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Phosphorylation of a Reconstituted Potassium Channel

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Ion Channel Reconstitution

Abstract

Ion channels in biological membranes are dynamic entities. They of course act as pores through which ions can move down their electrochemical gradients, but more than that, many of them are regulatable pores. Channels can exist in more than one functional state, and rapid transitions between these states can be regulated by the voltage across the membrane or by the binding of a small molecule to a specific receptor that is intimately associated with the channel. Furthermore, it is now becoming evident that these rapid transitions are themselves subject to longer-term modulation, which may last for seconds, minutes, or even hours.

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References

  • Adams, W. B., and Levitan, I. B., 1982, Intracellular injection of protein kinase inhibitor blocks the serotonin-induced increase in K+ conductance in Aplysia neuron R15, Proc. Natl. Acad. Sci. U.S.A. 79:3877–3880.

    Article  PubMed  CAS  Google Scholar 

  • Alkon, D. L., Acosta-Urquidi, J., Olds, J., Kuzma, G., and Neary, J. T., 1983, Protein kinase injection reduces voltage-dependent potassium currents, Science 219:303–306.

    Article  PubMed  CAS  Google Scholar 

  • Castellucci, V. F., Kandel, E. R., Schwartz, J. H., Wilson, F. D., Nairn, A. C., and Greengard, P., 1980, Intracellular injection of the catalytic subunit of cyclic AMP-dependent protein kinase simulates facilitation of transmitter release underlying behavioral sensitization in Aplysia, Proc. Natl. Acad. Sci. U.S.A. 77:7492–7496.

    Article  CAS  Google Scholar 

  • Castellucci, V. F., Nairn, A., Greengard, P., Schwartz, J. H., and Kandel, E. R., 1982, Inhibitor of adenosine 3′:5′-monophosphate-dependent protein kinase blocks presynaptic facilitation in Aplysia, J. Neurosci. 2:1673–1681.

    CAS  Google Scholar 

  • Cohen, P., 1982, The role of protein phosphorylation in neural and hormonal control of cellular activity, Nature 296:613–620.

    Article  PubMed  CAS  Google Scholar 

  • Coronado, R., and Latorre, R., 1983, Phospholipid bilayers made from monolayers on patch-clamp pipettes, Biophys. J., 43:231-236.

    Google Scholar 

  • DePeyer, J. E., Cachelin, A. B., Levitan, I. B., and Reuter, H., 1982, Ca2+-Activated K+ conductance in internally perfused snail neurons is enhanced by protein phosphorylation, Proc. Natl. Acad. Sci. U.S.A. 79:4207–4211.

    Article  CAS  Google Scholar 

  • Ewald, D., Williams, A., and Levitan, I. B., 1985, Modulation of single Ca2+-dependent K+ channel activity by protein phosphorylation, Nature 315:503–506.

    Article  PubMed  CAS  Google Scholar 

  • Hamill, O. P., Marty, A., Neher, E., Sakmann, B., and Sigworth, F. J., 1981, Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches, Pfluegers Arch. 391:85–100.

    Article  CAS  Google Scholar 

  • Kaczmarek, L. K., Jennings, K. R., Struwasser, F., Nairn, A. C., Walter, U., Wilson, F. D., and Greengard, P., 1980, Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture, Proc. Natl. Acad. Sci. U.S.A. 77:7487–7491.

    Article  PubMed  CAS  Google Scholar 

  • Maruyama, Y., and Petersen, O. H., 1982, Cholecystokinin activation of single-channel currents is mediated by internal messenger in pancreatic acinar cells, Nature 300:61–63.

    Article  PubMed  CAS  Google Scholar 

  • Osterrieder, W., Brum, G., Hescheler, J., Trautwein, W., Flockerzi, V., and Hofmann, F., 1982, Injection of subunits of cyclic AMP-dependent protein kinase into cardiac myocytes modulates Ca2+ current, Nature 298:576–578.

    Article  PubMed  CAS  Google Scholar 

  • Shuster, M., Camardo, J., Siegelbaum, S., and Kandel, E. R., 1985, Cyclic AMP-dependent protein kinase closes the serotonin-sensitive K+ channels of Aplysia sensory neurons in cell-free membrane patches, Nature 313:392–395.

    Article  PubMed  CAS  Google Scholar 

  • Siegelbaum, S. A., and Tsien, R. W., 1983, Modulation of gated ion channels as a mode of transmitter action, Trends Neurosci. 6:307–313.

    Article  CAS  Google Scholar 

  • Siegelbaum, S. A., Camardo, J. S., and Kandel, E. R., 1982, Serotonin and cyclic AMP close single K+ channels in Aplysia sensory neurones, Nature 299:413–417.

    Article  PubMed  CAS  Google Scholar 

  • Suarez-Isla, B. A., Wan, K., Lindstrom, J., and Montai, M., 1983, Single-channel recordings from purified acetylcholine receptors reconstituted in bilayers formed at the tip of patch pipets, Biochemistry 22:2319–2323.

    Article  PubMed  CAS  Google Scholar 

  • Wilmsen, U., Methfessel, C., Hanke, W., and Boheim, G., 1983, Channel current fluctuation studies with solvent-free lipid bilayers using Neher-Sakmann pipettes, in: Physical Chemistry of Transmembrane Ion Motions, pp. 479-485, Elsevier, Amsterdam.

    Google Scholar 

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© 1986 Springer Science+Business Media New York

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Levitan, I.B. (1986). Phosphorylation of a Reconstituted Potassium Channel. In: Miller, C. (eds) Ion Channel Reconstitution. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1361-9_21

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  • DOI: https://doi.org/10.1007/978-1-4757-1361-9_21

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-1363-3

  • Online ISBN: 978-1-4757-1361-9

  • eBook Packages: Springer Book Archive

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