism of Quenching of Phototransduction Krupnick, Jason G.; Gurevich, Vsevolod V.; Benovic, Jeffrey L. Journal of Biological Chemistry, Vol. 272, Issue 29 https://doi.org/10.1074/jbc.272.29.18125	journal	July 1997
β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor Goodman, Oscar B.; Krupnick, Jason G.; Santini, Francesca Nature, Vol. 383, Issue 6599 https://doi.org/10.1038/383447a0	journal	October 1996
The 2-adrenergic receptor/ arrestin complex recruits the clathrin adaptor AP-2 during endocytosis Laporte, S. A.; Oakley, R. H.; Zhang, J. Proceedings of the National Academy of Sciences, Vol. 96, Issue 7 https://doi.org/10.1073/pnas.96.7.3712	journal	March 1999
The Diverse Roles of Arrestin Scaffolds in G Protein–Coupled Receptor Signaling Peterson, Yuri K.; Luttrell, Louis M. Pharmacological Reviews, Vol. 69, Issue 3 https://doi.org/10.1124/pr.116.013367	journal	April 2017
The structural basis of arrestin-mediated regulation of G-protein-coupled receptors Gurevich, Vsevolod V.; Gurevich, Eugenia V. Pharmacology & Therapeutics, Vol. 110, Issue 3 https://doi.org/10.1016/j.pharmthera.2005.09.008	journal	June 2006
The functional cycle of visual arrestins in photoreceptor cells Gurevich, Vsevolod V.; Hanson, Susan M.; Song, Xiufeng Progress in Retinal and Eye Research, Vol. 30, Issue 6 https://doi.org/10.1016/j.preteyeres.2011.07.002	journal	November 2011
The molecular acrobatics of arrestin activation Gurevich, Vsevolod V.; Gurevich, Eugenia V. Trends in Pharmacological Sciences, Vol. 25, Issue 2 https://doi.org/10.1016/j.tips.2003.12.008	journal	February 2004
G protein-coupled receptor kinases: More than just kinases and not only for GPCRs Gurevich, Eugenia V.; Tesmer, John J. G.; Mushegian, Arcady Pharmacology & Therapeutics, Vol. 133, Issue 1 https://doi.org/10.1016/j.pharmthera.2011.08.001	journal	January 2012
Structural Basis of Arrestin-Dependent Signal Transduction Chen, Qiuyan; Iverson, Tina M.; Gurevich, Vsevolod V. Trends in Biochemical Sciences, Vol. 43, Issue 6 https://doi.org/10.1016/j.tibs.2018.03.005	journal	June 2018
Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin. Palczewski, K.; Pulvermüller, A.; Buczyłko, J. Journal of Biological Chemistry, Vol. 266, Issue 28 https://doi.org/10.1016/S0021-9258(18)55112-7	journal	October 1991
Elucidation of Inositol Hexaphosphate and Heparin Interaction Sites and Conformational Changes in Arrestin-1 by Solution Nuclear Magnetic Resonance Zhuang, Tiandi; Vishnivetskiy, Sergey A.; Gurevich, Vsevolod V. Biochemistry, Vol. 49, Issue 49 https://doi.org/10.1021/bi101596g	journal	December 2010
Nonvisual Arrestin Oligomerization and Cellular Localization Are Regulated by Inositol Hexakisphosphate Binding Milano, Shawn K.; Kim, You-Me; Stefano, Frank P. Journal of Biological Chemistry, Vol. 281, Issue 14 https://doi.org/10.1074/jbc.M512703200	journal	January 2006
A Model for Arrestin’s Regulation: The 2.8 Å Crystal Structure of Visual Arrestin Hirsch, Joel A.; Schubert, Carsten; Gurevich, Vsevolod V. Cell, Vol. 97, Issue 2 https://doi.org/10.1016/S0092-8674(00)80735-7	journal	April 1999
Crystal Structure of β-Arrestin at 1.9 Å Han, May; Gurevich, Vsevolod V.; Vishnivetskiy, Sergey A. Structure, Vol. 9, Issue 9 https://doi.org/10.1016/S0969-2126(01)00644-X	journal	September 2001
Crystal Structure of Cone Arrestin at 2.3Å: Evolution of Receptor Specificity Sutton, R. Bryan; Vishnivetskiy, Sergey A.; Robert, Justin Journal of Molecular Biology, Vol. 354, Issue 5 https://doi.org/10.1016/j.jmb.2005.10.023	journal	December 2005
Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes Zhan, Xuanzhi; Gimenez, Luis E.; Gurevich, Vsevolod V. Journal of Molecular Biology, Vol. 406, Issue 3 https://doi.org/10.1016/j.jmb.2010.12.034	journal	February 2011
Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide Shukla, Arun K.; Manglik, Aashish; Kruse, Andrew C. Nature, Vol. 497, Issue 7447 https://doi.org/10.1038/nature12120	journal	April 2013
Binding of inositol phosphates to arrestin Palczewski, Krzysztof; Pulvermüller, Alexander; Buczylko, Janina FEBS Letters, Vol. 295, Issue 1-3 https://doi.org/10.1016/0014-5793(91)81416-6	journal	December 1991
A Model for the Solution Structure of the Rod Arrestin Tetramer Hanson, Susan M.; Dawson, Eric S.; Francis, Derek J. Structure, Vol. 16, Issue 6 https://doi.org/10.1016/j.str.2008.03.006	journal	June 2008
Structure and function of the visual arrestin oligomer Hanson, Susan M.; Van Eps, Ned; Francis, Derek J. The EMBO Journal, Vol. 26, Issue 6 https://doi.org/10.1038/sj.emboj.7601614	journal	March 2007
Opposing Effects of Inositol Hexakisphosphate on Rod Arrestin and Arrestin2 Self-Association ^† Hanson, Susan M.; Vishnivetskiy, Sergey A.; Hubbell, Wayne L. Biochemistry, Vol. 47, Issue 3 https://doi.org/10.1021/bi7021359	journal	January 2008
Robust Self-Association Is a Common Feature of Mammalian Visual Arrestin-1 Kim, Miyeon; Hanson, Susan M.; Vishnivetskiy, Sergey A. Biochemistry, Vol. 50, Issue 12 https://doi.org/10.1021/bi1018607	journal	March 2011
Visual Arrestin Activity May Be Regulated by Self-association Schubert, Carsten; Hirsch, Joel A.; Gurevich, Vsevolod V. Journal of Biological Chemistry, Vol. 274, Issue 30 https://doi.org/10.1074/jbc.274.30.21186	journal	July 1999
Homo- and Hetero-oligomerization of β-Arrestins in Living Cells Storez, Hélène; Scott, Mark G. H.; Issafras, Hassan Journal of Biological Chemistry, Vol. 280, Issue 48 https://doi.org/10.1074/jbc.M508001200	journal	December 2005
Each rhodopsin molecule binds its own arrestin Hanson, S. M.; Gurevich, E. V.; Vishnivetskiy, S. A. Proceedings of the National Academy of Sciences, Vol. 104, Issue 9 https://doi.org/10.1073/pnas.0610886104	journal	February 2007
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Kang, Yanyong; Zhou, X. Edward; Gao, Xiang Nature, Vol. 523, Issue 7562 https://doi.org/10.1038/nature14656	journal	July 2015
A complex structure of arrestin-2 bound to a G protein-coupled receptor Yin, Wanchao; Li, Zhihai; Jin, Mingliang Cell Research, Vol. 29, Issue 12 https://doi.org/10.1038/s41422-019-0256-2	journal	November 2019
Structure of the M2 muscarinic receptor–β-arrestin complex in a lipid nanodisc Staus, Dean P.; Hu, Hongli; Robertson, Michael J. Nature, Vol. 579, Issue 7798 https://doi.org/10.1038/s41586-020-1954-0	journal	January 2020
Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor Lee, Yang; Warne, Tony; Nehmé, Rony Nature, Vol. 583, Issue 7818 https://doi.org/10.1038/s41586-020-2419-1	journal	June 2020
Structure of the neurotensin receptor 1 in complex with β-arrestin 1 Huang, Weijiao; Masureel, Matthieu; Qu, Qianhui Nature, Vol. 579, Issue 7798 https://doi.org/10.1038/s41586-020-1953-1	journal	January 2020
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin Hanson, S. M.; Francis, D. J.; Vishnivetskiy, S. A. Proceedings of the National Academy of Sciences, Vol. 103, Issue 13 https://doi.org/10.1073/pnas.0600733103	journal	March 2006
Identification of Receptor Binding-induced Conformational Changes in Non-visual Arrestins Zhuo, Ya; Vishnivetskiy, Sergey A.; Zhan, Xuanzhi Journal of Biological Chemistry, Vol. 289, Issue 30 https://doi.org/10.1074/jbc.M114.560680	journal	July 2014
Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin Zhuang, T.; Chen, Q.; Cho, M. -K. Proceedings of the National Academy of Sciences, Vol. 110, Issue 3 https://doi.org/10.1073/pnas.1215176110	journal	December 2012
Arrestin Mobilizes Signaling Proteins to the Cytoskeleton and Redirects their Activity Hanson, Susan M.; Cleghorn, Whitney M.; Francis, Derek J. Journal of Molecular Biology, Vol. 368, Issue 2 https://doi.org/10.1016/j.jmb.2007.02.053	journal	April 2007
Comparison of the levels of inositol metabolites in transformed haemopoietic cells and their normal counterparts Bunce, C. M.; French, P. J.; Allen, P. Biochemical Journal, Vol. 289, Issue 3 https://doi.org/10.1042/bj2890667	journal	February 1993
Arrestin2 and arrestin3 are differentially expressed in the rat brain during postnatal development Gurevich, E. V.; Benovic, J. L.; Gurevich, V. V. Neuroscience, Vol. 109, Issue 3 https://doi.org/10.1016/S0306-4522(01)00511-5	journal	February 2002
Arrestin2 expression selectively increases during neural differentiation: Arrestin2 in neural development Gurevich, Eugenia V.; Benovic, Jeffrey L.; Gurevich, Vsevolod V. Journal of Neurochemistry, Vol. 91, Issue 6 https://doi.org/10.1111/j.1471-4159.2004.02830.x	journal	December 2004
Inference of Macromolecular Assemblies from Crystalline State Krissinel, Evgeny; Henrick, Kim Journal of Molecular Biology, Vol. 372, Issue 3 https://doi.org/10.1016/j.jmb.2007.05.022	journal	September 2007
Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes Indrischek, Henrike; Prohaska, Sonja J.; Gurevich, Vsevolod V. BMC Evolutionary Biology, Vol. 17, Issue 1 https://doi.org/10.1186/s12862-017-1001-4	journal	July 2017
Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family. Attramadal, H.; Arriza, J. L.; Aoki, C. Journal of Biological Chemistry, Vol. 267, Issue 25 https://doi.org/10.1016/S0021-9258(19)37125-X	journal	September 1992
Polypeptide variants of beta-arrestin and arrestin3 Sterne-Marr, R.; Gurevich, V. V.; Goldsmith, P. Journal of Biological Chemistry, Vol. 268, Issue 21 https://doi.org/10.1016/S0021-9258(18)82304-3	journal	July 1993
beta -Arrestin 2: A Receptor-Regulated MAPK Scaffold for the Activation of JNK3 McDonald, P. H. Science, Vol. 290, Issue 5496 https://doi.org/10.1126/science.290.5496.1574	journal	November 2000
Identification of a Motif in the Carboxyl Terminus of β-Arrestin2 Responsible for Activation of JNK3 Miller, William E.; McDonald, Patricia H.; Cai, Sheng F. Journal of Biological Chemistry, Vol. 276, Issue 30 https://doi.org/10.1074/jbc.M102264200	journal	May 2001
Identification of Arrestin-3-specific Residues Necessary for JNK3 Kinase Activation Seo, Jungwon; Tsakem, Elviche L.; Breitman, Maya Journal of Biological Chemistry, Vol. 286, Issue 32 https://doi.org/10.1074/jbc.M111.260448	journal	August 2011
How Does Arrestin Assemble MAPKs into a Signaling Complex? Song, Xiufeng; Coffa, Sergio; Fu, Haian Journal of Biological Chemistry, Vol. 284, Issue 1 https://doi.org/10.1074/jbc.M806124200	journal	November 2008
Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin Gurevich, V. V.; Benovic, J. L. Journal of Biological Chemistry, Vol. 268, Issue 16 https://doi.org/10.1016/S0021-9258(19)50248-4	journal	June 1993
Arrestin Interactions with G Protein-coupled Receptors Gurevich, Vsevolod V.; Dion, Stephane B.; Onorato, James J. Journal of Biological Chemistry, Vol. 270, Issue 2 https://doi.org/10.1074/jbc.270.2.720	journal	January 1995
Visual and Both Non-visual Arrestins in Their “Inactive” Conformation Bind JNK3 and Mdm2 and Relocalize Them from the Nucleus to the Cytoplasm Song, Xiufeng; Raman, Dayanidhi; Gurevich, Eugenia V. Journal of Biological Chemistry, Vol. 281, Issue 30 https://doi.org/10.1074/jbc.M603659200	journal	July 2006
Differential Nucleocytoplasmic Shuttling of β-Arrestins: CHARACTERIZATION OF A LEUCINE-RICH NUCLEAR EXPORT SIGNAL IN β-ARRESTIN2 Scott, Mark G. H.; Le Rouzic, Erwann; Périanin, Axel Journal of Biological Chemistry, Vol. 277, Issue 40 https://doi.org/10.1074/jbc.M207552200	journal	August 2002
Subcellular Localization of β-Arrestins Is Determined by Their Intact N Domain and the Nuclear Export Signal at the C Terminus Wang, Ping; Wu, Yalan; Ge, Xin Journal of Biological Chemistry, Vol. 278, Issue 13 https://doi.org/10.1074/jbc.M208109200	journal	March 2003
Targeting the JNK MAPK cascade for inhibition: basic science and therapeutic potential Bogoyevitch, Marie A.; Boehm, Ingrid; Oakley, Aaron Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1697, Issue 1-2 https://doi.org/10.1016/j.bbapap.2003.11.016	journal	March 2004
β-Arrestin2 oligomers impair the clearance of pathological tau and increase tau aggregates Woo, Jung-A A.; Liu, Tian; Fang, Cenxiao C. Proceedings of the National Academy of Sciences, Vol. 117, Issue 9 https://doi.org/10.1073/pnas.1917194117	journal	February 2020
Conformation of receptor-bound visual arrestin Kim, M.; Vishnivetskiy, S. A.; Van Eps, N. Proceedings of the National Academy of Sciences, Vol. 109, Issue 45 https://doi.org/10.1073/pnas.1216304109	journal	October 2012
Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins Toledo Warshaviak, Dora; Khramtsov, Valery V.; Cascio, Duilio Journal of Magnetic Resonance, Vol. 232 https://doi.org/10.1016/j.jmr.2013.04.013	journal	July 2013
Improved radiation dose efficiency in solution SAXS using a sheath flow sample environment Kirby, Nigel; Cowieson, Nathan; Hawley, Adrian M. Acta Crystallographica Section D Structural Biology, Vol. 72, Issue 12 https://doi.org/10.1107/S2059798316017174	journal	November 2016
BioXTAS RAW : improvements to a free open-source program for small-angle X-ray scattering data reduction and analysis Hopkins, Jesse Bennett; Gillilan, Richard E.; Skou, Soren Journal of Applied Crystallography, Vol. 50, Issue 5 https://doi.org/10.1107/S1600576717011438	journal	September 2017
Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering Meisburger, Steve P.; Taylor, Alexander B.; Khan, Crystal A. Journal of the American Chemical Society, Vol. 138, Issue 20 https://doi.org/10.1021/jacs.6b01563	journal	May 2016
PRIMUS: a Windows PC-based system for small-angle scattering data analysis Konarev, Petr V.; Volkov, Vladimir V.; Sokolova, Anna V. Journal of Applied Crystallography, Vol. 36, Issue 5, p. 1277-1282 https://doi.org/10.1107/S0021889803012779	journal	September 2003
Accurate assessment of mass, models and resolution by small-angle scattering Rambo, Robert P.; Tainer, John A. Nature, Vol. 496, Issue 7446 https://doi.org/10.1038/nature12070	journal	April 2013
Determination of the regularization parameter in indirect-transform methods using perceptual criteria Svergun, D. I. Journal of Applied Crystallography, Vol. 25, Issue 4, p. 495-503 https://doi.org/10.1107/S0021889892001663	journal	August 1992
DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering Franke, Daniel; Svergun, Dmitri I. Journal of Applied Crystallography, Vol. 42, Issue 2, p. 342-346 https://doi.org/10.1107/S0021889809000338	journal	January 2009
Uniqueness of ab initio shape determination in small-angle scattering Volkov, Vladimir V.; Svergun, Dmitri I. Journal of Applied Crystallography, Vol. 36, Issue 3, p. 860-864 https://doi.org/10.1107/S0021889803000268	journal	April 2003
Restoring Low Resolution Structure of Biological Macromolecules from Solution Scattering Using Simulated Annealing Svergun, D. I. Biophysical Journal, Vol. 76, Issue 6, p. 2879-2886 https://doi.org/10.1016/S0006-3495(99)77443-6	journal	June 1999
Ambiguity assessment of small-angle scattering curves from monodisperse systems Petoukhov, Maxim V.; Svergun, Dmitri I. Acta Crystallographica Section D Biological Crystallography, Vol. 71, Issue 5 https://doi.org/10.1107/S1399004715002576	journal	April 2015

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