Living organisms require detecting the environmental thermal clues for survival, allowing them to avoid noxious stimuli or find prey moving in the dark. In mammals, the Transient Receptor Potential ion channels superfamily is constituted by 27 polymodal receptors whose activity is controlled by small ligands, peptide toxins, protons and voltage. The thermoTRP channels subgroup exhibits unparalleled temperature dependence -behaving as heat and cold sensors. Functional studies have dissected their biophysical features in detail, and the advances of single-particle Cryogenic Electron microscopy provided the structural framework required to propose detailed channel gating mechanisms. However, merging structural and functional evidence for temperature-driven gating of thermoTRP channels has been a hard nut to crack, remaining an open question nowadays. Here we revisit the highlights on the study of heat and cold sensing in thermoTRP channels in the light of the structural data that has emerged during recent years.
Long Terminal Repeat (LTR) retrotransposons replicate through “copy and paste” mechanisms mediated by reverse transcription in virus-like particles (VLPs) and integration in the nucleus (see article from Lee and Martienssen, pp. 2241–2251). VLP DNA-sequencing reveals complementary DNA (cDNA) replication intermediates from active retrotransposons. Instead of functional linear intermediates that integrate in the nucleus, the Arabidopsis retroelement SISYPHUS lacks features important for nuclear import, and instead accumulates circular cDNA from futile autointegration within the VLP. In Greek mythology, Sisyphus was condemned to the futile task of rolling a huge boulder uphill eternally. Image created and provided Seung Cho Lee, Evan Ernst, and Robert A. Martienssen.
Thermodynamic and structural basis of temperature-dependent gating in TRP channels
Ignacio Diaz-Franulic, Christian Verdugo, Felipe Gonzalez, Fernando Gonzalez-Nilo, Ramon Latorre; Thermodynamic and structural basis of temperature-dependent gating in TRP channels. Biochem Soc Trans 1 November 2021; 49 (5): 2211–2219. doi: https://doi.org/10.1042/BST20210301
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