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Volumn 108, Issue 49, 2011, Pages 19492-19497

A thermodynamic framework for understanding temperature sensing by transient receptor potential (TRP) channels

Author keywords

Hydrophobic interaction; TRPC5; TRPM8; TRPV

Indexed keywords

TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 83755207202     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1117485108     Document Type: Article
Times cited : (198)

References (48)
  • 2
    • 33846807748 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in disease
    • DOI 10.1152/physrev.00021.2006
    • Nilius B, Owsianik G, Voets T, Peters JA (2007) Transient receptor potential cation channels in disease. Physiol Rev 87:165-217. (Pubitemid 46207713)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 165-217
    • Nilius, B.1    Owsianik, G.2    Voets, T.3    Peters, J.A.4
  • 3
    • 77956272001 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family
    • Wu LJ, Sweet TB, Clapham DE (2010) International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family. Pharmacol Rev 62:381-404.
    • (2010) Pharmacol Rev , vol.62 , pp. 381-404
    • Wu, L.J.1    Sweet, T.B.2    Clapham, D.E.3
  • 4
    • 0033119629 scopus 로고    scopus 로고
    • A capsaicin-receptor homologue with a high threshold for noxious heat
    • DOI 10.1038/18906
    • Caterina MJ, Rosen TA, Tominaga M, Brake AJ, Julius D (1999) A capsaicin-receptor homologue with a high threshold for noxious heat. Nature 398:436-441. (Pubitemid 29180377)
    • (1999) Nature , vol.398 , Issue.6726 , pp. 436-441
    • Caterina, M.J.1    Rosen, T.A.2    Tominaga, M.3    Brake, A.J.4    Julius, D.5
  • 5
    • 41749117999 scopus 로고    scopus 로고
    • Pharmacological blockade of the vanilloid receptor TRPV1 elicits marked hyperthermia in humans
    • Gavva NR, et al. (2008) Pharmacological blockade of the vanilloid receptor TRPV1 elicits marked hyperthermia in humans. Pain 136:202-210.
    • (2008) Pain , vol.136 , pp. 202-210
    • Gavva, N.R.1
  • 6
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation
    • DOI 10.1038/nature719
    • McKemy DD, Neuhausser WM, Julius D (2002) Identification of a cold receptor reveals a general role for TRP channels in thermosensation. Nature 416:52-58. (Pubitemid 34215395)
    • (2002) Nature , vol.416 , Issue.6876 , pp. 52-58
    • McKemy, D.D.1    Neuhausser, W.M.2    Julius, D.3
  • 8
    • 2942536048 scopus 로고    scopus 로고
    • TRPM8 activation by menthol, icilin, and cold is differentially modulated by intracellular pH
    • DOI 10.1523/JNEUROSCI.0890-04.2004
    • Andersson DA, Chase HW, Bevan S (2004) TRPM8 activation by menthol, icilin, and cold is differentially modulated by intracellular pH. J Neurosci 24:5364-5369. (Pubitemid 38747678)
    • (2004) Journal of Neuroscience , vol.24 , Issue.23 , pp. 5364-5369
    • Andersson, D.A.1    Chase, H.W.N.2    Bevan, S.3
  • 9
    • 0242385383 scopus 로고    scopus 로고
    • Thermodynamics of Heat Activation of Single Capsaicin Ion Channels VR1
    • Liu B, Hui K, Qin F (2003) Thermodynamics of heat activation of single capsaicin ion channels VR1. Biophys J 85:2988-3006. (Pubitemid 37345788)
    • (2003) Biophysical Journal , vol.85 , Issue.5 , pp. 2988-3006
    • Liu, B.1    Hui, K.2    Qin, F.3
  • 10
    • 59049096524 scopus 로고    scopus 로고
    • TRPA1 acts as a cold sensor in vitro and in vivo
    • Karashima Y, et al. (2009) TRPA1 acts as a cold sensor in vitro and in vivo. Proc Natl Acad Sci USA 106:1273-1278.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1273-1278
    • Karashima, Y.1
  • 12
    • 81055141456 scopus 로고    scopus 로고
    • Transient receptor potential cation channel, subfamily C, member 5 (TRPC5) is a cold-transducer in the peripheral nervous system
    • Zimmermann K, et al. (2011) Transient receptor potential cation channel, subfamily C, member 5 (TRPC5) is a cold-transducer in the peripheral nervous system. Proc Natl Acad Sci USA 108:18114-18119.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18114-18119
    • Zimmermann, K.1
  • 14
    • 0037033077 scopus 로고    scopus 로고
    • Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells
    • DOI 10.1074/jbc.M208277200
    • Watanabe H, et al. (2002) Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells. J Biol Chem 277:47044-47051. (Pubitemid 36159212)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 47044-47051
    • Watanabe, H.1    Vriens, J.2    Suh, S.H.3    Benham, C.D.4    Droogmans, G.5    Nilius, B.6
  • 16
    • 77955667059 scopus 로고    scopus 로고
    • Kinetic and energetic analysis of thermally activated TRPV1 channels
    • Yao J, Liu B, Qin F (2010) Kinetic and energetic analysis of thermally activated TRPV1 channels. Biophys J 99:1743-1753.
    • (2010) Biophys J , vol.99 , pp. 1743-1753
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 17
    • 34447132940 scopus 로고    scopus 로고
    • A high-threshold heat-activated channel in cultured rat dorsal root ganglion neurons resembles TRPV2 and is blocked by gadolinium
    • DOI 10.1111/j.1460-9568.2007.05643.x
    • Leffler A, Linte RM, Nau C, Reeh P, Babes A (2007) A high-threshold heat-activated channel in cultured rat dorsal root ganglion neurons resembles TRPV2 and is blocked by gadolinium. Eur J Neurosci 26:12-22. (Pubitemid 47035448)
    • (2007) European Journal of Neuroscience , vol.26 , Issue.1 , pp. 12-22
    • Leffler, A.1    Linte, R.M.2    Nau, C.3    Reeh, P.4    Babes, A.5
  • 18
    • 79960580198 scopus 로고    scopus 로고
    • Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels
    • Yao J, Liu B, Qin F (2011) Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels. Proc Natl Acad Sci USA 108:11109-11114.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11109-11114
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 19
    • 0030775069 scopus 로고    scopus 로고
    • A two-state analysis of co-operative oxygen binding in the three human embryonic haemoglobins
    • Brittain T, Hofmann OM, Watmough NJ, Greenwood C, Weber RE (1997) A two-state analysis of co-operative oxygen binding in the three human embryonic haemoglobins. Biochem J 326:299-303. (Pubitemid 27417201)
    • (1997) Biochemical Journal , vol.326 , Issue.2 , pp. 299-303
    • Brittain, T.1    Hofmann, O.M.2    Watmough, N.J.3    Greenwood, C.4    Weber, R.E.5
  • 20
    • 0030670857 scopus 로고    scopus 로고
    • + channel N- and C-type inactivation
    • DOI 10.1007/s002490050098
    • Meyer R, Heinemann SH (1997) Temperature and pressure dependence of Shaker K+ channel N- and C-type inactivation. Eur Biophys J 26:433-445. (Pubitemid 27509260)
    • (1997) European Biophysics Journal , vol.26 , Issue.6 , pp. 433-445
    • Meyer, R.1    Heinemann, S.H.2
  • 21
    • 33846963817 scopus 로고    scopus 로고
    • A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance
    • DOI 10.1074/jbc.M610075200
    • Fang Y, Kolmakova-Partensky L, Miller C (2007) A bacterial arginine-agmatine exchange transporter involved in extreme acid resistance. J Biol Chem 282:176-182. (Pubitemid 47076634)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.1 , pp. 176-182
    • Fang, Y.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 22
    • 0019872621 scopus 로고
    • Thermodynamics of the binding of D-glucose to yeast hexokinase
    • Takahashi K, Casey JL, Sturtevant JM (1981) Thermodynamics of the binding of D-glucose to yeast hexokinase. Biochemistry 20:4693-4697.
    • (1981) Biochemistry , vol.20 , pp. 4693-4697
    • Takahashi, K.1    Casey, J.L.2    Sturtevant, J.M.3
  • 23
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin RL (1986) Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83:8069-8072.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 24
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W (1959) Some factors in the interpretation of protein denaturation. Adv Prot Chem 14:1-63.
    • (1959) Adv Prot Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 26
    • 0000820095 scopus 로고    scopus 로고
    • Thermodynamics of protein folding
    • Privalov PL (1997) Thermodynamics of protein folding. J Chem Thermo 29:447-474.
    • (1997) J Chem Thermo , vol.29 , pp. 447-474
    • Privalov, P.L.1
  • 27
    • 77249084607 scopus 로고    scopus 로고
    • The hydrophobic effect and its role in cold denaturation
    • Dias CL, et al. (2010) The hydrophobic effect and its role in cold denaturation. Cryobiology 60:91-99.
    • (2010) Cryobiology , vol.60 , pp. 91-99
    • Dias, C.L.1
  • 28
    • 0000616995 scopus 로고
    • Apparent molar heat capacities of amino acids and other organic compounds
    • Edsall JT (1935) Apparent molar heat capacities of amino acids and other organic compounds. J Am Chem Soc 54:1506-1507.
    • (1935) J Am Chem Soc , vol.54 , pp. 1506-1507
    • Edsall, J.T.1
  • 29
    • 0000013706 scopus 로고
    • An equation of state describing hydrophobic interactions
    • Gill SJ, Wadsö I (1976) An equation of state describing hydrophobic interactions. Proc Natl Acad Sci USA 73:2955-2958.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2955-2958
    • Gill, S.J.1    Wadsö, I.2
  • 30
    • 0035909449 scopus 로고    scopus 로고
    • Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines
    • Matulis D (2001) Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines. Biophys Chem 93:67-82.
    • (2001) Biophys Chem , vol.93 , pp. 67-82
    • Matulis, D.1
  • 31
    • 24544464348 scopus 로고
    • Structure of water and hydrophobic bonding in proteins. 1. A model for the thermodynamic properties of liquid water
    • Nemethy G, Scheraga HA (1962) Structure of water and hydrophobic bonding in proteins. 1. A model for the thermodynamic properties of liquid water. J Chem Phys 36:3382-3400.
    • (1962) J Chem Phys , vol.36 , pp. 3382-3400
    • Nemethy, G.1    Scheraga, H.A.2
  • 32
    • 0041624164 scopus 로고    scopus 로고
    • A new angle on heat capacity changes in hydrophobic solvation
    • Gallager KR, Sharp KA (2002) A new angle on heat capacity changes in hydrophobic solvation. J Am Chem Soc 125:9853-9860.
    • (2002) J Am Chem Soc , vol.125 , pp. 9853-9860
    • Gallager, K.R.1    Sharp, K.A.2
  • 33
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel
    • DOI 10.1074/jbc.C600153200
    • Jin X, Touhey J, Gaudet R (2006) Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J Biol Chem 281:25006-25010. (Pubitemid 44401888)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.35 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 34
    • 33748138924 scopus 로고    scopus 로고
    • Crystal structure of the human TRPV2 channel ankyrin repeat domain
    • DOI 10.1110/ps.062357206
    • McCleverty CJ, Koesema E, Patapoutian A, Lesley SA, Kreusch A (2006) Crystal structure of the human TRPV2 channel ankyrin repeat domain. Protein Sci 15:2201-2206. (Pubitemid 44316022)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2201-2206
    • Mccleverty, C.J.1    Koesema, E.2    Patapoutian, A.3    Lesley, S.A.4    Kreusch, A.5
  • 35
    • 39749115631 scopus 로고    scopus 로고
    • Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels
    • DOI 10.1021/bi702109w
    • Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R (2008) Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels. Biochemistry 47:2476-2484. (Pubitemid 351304553)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2476-2484
    • Phelps, C.B.1    Huang, R.J.2    Lishko, P.V.3    Wang, R.R.4    Gaudet, R.5
  • 36
    • 34250190946 scopus 로고    scopus 로고
    • The Ankyrin Repeats of TRPV1 Bind Multiple Ligands and Modulate Channel Sensitivity
    • DOI 10.1016/j.neuron.2007.05.027, PII S0896627307004060
    • Lishko PV, Procko E, Jin X, Phelps CB, Gaudet R (2007) The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54:905-918. (Pubitemid 46907502)
    • (2007) Neuron , vol.54 , Issue.6 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 37
    • 73649104785 scopus 로고    scopus 로고
    • Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain
    • Phelps CB, Wang RR, Choo SS, Gaudet R (2010) Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain. J Biol Chem 285:731-740.
    • (2010) J Biol Chem , vol.285 , pp. 731-740
    • Phelps, C.B.1    Wang, R.R.2    Choo, S.S.3    Gaudet, R.4
  • 38
    • 17844373771 scopus 로고    scopus 로고
    • 2 regulates the activation and desensitization of TRPM8 channels through the TRP domain
    • DOI 10.1038/nn1451
    • Rohács T, Lopes CM, Michailidis I, Logothetis DE (2005) PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain. Nat Neurosci 8:626-634. (Pubitemid 40594204)
    • (2005) Nature Neuroscience , vol.8 , Issue.5 , pp. 626-634
    • Rohacs, T.1    Lopes, C.M.B.2    Michailidis, I.3    Logothetis, D.E.4
  • 39
    • 77449112680 scopus 로고    scopus 로고
    • Structure-functional intimacies of transient receptor potential channels
    • Latorre R, Zaelzer C, Brauchi S (2009) Structure-functional intimacies of transient receptor potential channels. Q Rev Biophys 42:201-246.
    • (2009) Q Rev Biophys , vol.42 , pp. 201-246
    • Latorre, R.1    Zaelzer, C.2    Brauchi, S.3
  • 41
    • 0020608255 scopus 로고
    • A quantitative study of potassium channel kinetics in rat skeletal muscle from 1 to 37 degrees C
    • Beam KG, Donaldson PL (1983) A quantitative study of potassium channel kinetics in rat skeletal muscle from 1 to 37 degrees C. J Gen Physiol 81:485-512. (Pubitemid 13130077)
    • (1983) Journal of General Physiology , vol.81 , Issue.4 , pp. 485-512
    • Beam, K.G.1    Donaldson, P.L.2
  • 42
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels
    • DOI 10.1038/nature02732
    • Voets T, et al. (2004) The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels. Nature 430:748-754. (Pubitemid 39071340)
    • (2004) Nature , vol.430 , Issue.7001 , pp. 748-754
    • Voets, T.1    Droogmans, G.2    Wissenbach, U.3    Janssens, A.4    Flockerzi, V.5    Nilius, B.6
  • 45
    • 77951114632 scopus 로고    scopus 로고
    • Molecular basis of infrared detection by snakes
    • Gracheva EO, et al. (2010) Molecular basis of infrared detection by snakes. Nature 464:1006-1011.
    • (2010) Nature , vol.464 , pp. 1006-1011
    • Gracheva, E.O.1
  • 46
    • 78149485777 scopus 로고    scopus 로고
    • TRPA1 contributes to cold hypersensitivity
    • del Camino D, et al. (2010) TRPA1 contributes to cold hypersensitivity. J Neurosci 30:15165-15174.
    • (2010) J Neurosci , vol.30 , pp. 15165-15174
    • Del Camino, D.1
  • 47
    • 18144421118 scopus 로고    scopus 로고
    • Biphasic currents evoked by chemical or thermal activation of the heat-gated ion channel, TRPV3
    • DOI 10.1074/jbc.M500596200
    • Chung MK, Guler AD, Caterina MJ (2005) Biphasic currents evoked by chemical or thermal activation of the heat-gated ion channel, TRPV3. J Biol Chem 280:15928-15941. (Pubitemid 40616716)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 15928-15941
    • Chung, M.-K.1    Guler, A.D.2    Caterina, M.J.3
  • 48
    • 0036224803 scopus 로고    scopus 로고
    • II phase transition temperature for 1,2-dioleoyl-sn-glycero-3-phosphatidylethanolamine
    • Toombes GE, Finnefrock AC, Tate MW, Gruner SM (2002) Determination of L(alpha)-H(II) phase transition temperature for 1,2-dioleoyl-sn-glycero-3- phosphatidylethanolamine. Biophys J 82:2504-2510. (Pubitemid 34441289)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2504-2510
    • Toombes, G.E.S.1    Finnefrock, A.C.2    Tate, M.W.3    Gruner, S.M.4


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