PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain
By T. Rohacs, Coeli M. B. Lopes, I. Michailidis, D. Logothetis. Nature Neuroscience, 2005
600 citations recorded by the source corpus.
Subfields: Molecular Biology, Nutrition and Dietetics, Sensory Systems
View Paper: https://www.semanticscholar.org/paper/25126cc248b4e879c0988c7580d1ca5a7431dcc5
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Citations in the corpus
- An introduction to TRP channels. (2006, background): “It is presently unclear why PIP2 appears to stimulate some TRP channels (TRPV5, TRPM5, TRPM7, TRPM8) (22, 24) while inhibiting others (TRPV1) (25, 26).”
- PIP2 is a necessary cofactor for ion channel function: how and why? (2008, background): “For TRPM8 and TRPM4, PIP2 shifts the voltage range of activation toward negative potentials (54, 70).”
- Attenuated cold sensitivity in TRPM8 null mice. (2007, neutral): “Analogous to TRPV1 and TRPA1, activation of TRPM8 by menthol or icilin is modulated by certain inflammatory mediators, such as protons, phospholipids, and bradykinin (Andersson et al., 2004; Premkumar et al., 2005; Rohacs et al., 2005).”
- TRP Channels (2012, neutral): “TRPM8 undergoes Ca2+-dependent desensitization, which has been attributed to breakdown of PIP2, which has an activating effect on the channel (357).”
- Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “For example, inositol lipid regulation was mapped to the TRP domains of the cytoplasmic tails of TrpM8 channels (1138, 1284).”
- TRP channels and pain. (2013, background): “Furthermore, mutagenesis experiments suggest that, as in the case of TRPV1, a positively charged putative PIP2-interacting domain resides in the C-terminal cytoplasmic tail of TRPM8, specifically within the Trp domain (Rohács et al. 2005).”