Structural basis of arrestin-3 activation and signaling

Structural basis of arrestin-3 activation and signaling

While arrestins are mainly associated with GPCR signaling, arrestin-3 can signal independently of receptor interaction. Here the authors present the structure of arrestin-3 bound to inositol hexakisphosphate (IP6) and propose a model for arrestin-3 activation.

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Autores principales: Qiuyan Chen, Nicole A. Perry, Sergey A. Vishnivetskiy, Sandra Berndt, Nathaniel C. Gilbert, Ya Zhuo, Prashant K. Singh, Jonas Tholen, Melanie D. Ohi, Eugenia V. Gurevich, Chad A. Brautigam, Candice S. Klug, Vsevolod V. Gurevich, T. M. Iverson
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/5669fd07492147f39e3967f45e7f0f53
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spelling oai:doaj.org-article:5669fd07492147f39e3967f45e7f0f532021-12-02T14:40:49ZStructural basis of arrestin-3 activation and signaling10.1038/s41467-017-01218-82041-1723https://doaj.org/article/5669fd07492147f39e3967f45e7f0f532017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01218-8https://doaj.org/toc/2041-1723While arrestins are mainly associated with GPCR signaling, arrestin-3 can signal independently of receptor interaction. Here the authors present the structure of arrestin-3 bound to inositol hexakisphosphate (IP6) and propose a model for arrestin-3 activation.Qiuyan ChenNicole A. PerrySergey A. VishnivetskiySandra BerndtNathaniel C. GilbertYa ZhuoPrashant K. SinghJonas TholenMelanie D. OhiEugenia V. GurevichChad A. BrautigamCandice S. KlugVsevolod V. GurevichT. M. IversonNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Qiuyan Chen
Nicole A. Perry
Sergey A. Vishnivetskiy
Sandra Berndt
Nathaniel C. Gilbert
Ya Zhuo
Prashant K. Singh
Jonas Tholen
Melanie D. Ohi
Eugenia V. Gurevich
Chad A. Brautigam
Candice S. Klug
Vsevolod V. Gurevich
T. M. Iverson
Structural basis of arrestin-3 activation and signaling
description While arrestins are mainly associated with GPCR signaling, arrestin-3 can signal independently of receptor interaction. Here the authors present the structure of arrestin-3 bound to inositol hexakisphosphate (IP6) and propose a model for arrestin-3 activation.
format article
author Qiuyan Chen
Nicole A. Perry
Sergey A. Vishnivetskiy
Sandra Berndt
Nathaniel C. Gilbert
Ya Zhuo
Prashant K. Singh
Jonas Tholen
Melanie D. Ohi
Eugenia V. Gurevich
Chad A. Brautigam
Candice S. Klug
Vsevolod V. Gurevich
T. M. Iverson
author_facet Qiuyan Chen
Nicole A. Perry
Sergey A. Vishnivetskiy
Sandra Berndt
Nathaniel C. Gilbert
Ya Zhuo
Prashant K. Singh
Jonas Tholen
Melanie D. Ohi
Eugenia V. Gurevich
Chad A. Brautigam
Candice S. Klug
Vsevolod V. Gurevich
T. M. Iverson
author_sort Qiuyan Chen
title Structural basis of arrestin-3 activation and signaling
title_short Structural basis of arrestin-3 activation and signaling
title_full Structural basis of arrestin-3 activation and signaling
title_fullStr Structural basis of arrestin-3 activation and signaling
title_full_unstemmed Structural basis of arrestin-3 activation and signaling
title_sort structural basis of arrestin-3 activation and signaling
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/5669fd07492147f39e3967f45e7f0f53
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AT nicoleaperry structuralbasisofarrestin3activationandsignaling
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