Signalling Via the G Protein-Activated K + Channels

Signalling Via the G Protein-Activated K + Channels The inwardly rectifying K + channels of the GIRK (K ir 3) family, members of the superfamily of inwardly rectifying K + channels (K ir ), are important physiological tools to regulate excitability in heart and brain by neurotransmitters, and the only ion channels conclusively shown to be activated by a direct interaction with heterotrimeric G protein subunits. During the last decade, especially since their cloning in 1993, remarkable progress has been made in understanding the structure, mechanisms of gating, activation by G proteins, and modulation of these channels. However, much of the molecular details of structure and of gating by G protein subunits and other factors, mechanisms of modulation and desensitization, and determinants of specificity of coupling to G proteins, remain unknown. This review summarizes both the recent advances and the unresolved questions now on the agenda in GIRK studies. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cellular Signalling Elsevier

Signalling Via the G Protein-Activated K + Channels

Cellular Signalling, Volume 9 (8) – Dec 1, 1997

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Publisher
Elsevier
Copyright
Copyright © 1997 Elsevier Science Inc.
ISSN
0898-6568
eISSN
1873-3913
DOI
10.1016/S0898-6568(97)00095-8
Publisher site
See Article on Publisher Site

Abstract

The inwardly rectifying K + channels of the GIRK (K ir 3) family, members of the superfamily of inwardly rectifying K + channels (K ir ), are important physiological tools to regulate excitability in heart and brain by neurotransmitters, and the only ion channels conclusively shown to be activated by a direct interaction with heterotrimeric G protein subunits. During the last decade, especially since their cloning in 1993, remarkable progress has been made in understanding the structure, mechanisms of gating, activation by G proteins, and modulation of these channels. However, much of the molecular details of structure and of gating by G protein subunits and other factors, mechanisms of modulation and desensitization, and determinants of specificity of coupling to G proteins, remain unknown. This review summarizes both the recent advances and the unresolved questions now on the agenda in GIRK studies.

Journal

Cellular SignallingElsevier

Published: Dec 1, 1997

References

  • Nature
    Clapham, D.E.; Neer, E.J.
  • Neuropharmacology
    Doupnik, C.A.; Dessauer, C.W.; Slepak, V.Z.; Gilman, A.G.; Davidson, N.; Lester, H.A.
  • Neurosci. Lett.
    Henry, D.J.; Chavkin, C.
  • Biochemistry
    Kwatra, M.M.; Benovic, J.L.; Caron, M.G.; Lefkowitz, R.J.; Hosey, M.M.
  • Circulation Res.
    Nair, L.A.; Inglese, J.; Stoffel, R.; Koch, W.J.; Lefkowitz, R.J.; Kwatra, M.M.; Grant, A.O.
  • Science
    Roush, E.

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