Structural evidence for visual arrestin priming via complexation of phosphoinositols.

Autor:	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., 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., Kim K; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada., Furkert D; Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Strasse 10, 13125 Berlin, Germany., Jang K; Department of Lifestyle Medicine, Jeonbuk National University, Iksan 54596, Republic of Korea., Reichenwallner J; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada., 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., 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., Eger BT; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada., Choe HW; Department of Chemistry, Jeonbuk National University, Jeonju 54896, Republic of Korea., Fiedler D; Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Strasse 10, 13125 Berlin, Germany., 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., 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., 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., 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.
Jazyk:	angličtina
Zdroj:	Structure (London, England : 1993) [Structure] 2022 Feb 03; Vol. 30 (2), pp. 263-277.e5. Date of Electronic Publication: 2021 Oct 21.
DOI:	10.1016/j.str.2021.10.002
Abstrakt:	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. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2021 Elsevier Ltd. All rights reserved.)
Databáze:	MEDLINE
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