TRP (transient receptor potential) channels respond to a plethora of stimuli in a fine-tuned manner. We show here that both membrane potential and the level of PI (phosphatidylinositol) phosphates are efficient regulators of TRP channel gating. Recent work has shown that this regulation applies to several members of the TRPV (TRP vanilloid) subfamily (TRPV1 and TRPV5) and the TRPM (TRP melastatin) subfamily (TRPM4/TRPM5/TRPM7/TRPM8), whereas regulation of members of the TRPC subfamily is still disputed. The mechanism whereby PIP2 (PI 4,5-bisphosphate) acts on TRPM4, a Ca2+- and voltage-activated channel, is shown in detail in this paper: (i) PIP2 may bind directly to the channel, (ii) PIP2 induces sensitization to activation by Ca2+, and (iii) PIP2 shifts the voltage dependence towards negative and physiologically more meaningful potentials. A PIP2-binding pocket seems to comprise a part of the TRP domain and especially pleckstrin homology domains in the C-terminus.
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February 2007
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Conference Article|
January 22 2007
Regulation of TRP channels: a voltage–lipid connection
B. Nilius;
B. Nilius
1
1Department of Physiology, Campus Gasthuisberg, KU Leuven, Herestraat 49, B-3000 Leuven, Belgium
1To whom correspondence should be addressed (email bernd.nilius@med.kuleuven.be).
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F. Mahieu;
F. Mahieu
1Department of Physiology, Campus Gasthuisberg, KU Leuven, Herestraat 49, B-3000 Leuven, Belgium
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Y. Karashima;
Y. Karashima
1Department of Physiology, Campus Gasthuisberg, KU Leuven, Herestraat 49, B-3000 Leuven, Belgium
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T. Voets
T. Voets
1Department of Physiology, Campus Gasthuisberg, KU Leuven, Herestraat 49, B-3000 Leuven, Belgium
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Publisher: Portland Press Ltd
Received:
July 24 2006
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2007 The Biochemical Society
2007
Biochem Soc Trans (2007) 35 (1): 105–108.
Article history
Received:
July 24 2006
Citation
B. Nilius, F. Mahieu, Y. Karashima, T. Voets; Regulation of TRP channels: a voltage–lipid connection. Biochem Soc Trans 1 February 2007; 35 (1): 105–108. doi: https://doi.org/10.1042/BST0350105
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