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Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins

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Optogenetics

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 1293))

Abstract

Ion-transporting microbial rhodopsins are widely used as major molecular tools in optogenetics. They are categorized into light-gated ion channels and light-driven ion pumps. While the former passively transport various types of cations and anions in a light-dependent manner, light-driven ion pumps actively transport specific ions, such as H+, Na+, Cl−, against electrophysiological potential by using light energy. Since the ion transport by these pumps induces hyperpolarization of membrane potential and inhibit neural firing, light-driven ion-pumping rhodopsins are mostly applied as inhibitory optogenetics tools. Recent progress in genome and metagenome sequencing identified more than several thousands of ion-pumping rhodopsins from a wide variety of microbes, and functional characterization studies has been revealing many new types of light-driven ion pumps one after another. Since light-gated channels were reviewed in other chapters in this book, here the rapid progress in functional characterization, molecular mechanism study, and optogenetic application of ion-pumping rhodopsins were reviewed.

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Abbreviations

AntR:

Inward H+ pumping Antarctic rhodopsin

AR:

Acetabularia rhodopsin

Arch or AR3:

Archaerhodopsin-3

ASR:

Anabaena sensory rhodopsin

ASRT :

Anabaena sensory rhodopsin transducer

ATR-FTIR:

Attenuated total reflection-Fourier transform infrared

BacHR:

Bacterial halorhodopsin

BR:

Bacteriorhodopsin

ChR:

Channelrhodopsin

ClR:

Bacterial Cl− pump rhodopsin

CP:

Cytoplasmic

cryoEM:

Cryo-electron microscopy

CsR:

Coccomyxa subellipsoidea rhodopsin

DNP:

Dynamic nuclear-polarization

DsNaR:

Dokdonia sp. PRO95 Na+ pump rhodopsin

EPR:

Paramagnetic electron resonance

ER:

Endoplasmic reticulum

ESR:

Exiguobacterium sibiricum rhodopsin

FdNaR:

Flagellimonas sp_DIK Na+ pump rhodopsin

FR:

Fulvimarina pelagi rhodopsin

FTIR:

Fourier transform infrared

GlNaR:

Gillisia limnaea Na+ pump rhodopsin

GPCR:

G-protein coupled receptor

GR:

Gloeobacter rhodopsin

HKR:

Histidine kinase rhodopsin

HR:

Halorhodopsin

HS-AFM:

High-speed atomic force microscopy

HsHR:

Halobacterium salinarum halorhodopsin

IAA:

Indole-3-acetic acid

IaNaR:

Indibacter alkaliphilus Na+ pump rhodopsin

IC:

Internal cavity

KR2 or DeNaR:

Krokinobacter eikastus rhodopsin 2

LR:

Leptosphaeria rhodopsin

MrHR:

Mastigocladopsis repens halorhodopsin

NaR:

Na+ pump rhodopsin

NMR:

Nuclear magnetic resonance

NM-R3 or NmClR:

Nonlabens marinus bacterial Cl− pump rhodopsin

NR:

Neurospora rhodopsin

NsXeR:

Nanosalina xenorhodopsin

NyNaR:

Nonlabens sp. YIK_SED-11 Na+ pump rhodopsin

OLPVRII:

Organic Lake Phycodnavirus rhodopsin II

ORP:

Opsin-related proteins

PaR:

DTG rhodopsins from Pantoea ananatis

PhaeoRD:

Phaeosphaeria rhodopsin

pHR or NpHR:

Natronomonas pharaonis halorhodopsin

PoClR:

Parvularcula oceani bacterial Cl− pump rhodopsin

PoXeR:

Parvularcula oceani xenorhodopsin

PR:

Proteorhodopsin

PRG:

Proton release group

PspR:

DTG rhodopsins from Pseudomonas putida

PvR:

DTG rhodopsins from Pantoea vagans

QM/MM:

Quantum mechanics/molecular mechanics

RhGC:

Rhodopsin guanylyl cyclase

Rh-PDE:

Rhodopsin phosphodiesterase

RmXeR:

Rubricoccus marinus xenorhodopsin

RSB:

Retinal Schiff base

RxR:

Rubrobacter xylanophilus rhodopsin

SFX:

Serial femtosecond crystallography

SyHR:

Synechocystis sp. PCC 7509 halorhodopsin

SzR:

Schizorhodopsin

TM:

Transmembrane

TR:

Thermophilic rhodopsin

TR-SFX:

Time-resolved serial femtosecond crystallography

XeR:

Xenorhodopsin

XFEL:

X-ray free electron laser.

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Acknowledgments

The author would like to thank Drs. Leonid S. Brown and Oded Béjà for their careful reading of the manuscript and insightful comments.  I apologize to all authors whose research could not be cited because of space limitations. This work was supported by grants from the Japanese Ministry of Education, Culture, Sports, Science and Technology (17H03007), Takeda Science Foundation, The Mitsubishi Foundation, and Yamada Science Foundation.

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Correspondence to Keiichi Inoue .

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Inoue, K. (2021). Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins. In: Yawo, H., Kandori, H., Koizumi, A., Kageyama, R. (eds) Optogenetics. Advances in Experimental Medicine and Biology, vol 1293. Springer, Singapore. https://doi.org/10.1007/978-981-15-8763-4_6

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