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From Phototaxis to Biomedical Applications: Investigating the Molecular Mechanism of Channelrhodopsins

  • Chapter
Electrophysiology of Unconventional Channels and Pores

Part of the book series: Springer Series in Biophysics ((BIOPHYSICS,volume 18))

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Abstract

Phototactic response in the green algae Chlamydomonas reinhardtii is mediated through two rhodopsin proteins, channelrhodopsin-1 (ChR1) and channelrhodopsin-2 (ChR2). Similar to other microbial-type rhodopsins, ChRs have a seven transmembrane motif with a retinal moiety bound to a highly conserved lysine residue that activates the protein upon illumination with blue light. While most bacterial and algal homologues function as an ion pump, ChR2 is an inwardly rectified non-selective cation channel. Although ChR2 shares structural similarity to the proton pump bacteriorhodopsin (bR), ChR2 and bR have distinct functionality. The molecular determinants which define the differing protein functionalities can be elucidated through structure/function experiments. Moreover, the unique properties of ChR2 have paved the way for the emerging field of optogenetics. Cell-specific expression of ChR2 in vivo can invoke action potentials upon light activation and trigger downstream behavioral responses. However, the wild type properties of ChR2 limit the utility of this protein in biomedical applications. Therefore, understanding the underlying structural changes and mechanism of ion translocation for ChRs will be crucial for targeted engineering of ChR mutants with favorable optogenetic properties.

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Acknowledgements

The Dempski laboratory gratefully acknowledges the WPI Research Foundation for support.

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  1. Department of Chemistry and Biochemistry, Worcester Polytechnic Institute, 100 Institute Road, Worcester, MA, 01609, USA

    Ryan Richards & Robert E. Dempski

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Correspondence to Robert E. Dempski .

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  1. Department of Biology and Biochemistry, University of Houston, Houston, TX, USA

    Anne H. Delcour

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Richards, R., Dempski, R.E. (2015). From Phototaxis to Biomedical Applications: Investigating the Molecular Mechanism of Channelrhodopsins. In: Delcour, A.H. (eds) Electrophysiology of Unconventional Channels and Pores. Springer Series in Biophysics, vol 18. Springer, Cham. https://doi.org/10.1007/978-3-319-20149-8_15

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