Spicy science: David Julius and the discovery of temperature-sensitive TRP channels
نویسنده
چکیده
This invited biographical review covers the career of Dr. David Julius and his discovery of thermosensitive TRP channels. Dr. Julius is currently the Morris Herzstein Chair in Molecular Biology and Medicine and Professor and Chair of Physiology at the University of California, San Francisco Medical School. He is a member of the National Academy of Sciences and has received many distinguished awards for his landmark discoveries of the molecular basis of pain and thermosensation.
منابع مشابه
International Union of Pharmacology. XLIII. Compendium of voltage-gated ion channels: transient receptor potential channels.
The transient receptor potential (TRP) proteins are six transmembrane-containing subunits that combine to form cation-selective ion channels. TRP channels are present in yeast, Drosophila, Caenorhabditis elegans, and mammals. They are widely distributed and sense local changes in stimuli ranging from light to temperature and osmolarity. Mammals contain at least 22 distinct genes encoding these ...
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Sensory neurons report a wide range of temperatures, from noxious heat to noxious cold. Natural products that elicit psychophysical sensations of hot or cold, such as capsaicin or menthol, were instrumental in the discovery of thermal detectors belonging to the transient receptor potential (TRP) family of cation channels. Studies are now beginning to reveal how these channels contribute to ther...
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2017 marks the 20th anniversary of the molecular cloning by David Julius and colleagues (1997) of the long sought-after capsaicin receptor, now known as TRPV1 (Transient Receptor Potential Vanilloid 1) [1]. This seminal discovery has opened up a "hot" new field of basic research and launched drug discovery efforts into the large family (by the latest count 28 mammalian members, 27 in humans) of...
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Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be uniquely sensitive to heat, which has been presumed to be due to the existence of an unidentified temperature-sensing domain. Here we report that the homologous voltage-gated potassium (Kv) channels also exhibit high temperature sensitivi...
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