Dissection of the components for PIP2 activation and thermosensation in TRP channels

@article{citeulike:3328248, abstract = {10.1073/pnas.0703420104 Phosphatidylinositol 4,5-bisphosphate (PIP) plays a central role in the activation of several transient receptor potential (TRP) channels. The role of PIP on temperature gating of thermoTRP channels has not been explored in detail, and the process of temperature activation is largely unexplained. In this work, we have exchanged different segments of the C-terminal region between cold-sensitive (TRPM8) and heat-sensitive (TRPV1) channels, trying to understand the role of the segment in PIP and temperature activation. A chimera in which the proximal part of the C-terminal of TRPV1 replaces an equivalent section of TRPM8 C-terminal is activated by PIP and confers the phenotype of heat activation. PIP, but not temperature sensitivity, disappears when positively charged residues contained in the exchanged region are neutralized. Shortening the exchanged segment to a length of 11 aa produces voltage-dependent and temperature-insensitive channels. Our findings suggest the existence of different activation domains for temperature, PIP, and voltage. We provide an interpretation for channel–PIP interaction using a full-atom molecular model of TRPV1 and PIP docking analysis.}, author = {Brauchi, Sebastian and Orta, Gerardo and Mascayano, Carolina and Salazar, Marcelo and Raddatz, Natalia and Urbina, Hector and Rosenmann, Eduardo and Gonzalez-Nilo, Fernando and Latorre, Ramon }, citeulike-article-id = {3328248}, doi = {http://dx.doi.org/10.1073/pnas.0703420104}, journal = {Proceedings of the National Academy of Sciences}, keywords = {channel, modeling, pip2, structure, trp, trp8}, month = {June}, number = {24}, pages = {10246--10251}, posted-at = {2008-09-24 05:14:42}, priority = {2}, title = {Dissection of the components for PIP2 activation and thermosensation in TRP channels}, url = {http://dx.doi.org/10.1073/pnas.0703420104}, volume = {104}, year = {2007} }

TY - JOUR ID - citeulike:3328248 L3 - citeulike-article-id:3328248 N2 - 10.1073/pnas.0703420104 Phosphatidylinositol 4,5-bisphosphate (PIP) plays a central role in the activation of several transient receptor potential (TRP) channels. The role of PIP on temperature gating of thermoTRP channels has not been explored in detail, and the process of temperature activation is largely unexplained. In this work, we have exchanged different segments of the C-terminal region between cold-sensitive (TRPM8) and heat-sensitive (TRPV1) channels, trying to understand the role of the segment in PIP and temperature activation. A chimera in which the proximal part of the C-terminal of TRPV1 replaces an equivalent section of TRPM8 C-terminal is activated by PIP and confers the phenotype of heat activation. PIP, but not temperature sensitivity, disappears when positively charged residues contained in the exchanged region are neutralized. Shortening the exchanged segment to a length of 11 aa produces voltage-dependent and temperature-insensitive channels. Our findings suggest the existence of different activation domains for temperature, PIP, and voltage. We provide an interpretation for channel–PIP interaction using a full-atom molecular model of TRPV1 and PIP docking analysis. IS - 24 JF - Proceedings of the National Academy of Sciences EP - 10251 TI - Dissection of the components for PIP2 activation and thermosensation in TRP channels VL - 104 SP - 10246 KW - channel KW - modeling KW - pip2 KW - structure KW - trp KW - trp8 AU - Brauchi, Sebastian AU - Orta, Gerardo AU - Mascayano, Carolina AU - Salazar, Marcelo AU - Raddatz, Natalia AU - Urbina, Hector AU - Rosenmann, Eduardo AU - Gonzalez-Nilo, Fernando AU - Latorre, Ramon PY - 2007/06/12/ UR - http://dx.doi.org/10.1073/pnas.0703420104 ER -