Yet another PLoS ONE article was evaluated by F1000 Biology, making the total number of evaluated articles to 180. At any given time, about 3-4% of PLoS ONE articles are evaluated at F1000. Below is a simplified version of the evaluation of the article by Myers et al. The article was evaluated by Felix Viana of the UMH Instituto de Neurociencias, Spain.
Evolution of thermal response properties in a cold-activated TRP channel.
Myers BR, Sigal YM, Julius D
PLoS ONE 2009 4(5):e5741 [abstract on PubMed] [citations on Google Scholar] [related articles] [FREE full text]
Myers BR, Sigal YM, Julius D
PLoS ONE 2009 4(5):e5741 [abstract on PubMed] [citations on Google Scholar] [related articles] [FREE full text]
"This is an interesting study, comparing functional properties of ortholog thermosensitive TRPM8 channels in frogs and rats. It suggests that intrinsic thermosensitivity is tuned to the normal operating range of body temperature. Animals populate different ecological niches. Survival in these environments is strongly dependent on properly tuned sensory systems that allow the rapid detection of food and the avoidance of dangerous situations, like predators or exposure to extreme temperatures. TRPM8 is a transient receptor potential activated by cold temperatures and cooling compounds like menthol {1, 2}. In mice, TRPM8 is critical for the detection of mild cold temperatures, and perhaps for unpleasant or noxious cold. In this paper, the authors cloned and characterized the functional properties of frog, specifically Xenopus laevis and Xenopus tropicalis, TRPM8. These aquatic frogs are poikilotherms, their core body temperature fluctuates with environmental temperature, in a range clearly below the core body temperature of mammals and birds. While various properties (i.e. menthol sensitivity and voltage-dependence) of frog TRPM8 were similar to those described for rat and mice, there was a clear shift in the thermal response of the channel towards temperatures below their "normal" core temperature. The amino acid sequence of Xenopus TRPM8 displays 75% identity to the rat sequence. This result suggests that this thermo TRP is under strong evolutionary pressure, likely reflecting an important role in temperature sensing in species other than mammals. Besides the intrinsic interest of this novel information for thermosensory biology in general, a careful analysis of the differences in sequence between different species, and the construction of chimeras, may provide additional insights into the mechanism of temperature gating of TRPs, an important unsolved question".
References: {1} McKemy et al. Nature 2002, 416:52-8 [PMID:11882888]. {2} Peier et al. Cell 2002, 108:705-15 [PMID:11893340].
References: {1} McKemy et al. Nature 2002, 416:52-8 [PMID:11882888]. {2} Peier et al. Cell 2002, 108:705-15 [PMID:11893340].