Structural evidence for visual arrestin priming via complexation of phosphoinositols.

Animals Arrestin / chemistry Cattle Crystallography, X-Ray Inositol Phosphates / metabolism Mice Models, Molecular Protein Conformation Protein Domains Rhodopsin / metabolism Sequence Analysis, RNA Single-Cell Analysis
(1,4,5) myo-D-inositol triphosphate G protein-coupled receptor GPCR InsP(3) InsP(6) arrestin crystal structure myo-D-inositol hexakisphosphate phospholipase C photoreceptor phototransduction retina vision

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
03 02 2022
Historique:
received: 28 07 2021
revised: 06 09 2021
accepted: 29 09 2021
pubmed: 23 10 2021
medline: 22 3 2022
entrez: 22 10 2021
Statut: ppublish

Résumé

Visual arrestin (Arr1) terminates rhodopsin signaling by blocking its interaction with transducin. To do this, Arr1 translocates from the inner to the outer segment of photoreceptors upon light stimulation. Mounting evidence indicates that inositol phosphates (InsPs) affect Arr1 activity, but the Arr1-InsP molecular interaction remains poorly defined. We report the structure of bovine Arr1 in a ligand-free state featuring a near-complete model of the previously unresolved C-tail, which plays a crucial role in regulating Arr1 activity. InsPs bind to the N-domain basic patch thus displacing the C-tail, suggesting that they prime Arr1 for interaction with rhodopsin and help direct Arr1 translocation. These structures exhibit intact polar cores, suggesting that C-tail removal by InsP binding is insufficient to activate Arr1. These results show how Arr1 activity can be controlled by endogenous InsPs in molecular detail.

Identifiants

DOI: 10.1016/j.str.2021.10.002 PMID: 34678158 PMC: PMC8818024
pubmed: 34678158
pii: S0969-2126(21)00370-1
doi: 10.1016/j.str.2021.10.002
pmc: PMC8818024
mid: NIHMS1753853
pii:
doi:

Substances chimiques

Arrestin 0
Inositol Phosphates 0
Rhodopsin 9009-81-8

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

263-277.e5

Subventions

Organisme : NEI NIH HHS
ID : R01 EY009339
Pays : United States
Organisme : BLRD VA
ID : I01 BX004939
Pays : United States
Organisme : NEI NIH HHS
ID : P30 EY025585
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM111244
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM124165
Pays : United States
Organisme : NEI NIH HHS
ID : R24 EY024864
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103393
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007250
Pays : United States
Organisme : NEI NIH HHS
ID : P30 EY011373
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM133893
Pays : United States
Organisme : NEI NIH HHS
ID : T32 EY007157
Pays : United States
Organisme : CIHR
ID : PJT-159464
Pays : Canada
Organisme : NEI NIH HHS
ID : R24 EY027283
Pays : United States
Organisme : NEI NIH HHS
ID : F30 EY031566
Pays : United States

Informations de copyright

Copyright © 2021 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Christopher L Sander (CL)

Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA; Department of Ophthalmology and the Gavin Herbert Eye Institute, University of California, Irvine, CA 92697, USA.

Jennings Luu (J)

Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA; Department of Ophthalmology and the Gavin Herbert Eye Institute, University of California, Irvine, CA 92697, USA.

Kyumhyuk Kim (K)

Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.

David Furkert (D)

Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.

Kiyoung Jang (K)

Department of Lifestyle Medicine, Jeonbuk National University, Iksan 54596, Republic of Korea.

Joerg Reichenwallner (J)

Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.

MinSoung Kang (M)

Department of Lifestyle Medicine, Jeonbuk National University, Iksan 54596, Republic of Korea; Thin Film Materials Research Center, Korea Research Institute of Chemical Technology (KRICT), 141 Gajeong-ro, Daejeon 34114, Republic of Korea.

Ho-Jun Lee (HJ)

Department of Ophthalmology and the Gavin Herbert Eye Institute, University of California, Irvine, CA 92697, USA; Research Service, VA Long Beach Healthcare System, Long Beach, CA 90822, USA.

Bryan T Eger (BT)

Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.

Hui-Woog Choe (HW)

Department of Chemistry, Jeonbuk National University, Jeonju 54896, Republic of Korea.

Dorothea Fiedler (D)

Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.

Oliver P Ernst (OP)

Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada; Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.

Yong Ju Kim (YJ)

Department of Lifestyle Medicine, Jeonbuk National University, Iksan 54596, Republic of Korea; Department of Oriental Medicine Resources, College of Environmental and Bioresource Sciences, Jeonbuk National University, Iksan 54596, Republic of Korea.

Krzysztof Palczewski (K)

Department of Ophthalmology and the Gavin Herbert Eye Institute, University of California, Irvine, CA 92697, USA; Department of Chemistry and Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA; Department of Physiology & Biophysics, University of California, Irvine, CA 92697, USA.

Philip D Kiser (PD)

Department of Ophthalmology and the Gavin Herbert Eye Institute, University of California, Irvine, CA 92697, USA; Department of Physiology & Biophysics, University of California, Irvine, CA 92697, USA; Research Service, VA Long Beach Healthcare System, Long Beach, CA 90822, USA. Electronic address: pkiser@uci.edu.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Structural evidence for visual arrestin...
questionsmedicales.fr › Facteurs biologiques › Antigènes › Antigènes de surface › Arrestine › Structural evidence for visual arrestin...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Artiodactyla › Ruminants › Bovins › Structural evidence for visual arrestin...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Cristallographie aux rayons X › Structural evidence for visual arrestin...
questionsmedicales.fr › Glucides › Oses phosphates › Inositol phosphates › Structural evidence for visual arrestin...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Structural evidence for visual arrestin...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Structural evidence for visual arrestin...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structural evidence for visual arrestin...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Structural evidence for visual arrestin...
questionsmedicales.fr › Facteurs biologiques › Pigments biologiques › Pigments rétiniens › Opsines › Opsines des bâtonnets › Rhodopsine › Structural evidence for visual arrestin...
questionsmedicales.fr › Techniques d'investigation › Techniques génétiques › Analyse de séquence › Analyse de séquence d'ARN › Structural evidence for visual arrestin...
questionsmedicales.fr › Techniques d'investigation › Techniques cytologiques › Analyse sur cellule unique › Structural evidence for visual arrestin...