Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants

Biological Chemistry

Volumn 394, Issue 2, 2013, Pages 271-280

  Nagel, Georg ^a   Ullrich, Sybille ^a   Gueta, Ronnie ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

Electrophysiology; Expression; Light gated ion channel; Microbial rhodopsin; Optogenetics; Protein degradation

Indexed keywords

AMINO ACID; AROMATIC AMINO ACID; CATION CHANNEL; CHANNELRHODOPSIN 2; CYSTEINE; HALORHODOPSIN; OPSIN; RETINAL; RNA; THREONINE; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; CARRIER PROTEIN; CHANNELOPSIN-2, CHLAMYDOMONAS REINHARDTII;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHLORIDE PUMP; FLUORESCENCE; IMMUNOBLOTTING; MUTANT; NATRONOMONAS PHARAONIS; NONHUMAN; OOCYTE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN STABILITY; RETINA; WESTERN BLOTTING; ANIMAL; ANTAGONISTS AND INHIBITORS; DRUG EFFECTS; DRUG RESISTANCE; GENETICS; LIGHT; METABOLISM; MUTATION; RADIATION RESPONSE; XENOPUS LAEVIS;

ANIMALS; CARRIER PROTEINS; DRUG RESISTANCE; HALORHODOPSINS; LIGHT; MUTATION; OOCYTES; RETINALDEHYDE; XENOPUS LAEVIS;

EID: 84876561354     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0256     Document Type: Article

References (29)

1. Bamann, C., Nagel G., and Bamberg, E. (2010). Microbial rhodopsins in the spotlight. Curr. Opin. Neurobiol. 20, 610-616.
2. Berndt, A., Schoenenberger, P., Mattis, J., Tye, K.M., Deisseroth, K., Hegemann, P., and Oertner, T.G. (2011). High-efficiency channelrhodopsins for fast neuronal stimulation at low light levels. Proc. Natl. Acad. Sci. USA 108, 7595-7600.
3. Bissonnette, P., Noel, J., Coady, M.J., and Lapointe, J.Y. (1999). Functional expression of tagged human Na +-glucose cotransporter in Xenopus laevis oocytes. J. Physiol. 520 ( Pt 2 ), 359-371. (Pubitemid 29511900)
4. Boyden, E.S., Zhang, F., Bamberg, E., Nagel, G., and Deisseroth, K. (2005). Millisecond-timescale, genetically targeted optical control of neural activity. Nat. Neurosci. 8, 1263-1268. (Pubitemid 43348147)
5. Curnow, P. and Booth, P.J. (2010). The contribution of a covalently bound cofactor to the folding and thermodynamic stability of an integral membrane protein. J. Mol. Biol. 403, 630-642.
6. Geiger, D., Maierhofer, T., Al-Rasheid, K.A., Scherzer, S., Mumm, P., Liese, A., Ache, P., Wellmann, C., Marten, I., Grill, E., et al. (2011). Stomatal closure by fast abscisic acid signaling is mediated by the guard cell anion channel SLAH3 and the receptor RCAR1.
7. Sci. Signal. 4, ra32.
8. Kato, H.E., Zhang, F., Yizhar, O., Ramakrishnan, C., Nishizawa, T., Hirata, K., Ito, J., Aita, Y., Tsukazaki, T., Hayashi, S., et al. (2012). Crystal structure of the channelrhodopsin light-gated cation channel. Nature 482, 369-384.
9. Lanyi, J.K., Duschl, A., Hatfield, G.W., May, K., and Oesterhelt, D. (1990). The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins. J. Biol. Chem. 265, 1253-1260.
10. Lanyi, J.K. and Oesterhelt, D. (1982). Identification of the retinalbinding protein in halorhodopsin. J. Biol. Chem. 257, 2674-2677.
11. Lanyi, J.K., Zimanyi, L., Nakanishi, K., Derguini, F., Okabe, M., and Honig, B. (1988). Chromophore/protein and chromophore/ anion interactions in halorhodopsin. Biophys. J. 53, 185-191.
12. Leckner, J., Bonander, N., Wittung-Stafshede, P., Malmstrom, B.G., and Karlsson, B.G. (1997). The effect of the metal ion on the folding energetics of azurin: a comparison of the native, zinc and apoprotein. Biochim. Biophys. Acta 1342, 19-27. (Pubitemid 27464825)
13. Leduc-Nadeau, A., Lahjouji, K., Bissonnette, P., Lapointe, J.Y., and Bichet, D.G. (2007). Elaboration of a novel technique for purification of plasma membranes from Xenopus laevis oocytes.2 Am. J. Physiol. Cell Physiol. 292, C1132-1136. (Pubitemid 46440398)
14. Maiti, T.K., Engelhard, M., and Sheves, M. (2009). Retinal-protein interactions in halorhodopsin from Natronomonas pharaonis: binding and retinal thermal isomerization catalysis. J. Mol. Biol. 394, 472-484.
15. Nagel, G., Mockel, B., Buldt, G., and Bamberg, E. (1995). Functional expression of bacteriorhodopsin in oocytes allows direct measurement of voltage dependence of light induced H + pumping. FEBS Lett. 377, 263-266. (Pubitemid 26015079)
16. Nagel, G., Ollig, D., Fuhrmann, M., Kateriya, S., Mustl, A. M., Bamberg, E., and Hegemann, P. (2002). Channelrhodopsin-1: a light-gated proton channel in green algae. Science 2 96, 2395-2 398. (Pubitemid 34734214)
17. Nagel, G., Szellas, T., Huhn, W., Kateriya, S., Adeishvili, N., Berthold, P., Ollig, D., Hegemann, P., and Bamberg, E. (2003). Channelrhodopsin-2, a directly light-gated cation-selective membrane channel. Proc. Natl. Acad. Sci. USA 100, 13940-13945. (Pubitemid 37499170)
18. Nagel, G., Brauner, M., Liewald, J.F., Adeishvili, N., Bamberg, E., and Gottschalk, A. (2005). Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses. Curr. Biol. 15, 2279-2284. (Pubitemid 41790623)
19. Nagel, G., Szellas, T., Kateriya, S., Adeishvili, N., Hegemann, P., and Bamberg, E. (2005). Channelrhodopsins: directly light-gated cation channels. Biochem. Soc. Trans. 33, 863-866. (Pubitemid 41160880)
20. Pozdnyakova, I., Guidry, J., and Wittung-Stafshede, P. (2001). Copper stabilizes azurin by decreasing the unfolding rate. Arch. Biochem. Biophys. 390, 146-148. (Pubitemid 32493580)
21. Redmond, T.M., Yu, S., Lee, E., Bok, D., Hamasaki, D., Chen, N., Goletz, P., Ma, J.X., Crouch, R.K., and Pfeifer, K. (1998). Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle. Nat. Genet. 20, 344-351. (Pubitemid 28541631)
22. Schroll, C., Riemensperger, T., Bucher, D., Ehmer, J., Voller, T., Erbguth, K., Gerber, B., Hendel, T., Nagel, G., Buchner, E., et al. (2006). Light-induced activation of distinct modulatory neurons triggers appetitive or aversive learning in Drosophila larvae. Curr. Biol. 16, 1741-1747. (Pubitemid 44691780)
23. Seki, T., Fujishita, S., Azuma, M., and Suzuki, T. (1987). Retinal and 3-dehydroretinal in the egg of the clawed toad, Xenopus laevis. Zool. Sci. 4, 475-481.
24. von Lintig, J., Dreher, A., Kiefer, C., Wernet, M.F., and Vogt, K. (2001). Analysis of the blind Drosophila mutant ninaB identifies the gene encoding the key enzyme for vitamin A formation invivo. Proc. Natl. Acad. Sci. USA 98, 1130-1135. (Pubitemid 32121198)
25. Wang, T. and Montell, C. (2005). Rhodopsin formation in Drosophila is dependent on the PINTA retinoid-binding protein. J. Neurosci. 25, 5187-5194. (Pubitemid 40726971)
26. Wang, T., Jiao, Y., and Montell, C. (2007). Dissection of the pathway required for generation of vitamin A and for Drosophila phototransduction. J. Cell Biol. 177, 305-316. (Pubitemid 46658641)
27. Wittung-Stafshede, P. (2002). Role of cofactors in protein folding. Acc. Chem. Res. 35, 201-208.
28. Yamashita, Y., Kikukawa, T., Tsukamoto, T., Kamiya, M., Aizawa, T., Kawano, K., Miyauchi, S., Kamo, N., and Demura, M. (2011). Expression of salinarum halorhodopsin in Escherichia coli cells: solubilization in the presence of retinal yields the natural state. Biochim. Biophys. Acta 1808, 2905-2912.
29. Zhang, F., Wang, L.P., Brauner, M., Liewald, J.F., Kay, K., Watzke, N., Wood, P.G., Bamberg, E., Nagel, G., Gottschalk, A., et al. (2007). Multimodal fast optical interrogation of neural circuitry. Nature 446, 633-639. (Pubitemid 46606891)