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History and Perspectives of Ion-Transporting Rhodopsins

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Optogenetics

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

Abstract

The first light-sensing proteins used in optogenetics were rhodopsins. The word “rhodopsin” originates from the Greek words “rhodo” and “opsis,” indicating rose and sight, respectively. Although the classical meaning of rhodopsin is the red-colored pigment in our eyes, the modern meaning of rhodopsin encompasses photoactive proteins containing a retinal chromophore in animals and microbes. Animal and microbial rhodopsins possess 11-cis and all-trans retinal, respectively, to capture light in seven transmembrane α-helices, and photoisomerizations into all-trans and 13-cis forms, respectively, initiate each function. We are able to find ion-transporting proteins in microbial rhodopsins, such as light-gated channels and light-driven pumps, which are the main tools in optogenetics. In this chapter, historical aspects and molecular properties of rhodopsins are introduced. In the first part, “what is rhodopsin?”, general introduction of rhodopsin is presented. Then, molecular mechanism of bacteriorodopsin, a light-driven proton pump and the best-studied microbial rhodopsin, is described. In the section of channelrhodopsin, the light-gated ion channel, molecular properties, and several variants are introduced. As the history has proven, understanding the molecular mechanism of microbial rhodopsins is a prerequisite for useful functional design of optogenetics tools in future.

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Abbreviations

ACR:

Anion channel rhodopsin

Arch:

Archaerhodopsin 3

ASR:

Anabaena sensory rhodopsin

BR:

Bacteriorhodopsin

ChR:

Channelrhodopsin

CP:

Cytoplasmic

EC:

Extracellular

GPCR:

G-protein-coupled receptors

GtCCR4:

Cation channel rhodopsin from Guillardia theta

HeR:

Heliorhodopsin

HR:

Halorhodopsin

PoXeR:

Rhodopsin from Parvularcula oceani

Rh-GC:

Light-activated guanylyl cyclase rhodopsin

Rh-PDE:

Light-activated phosphodiesterase rhodopsin

RSB:

Retinal Schiff base

SRI:

Sensory rhodopsin I

SRII:

Sensory rhodopsin II

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Acknowledgments

This work was supported by Japanese Ministry of Education, Culture, Sports and Technology Grants 18H03986, 19H04959, and JST CREST Grant JPMJCR1753.

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Authors and Affiliations

  1. Department of Life Science and Applied Chemistry & OptoBioTechnology Research Center, Nagoya Institute of Technology, Nagoya, Japan

    Hideki Kandori

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  1. Hideki Kandori
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Correspondence to Hideki Kandori .

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Editors and Affiliations

  1. The Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan

    Hiromu Yawo

  2. OptoBioTechnology Research Center, Nagoya Institute of Technology, Nagoya, Japan

    Hideki Kandori

  3. National Institutes of Natural Sciences, Tokyo, Japan

    Amane Koizumi

  4. Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan

    Ryoichiro Kageyama

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Kandori, H. (2021). History and Perspectives of Ion-Transporting 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_1

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