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  • 1
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    Structural basis for the coupling between activation and inactivation gates in K(+) channels (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-07-09
    Description: The coupled interplay between activation and inactivation gating is a functional hallmark of K(+) channels. This coupling has been experimentally demonstrated through ion interaction effects and cysteine accessibility, and is associated with a well defined boundary of energetically coupled residues. The structure of the K(+) channel KcsA in its fully open conformation, in addition to four other partial channel openings, richly illustrates the structural basis of activation-inactivation gating. Here, we identify the mechanistic principles by which movements on the inner bundle gate trigger conformational changes at the selectivity filter, leading to the non-conductive C-type inactivated state. Analysis of a series of KcsA open structures suggests that, as a consequence of the hinge-bending and rotation of the TM2 helix, the aromatic ring of Phe 103 tilts towards residues Thr 74 and Thr 75 in the pore-helix and towards Ile 100 in the neighbouring subunit. This allows the network of hydrogen bonds among residues Trp 67, Glu 71 and Asp 80 to destabilize the selectivity filter, allowing entry to its non-conductive conformation. Mutations at position 103 have a size-dependent effect on gating kinetics: small side-chain substitutions F103A and F103C severely impair inactivation kinetics, whereas larger side chains such as F103W have more subtle effects. This suggests that the allosteric coupling between the inner helical bundle and the selectivity filter might rely on straightforward mechanical deformation propagated through a network of steric contacts. Average interactions calculated from molecular dynamics simulations show favourable open-state interaction-energies between Phe 103 and the surrounding residues. We probed similar interactions in the Shaker K(+) channel where inactivation was impaired in the mutant I470A. We propose that side-chain rearrangements at position 103 mechanically couple activation and inactivation in KcsA and a variety of other K(+) channels.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3033755/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3033755/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cuello, Luis G -- Jogini, Vishwanath -- Cortes, D Marien -- Pan, Albert C -- Gagnon, Dominique G -- Dalmas, Olivier -- Cordero-Morales, Julio F -- Chakrapani, Sudha -- Roux, Benoit -- Perozo, Eduardo -- R01 GM057846/GM/NIGMS NIH HHS/ -- R01 GM057846-15/GM/NIGMS NIH HHS/ -- R01 GM062342/GM/NIGMS NIH HHS/ -- R01 GM062342-05/GM/NIGMS NIH HHS/ -- R01-GM57846/GM/NIGMS NIH HHS/ -- R01-GM62342/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 Jul 8;466(7303):272-5. doi: 10.1038/nature09136.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, The University of Chicago, 929 E 57th Street, Chicago, Illinois 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20613845" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Cysteine/genetics/metabolism ; Electron Spin Resonance Spectroscopy ; Humans ; Hydrogen Bonding ; *Ion Channel Gating ; Kinetics ; Models, Molecular ; Molecular Dynamics Simulation ; Phenylalanine/metabolism ; Potassium Channels/*chemistry/genetics/*metabolism ; Protein Conformation ; Shaker Superfamily of Potassium Channels/chemistry/genetics/metabolism ; Streptomyces lividans/*chemistry ; Structure-Activity Relationship
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Ganglion-specific splicing of TRPV1 underlies infrared sensation in vampire bats (2011)
    Nature Publishing Group (NPG)
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    Publication Date: 2011-08-05
    Description: Vampire bats (Desmodus rotundus) are obligate blood feeders that have evolved specialized systems to suit their sanguinary lifestyle. Chief among such adaptations is the ability to detect infrared radiation as a means of locating hotspots on warm-blooded prey. Among vertebrates, only vampire bats, boas, pythons and pit vipers are capable of detecting infrared radiation. In each case, infrared signals are detected by trigeminal nerve fibres that innervate specialized pit organs on the animal's face. Thus, vampire bats and snakes have taken thermosensation to the extreme by developing specialized systems for detecting infrared radiation. As such, these creatures provide a window into the molecular and genetic mechanisms underlying evolutionary tuning of thermoreceptors in a species-specific or cell-type-specific manner. Previously, we have shown that snakes co-opt a non-heat-sensitive channel, vertebrate TRPA1 (transient receptor potential cation channel A1), to produce an infrared detector. Here we show that vampire bats tune a channel that is already heat-sensitive, TRPV1, by lowering its thermal activation threshold to about 30 degrees C. This is achieved through alternative splicing of TRPV1 transcripts to produce a channel with a truncated carboxy-terminal cytoplasmic domain. These splicing events occur exclusively in trigeminal ganglia, and not in dorsal root ganglia, thereby maintaining a role for TRPV1 as a detector of noxious heat in somatic afferents. This reflects a unique organization of the bat Trpv1 gene that we show to be characteristic of Laurasiatheria mammals (cows, dogs and moles), supporting a close phylogenetic relationship with bats. These findings reveal a novel molecular mechanism for physiological tuning of thermosensory nerve fibres.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3535012/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3535012/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gracheva, Elena O -- Cordero-Morales, Julio F -- Gonzalez-Carcacia, Jose A -- Ingolia, Nicholas T -- Manno, Carlo -- Aranguren, Carla I -- Weissman, Jonathan S -- Julius, David -- GM080853/GM/NIGMS NIH HHS/ -- NS047723/NS/NINDS NIH HHS/ -- NS055299/NS/NINDS NIH HHS/ -- P01 AG010770/AG/NIA NIH HHS/ -- R01 NS055299/NS/NINDS NIH HHS/ -- R37 NS047723/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Aug 3;476(7358):88-91. doi: 10.1038/nature10245.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, California 94158-2517, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21814281" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing/*genetics ; Amino Acid Sequence ; Animals ; Cattle ; Chiroptera/anatomy & histology/classification/*genetics/*physiology ; Face/anatomy & histology/innervation ; Feeding Behavior/physiology ; HEK293 Cells ; Hot Temperature ; Humans ; *Infrared Rays ; Molecular Sequence Data ; Organ Specificity/genetics ; Phylogeny ; Predatory Behavior/physiology ; Protein Isoforms/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; Sensation/*physiology ; TRPV Cation Channels/chemistry/*genetics/metabolism ; Trigeminal Ganglion/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Molecular basis of infrared detection by snakes (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-03-17
    Description: Snakes possess a unique sensory system for detecting infrared radiation, enabling them to generate a 'thermal image' of predators or prey. Infrared signals are initially received by the pit organ, a highly specialized facial structure that is innervated by nerve fibres of the somatosensory system. How this organ detects and transduces infrared signals into nerve impulses is not known. Here we use an unbiased transcriptional profiling approach to identify TRPA1 channels as infrared receptors on sensory nerve fibres that innervate the pit organ. TRPA1 orthologues from pit-bearing snakes (vipers, pythons and boas) are the most heat-sensitive vertebrate ion channels thus far identified, consistent with their role as primary transducers of infrared stimuli. Thus, snakes detect infrared signals through a mechanism involving radiant heating of the pit organ, rather than photochemical transduction. These findings illustrate the broad evolutionary tuning of transient receptor potential (TRP) channels as thermosensors in the vertebrate nervous system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855400/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855400/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gracheva, Elena O -- Ingolia, Nicholas T -- Kelly, Yvonne M -- Cordero-Morales, Julio F -- Hollopeter, Gunther -- Chesler, Alexander T -- Sanchez, Elda E -- Perez, John C -- Weissman, Jonathan S -- Julius, David -- GM080853/GM/NIGMS NIH HHS/ -- NS047723/NS/NINDS NIH HHS/ -- NS055299/NS/NINDS NIH HHS/ -- P01 AG010770/AG/NIA NIH HHS/ -- P40 RR018300-06/RR/NCRR NIH HHS/ -- R01 NS055299/NS/NINDS NIH HHS/ -- R01 NS055299-04/NS/NINDS NIH HHS/ -- R01 NS055299-04S1/NS/NINDS NIH HHS/ -- R37 NS047723/NS/NINDS NIH HHS/ -- R37 NS047723-18/NS/NINDS NIH HHS/ -- R37 NS047723-19/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2010 Apr 15;464(7291):1006-11. doi: 10.1038/nature08943. Epub 2010 Mar 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, California 94158-2517, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20228791" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Boidae/genetics/metabolism ; Chickens ; Cloning, Molecular ; Crotalus/anatomy & histology/genetics/metabolism/*physiology ; *Hot Temperature ; *Infrared Rays ; Light Signal Transduction/*physiology/*radiation effects ; Molecular Sequence Data ; Predatory Behavior/physiology/radiation effects ; Rats ; Sensory Receptor Cells/metabolism ; Transient Receptor Potential Channels/genetics/*metabolism ; Trigeminal Ganglion/cytology/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Cytoplasmic ankyrin repeats of transient receptor potential A1 (TRPA1) dictate sensitivity to thermal and chemical stimuli (2011)
    National Academy of Sciences
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    Publication Date: 2011-09-19
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 5
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    Cytoplasmic ankyrin repeats of transient receptor potential A1 (TRPA1) dictate sensitivity to thermal and chemical stimuli [Physiology] (2011)
    National Academy of Sciences
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    Publication Date: 2011-11-16
    Description: Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide array of physical and chemical stimuli, making them important components of sensory systems in both vertebrate and invertebrate organisms. Mammalian TRPA1 channels are activated by chemically reactive irritants, whereas snake and Drosophila TRPA1 orthologs are preferentially activated by heat. By comparing human and rattlesnake TRPA1 channels, we have identified two portable heat-sensitive modules within the ankyrin repeat-rich aminoterminal cytoplasmic domain of the snake ortholog. Chimeric channel studies further demonstrate that sensitivity to chemical stimuli and modulation by intracellular calcium also localize to the N-terminal ankyrin repeat-rich domain, identifying this region as an integrator of diverse physiological signals that regulate sensory neuron excitability. These findings provide a framework for understanding how restricted changes in TRPA1 sequence account for evolution of physiologically diverse channels, also identifying portable modules that specify thermosensitivity.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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