PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29425510-8 2018 Interestingly, we found that PIP2 facilitates the N-C interaction in TRPM8/-V1, resulting in channel potentiation. Phosphatidylinositol 4,5-Diphosphate 29-33 transient receptor potential cation channel subfamily M member 8 Homo sapiens 69-78 29038158-4 2017 TRPM8 activation by CFA was potentiated by cold temperature involving the phosphatidylinositol 4,5-bisphosphate binding residue (L1008), but was independent of the icilin and menthol binding site residue Y745 and, essentially, the N-terminal amino acids 1-800. Phosphatidylinositol 4,5-Diphosphate 74-111 transient receptor potential cation channel subfamily M member 8 Homo sapiens 0-5 21762971-7 2011 TRPM8 receptor function and hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) were characterized by means of Ca(2+) imaging and spatiotemporal dynamics of phospholipase C (PLC) delta1-pleckstrin homology-green fluorescent protein, respectively. Phosphatidylinositol 4,5-Diphosphate 42-79 transient receptor potential cation channel subfamily M member 8 Homo sapiens 0-5 23554496-0 2013 Ambient temperature affects the temperature threshold for TRPM8 activation through interaction of phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 98-135 transient receptor potential cation channel subfamily M member 8 Homo sapiens 58-63 23554496-7 2013 These findings suggest that ambient temperature does affect the temperature threshold for TRPM8 activation through interaction of PIP2. Phosphatidylinositol 4,5-Diphosphate 130-134 transient receptor potential cation channel subfamily M member 8 Homo sapiens 90-95 21762971-7 2011 TRPM8 receptor function and hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) were characterized by means of Ca(2+) imaging and spatiotemporal dynamics of phospholipase C (PLC) delta1-pleckstrin homology-green fluorescent protein, respectively. Phosphatidylinositol 4,5-Diphosphate 81-85 transient receptor potential cation channel subfamily M member 8 Homo sapiens 0-5 26657057-8 2016 RESULTS: Either co-transfection with Pirt or intracellular application of PIP2 (but not PI) significantly enhanced menthol-induced TRPM8 currents. Phosphatidylinositol 4,5-Diphosphate 74-78 transient receptor potential cation channel subfamily M member 8 Homo sapiens 131-136 26657057-9 2016 Furthermore, Pirt and PIP2 synergistically modulated menthol-induced TRPM8 currents. Phosphatidylinositol 4,5-Diphosphate 22-26 transient receptor potential cation channel subfamily M member 8 Homo sapiens 69-74 26657057-11 2016 CONCLUSION: Pirt and PIP2 synergistically enhance TRPM8 channel activity, and Pirt regulates TRPM8 channel activity by increasing the single channel conductance. Phosphatidylinositol 4,5-Diphosphate 21-25 transient receptor potential cation channel subfamily M member 8 Homo sapiens 50-55 26536261-4 2015 Inferences of TRPM8 structure have come from mutagenesis experiments coupled to electrophysiology, mainly regarding the fourth transmembrane helix (S4), which constitutes a moderate voltage-sensing domain, and about cold sensor and phosphatidylinositol 4,5-bisphosphate binding sites, which are both located in the C-terminus of TRPM8. Phosphatidylinositol 4,5-Diphosphate 232-269 transient receptor potential cation channel subfamily M member 8 Homo sapiens 14-19 25352597-1 2014 Expressed in somatosensory neurons of the dorsal root and trigeminal ganglion, the transient receptor potential melastatin 8 (TRPM8) channel is a Ca(2+)-permeable cation channel activated by cold, voltage, phosphatidylinositol 4,5-bisphosphate, and menthol. Phosphatidylinositol 4,5-Diphosphate 206-243 transient receptor potential cation channel subfamily M member 8 Homo sapiens 83-124 25352597-1 2014 Expressed in somatosensory neurons of the dorsal root and trigeminal ganglion, the transient receptor potential melastatin 8 (TRPM8) channel is a Ca(2+)-permeable cation channel activated by cold, voltage, phosphatidylinositol 4,5-bisphosphate, and menthol. Phosphatidylinositol 4,5-Diphosphate 206-243 transient receptor potential cation channel subfamily M member 8 Homo sapiens 126-131 22005680-0 2011 Decrease in phosphatidylinositol 4,5-bisphosphate levels mediates desensitization of the cold sensor TRPM8 channels. Phosphatidylinositol 4,5-Diphosphate 12-49 transient receptor potential cation channel subfamily M member 8 Homo sapiens 101-106 22005680-2 2011 Here we show that activation of TRPM8 by cold or menthol evokes a decrease in cellular phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] levels. Phosphatidylinositol 4,5-Diphosphate 87-124 transient receptor potential cation channel subfamily M member 8 Homo sapiens 32-37 22005680-5 2011 Intracellular dialysis of PtdIns(4,5)P(2) inhibited desensitization both in native neuronal and recombinant TRPM8 channels. Phosphatidylinositol 4,5-Diphosphate 26-41 transient receptor potential cation channel subfamily M member 8 Homo sapiens 108-113 19019830-6 2009 These results suggest an adaptation model whereby TRPM8-mediated Ca2+ influx activates PLC, thereby decreasing PIP2 levels and resulting in reduced TRPM8 activity. Phosphatidylinositol 4,5-Diphosphate 111-115 transient receptor potential cation channel subfamily M member 8 Homo sapiens 50-55 19019830-5 2009 Additionally, TRPM8 activity is sensitive to the phospholipid phosphoinositol 4,5-bisphosphate (PIP2), a substrate for the enzyme phospholipase C (PLC). Phosphatidylinositol 4,5-Diphosphate 96-100 transient receptor potential cation channel subfamily M member 8 Homo sapiens 14-19 15852009-2 2005 Here, we demonstrate a central role for phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) in the activation of recombinant TRPM8 channels by both cold and menthol. Phosphatidylinositol 4,5-Diphosphate 40-77 transient receptor potential cation channel subfamily M member 8 Homo sapiens 125-130 19404398-6 2009 Furthermore, addition of scPPX1 altered the voltage-dependence and blocked the activity of the purified TRPM8 channels reconstituted into planar lipid bilayers, where the activity of the channel was initiated by cold and menthol in the presence of phosphatidylinositol 4,5-biphosphate (PtdIns(4,5)P(2)). Phosphatidylinositol 4,5-Diphosphate 248-284 transient receptor potential cation channel subfamily M member 8 Homo sapiens 104-109 17548815-4 2007 A chimera in which the proximal part of the C-terminal of TRPV1 replaces an equivalent section of TRPM8 C-terminal is activated by PIP2 and confers the phenotype of heat activation. Phosphatidylinositol 4,5-Diphosphate 131-135 transient receptor potential cation channel subfamily M member 8 Homo sapiens 98-103 17074062-0 2007 Ethanol inhibits cold-menthol receptor TRPM8 by modulating its interaction with membrane phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 89-126 transient receptor potential cation channel subfamily M member 8 Homo sapiens 39-44 15716403-0 2005 Functional control of cold- and menthol-sensitive TRPM8 ion channels by phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 72-109 transient receptor potential cation channel subfamily M member 8 Homo sapiens 50-55 15716403-8 2005 The crucial role of PIP2 on the function of TRPM8 suggests that the membrane PIP2 level may be an important regulator of cold transduction in vivo. Phosphatidylinositol 4,5-Diphosphate 20-24 transient receptor potential cation channel subfamily M member 8 Homo sapiens 44-49 15716403-8 2005 The crucial role of PIP2 on the function of TRPM8 suggests that the membrane PIP2 level may be an important regulator of cold transduction in vivo. Phosphatidylinositol 4,5-Diphosphate 77-81 transient receptor potential cation channel subfamily M member 8 Homo sapiens 44-49 32245175-3 2020 The emerging mechanism of PIRT-dependent TRPM8 regulation involves a competitive interaction between PIRT and TRPM8 for the activating phosphatidylinositol 4,5-bisphosphate (PIP2) lipid. Phosphatidylinositol 4,5-Diphosphate 135-172 transient receptor potential cation channel subfamily M member 8 Homo sapiens 41-46 32245175-3 2020 The emerging mechanism of PIRT-dependent TRPM8 regulation involves a competitive interaction between PIRT and TRPM8 for the activating phosphatidylinositol 4,5-bisphosphate (PIP2) lipid. Phosphatidylinositol 4,5-Diphosphate 135-172 transient receptor potential cation channel subfamily M member 8 Homo sapiens 110-115 32245175-3 2020 The emerging mechanism of PIRT-dependent TRPM8 regulation involves a competitive interaction between PIRT and TRPM8 for the activating phosphatidylinositol 4,5-bisphosphate (PIP2) lipid. Phosphatidylinositol 4,5-Diphosphate 174-178 transient receptor potential cation channel subfamily M member 8 Homo sapiens 41-46 32245175-3 2020 The emerging mechanism of PIRT-dependent TRPM8 regulation involves a competitive interaction between PIRT and TRPM8 for the activating phosphatidylinositol 4,5-bisphosphate (PIP2) lipid. Phosphatidylinositol 4,5-Diphosphate 174-178 transient receptor potential cation channel subfamily M member 8 Homo sapiens 110-115 31141957-5 2019 The recently described structures of the TRPM8 channel alone or complexed with known agonists and PIP2 are also discussed. Phosphatidylinositol 4,5-Diphosphate 98-102 transient receptor potential cation channel subfamily M member 8 Homo sapiens 41-46 30733385-2 2019 Activation of TRPM8 by cooling compounds relies on allosteric actions of agonist and membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), but lack of structural information has thus far precluded a mechanistic understanding of ligand and lipid sensing by TRPM8. Phosphatidylinositol 4,5-Diphosphate 100-137 transient receptor potential cation channel subfamily M member 8 Homo sapiens 14-19 30733385-2 2019 Activation of TRPM8 by cooling compounds relies on allosteric actions of agonist and membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), but lack of structural information has thus far precluded a mechanistic understanding of ligand and lipid sensing by TRPM8. Phosphatidylinositol 4,5-Diphosphate 139-143 transient receptor potential cation channel subfamily M member 8 Homo sapiens 14-19 30733385-3 2019 Using cryo-electron microscopy, we determined the structures of TRPM8 in complex with the synthetic cooling compound icilin, PIP2, and Ca2+, as well as in complex with the menthol analog WS-12 and PIP2 Our structures reveal the binding sites for cooling agonists and PIP2 in TRPM8. Phosphatidylinositol 4,5-Diphosphate 125-129 transient receptor potential cation channel subfamily M member 8 Homo sapiens 64-69 31216483-2 2019 Both Galphaq and the downstream hydrolysis of phosphatidylinositol 4, 5-bisphosphate (PIP2) inhibit TRPM8. Phosphatidylinositol 4,5-Diphosphate 46-84 transient receptor potential cation channel subfamily M member 8 Homo sapiens 100-105 31216483-2 2019 Both Galphaq and the downstream hydrolysis of phosphatidylinositol 4, 5-bisphosphate (PIP2) inhibit TRPM8. Phosphatidylinositol 4,5-Diphosphate 86-90 transient receptor potential cation channel subfamily M member 8 Homo sapiens 100-105 30733385-4 2019 Notably, PIP2 binds to TRPM8 in two different modes, which illustrate the mechanism of allosteric coupling between PIP2 and agonists. Phosphatidylinositol 4,5-Diphosphate 9-13 transient receptor potential cation channel subfamily M member 8 Homo sapiens 23-28 30733385-4 2019 Notably, PIP2 binds to TRPM8 in two different modes, which illustrate the mechanism of allosteric coupling between PIP2 and agonists. Phosphatidylinositol 4,5-Diphosphate 115-119 transient receptor potential cation channel subfamily M member 8 Homo sapiens 23-28