메뉴 건너뛰기




Volumn 16, Issue 7, 2009, Pages 704-710

Structural determinants of gating in the TRPV1 channel

Author keywords

[No Author keywords available]

Indexed keywords

CAPSAICIN; CYSTEINE; MUTANT PROTEIN; VANILLOID RECEPTOR 1;

EID: 67650330293     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1633     Document Type: Article
Times cited : (96)

References (50)
  • 2
    • 0034693266 scopus 로고    scopus 로고
    • Identification of an aspartic residue in the P-loop of the vanilloid receptor that modulates pore properties
    • García-Martínez, C., Morenilla-Palao, C., Planells-Cases, R., Merino, J.M. & Ferrer-Montiel, A. Identification of an aspartic residue in the P-loop of the vanilloid receptor that modulates pore properties. J. Biol. Chem. 275, 32552-32558 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 32552-32558
    • García-Martínez, C.1    Morenilla-Palao, C.2    Planells-Cases, R.3    Merino, J.M.4    Ferrer-Montiel, A.5
  • 3
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • Montell, C. The TRP superfamily of cation channels. Sci. STKE 2005, re3 (2005).
    • (2005) Sci. STKE , vol.2005
    • Montell, C.1
  • 4
    • 39749169006 scopus 로고    scopus 로고
    • A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic
    • Salazar, H. et al. A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. Nat. Neurosci. 11, 255-261 (2008).
    • (2008) Nat. Neurosci , vol.11 , pp. 255-261
    • Salazar, H.1
  • 5
    • 20144371097 scopus 로고    scopus 로고
    • The pungency of garlic: Activation of TRPA1 and TRPV1 in response to allicin
    • Macpherson, L.J. et al. The pungency of garlic: activation of TRPA1 and TRPV1 in response to allicin. Curr. Biol. 15, 929-934 (2005).
    • (2005) Curr. Biol , vol.15 , pp. 929-934
    • Macpherson, L.J.1
  • 6
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham, D.E. TRP channels as cellular sensors. Nature 426, 517-524 (2003).
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 7
    • 0038274530 scopus 로고    scopus 로고
    • Thermosensation, hot findings make TRPNs very cool
    • Montell, C. Thermosensation, hot findings make TRPNs very cool. Curr. Biol. 13, 476-478 (2003).
    • (2003) Curr. Biol , vol.13 , pp. 476-478
    • Montell, C.1
  • 8
    • 0034926291 scopus 로고    scopus 로고
    • The vanilloid receptor: A molecular gateway to the pain pathway
    • Caterina, M.J. & Julius, D. The vanilloid receptor: a molecular gateway to the pain pathway. Annu. Rev. Neurosci. 24, 487-517 (2001).
    • (2001) Annu. Rev. Neurosci , vol.24 , pp. 487-517
    • Caterina, M.J.1    Julius, D.2
  • 9
    • 0035855860 scopus 로고    scopus 로고
    • Molecular mechanisms of nociception
    • Julius, D. & Basbaum, A.I. Molecular mechanisms of nociception. Nature 413, 203-210 (2001).
    • (2001) Nature , vol.413 , pp. 203-210
    • Julius, D.1    Basbaum, A.I.2
  • 10
    • 33747235382 scopus 로고    scopus 로고
    • Inflammatory pain: The cellular basis of heat hyperalgesia
    • Huang, J., Zhang, X. & McNaughton, P.A. Inflammatory pain: the cellular basis of heat hyperalgesia. Curr. Neuropharmacol. 4, 197-206 (2006).
    • (2006) Curr. Neuropharmacol , vol.4 , pp. 197-206
    • Huang, J.1    Zhang, X.2    McNaughton, P.A.3
  • 12
    • 34248138496 scopus 로고    scopus 로고
    • The vanilloid receptor TRPV1: 10 years from channel cloning to antagonist proof-of-concept
    • Szallasi, A., Cortright, D.N., Blum, C.A. & Eid, S.R. The vanilloid receptor TRPV1: 10 years from channel cloning to antagonist proof-of-concept. Nat. Rev. Drug Discov. 6, 357-372 (2007).
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 357-372
    • Szallasi, A.1    Cortright, D.N.2    Blum, C.A.3    Eid, S.R.4
  • 13
    • 42349109026 scopus 로고    scopus 로고
    • A primer on ankyrin repeat function in TRP channels and beyond
    • Gaudet, R. A primer on ankyrin repeat function in TRP channels and beyond. Mol. Biosyst. 4, 372-379 (2008).
    • (2008) Mol. Biosyst , vol.4 , pp. 372-379
    • Gaudet, R.1
  • 14
    • 34250190946 scopus 로고    scopus 로고
    • The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity
    • Lishko, P.V., Procko, E., Jin, X., Phelps, C.B. & Gaudet, R. The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54, 905-918 (2007).
    • (2007) Neuron , vol.54 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 16
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel
    • Jin, X., Touhey, J. & Gaudet, R. Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. 281, 25006-25010 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 18
    • 59449083489 scopus 로고    scopus 로고
    • Properties of the inner pore region of TRPV1 channels revealed by block with quaternary ammoniums
    • Jara-Oseguera, A., Llorente, I., Rosenbaum, T. & Islas, L.D. Properties of the inner pore region of TRPV1 channels revealed by block with quaternary ammoniums. J. Gen. Physiol. 132, 547-562 (2008).
    • (2008) J. Gen. Physiol , vol.132 , pp. 547-562
    • Jara-Oseguera, A.1    Llorente, I.2    Rosenbaum, T.3    Islas, L.D.4
  • 19
    • 1342325396 scopus 로고    scopus 로고
    • Outer pore topology of the ECaC-TRPV5 channel by cysteine scan mutagenesis
    • Dodier, Y. et al. Outer pore topology of the ECaC-TRPV5 channel by cysteine scan mutagenesis. J. Biol. Chem. 279, 6853-6862 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 6853-6862
    • Dodier, Y.1
  • 20
    • 0029860763 scopus 로고    scopus 로고
    • On the use of thiol-modifying agents to determine channel topology
    • Holmgren, M., Liu, Y., Xu, Y. & Yellen, G. On the use of thiol-modifying agents to determine channel topology. Neuropharmacology 35, 797-804 (1996).
    • (1996) Neuropharmacology , vol.35 , pp. 797-804
    • Holmgren, M.1    Liu, Y.2    Xu, Y.3    Yellen, G.4
  • 23
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • Lu, Q. & Miller, C. Silver as a probe of pore-forming residues in a potassium channel. Science 268, 304-307 (1995).
    • (1995) Science , vol.268 , pp. 304-307
    • Lu, Q.1    Miller, C.2
  • 24
    • 0026489631 scopus 로고
    • Thermal motions of surface α-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping
    • Careaga, C.L. & Falke, J.J. Thermal motions of surface α-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226, 1219-1235 (1992).
    • (1992) J. Mol. Biol , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 25
    • 0014284027 scopus 로고
    • Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex
    • Kobashi, K. Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex. Biochim. Biophys. Acta 158, 239-245 (1968).
    • (1968) Biochim. Biophys. Acta , vol.158 , pp. 239-245
    • Kobashi, K.1
  • 26
    • 34547953765 scopus 로고    scopus 로고
    • ThermoTRP channels as modular proteins with allosteric gating
    • Latorre, R., Brauchi, S., Orta, G., Zaelzer, C. & Vargas, G. ThermoTRP channels as modular proteins with allosteric gating. Cell Calcium 42, 427-438 (2007).
    • (2007) Cell Calcium , vol.42 , pp. 427-438
    • Latorre, R.1    Brauchi, S.2    Orta, G.3    Zaelzer, C.4    Vargas, G.5
  • 28
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280, 69-77 (1998).
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 29
    • 0141817701 scopus 로고    scopus 로고
    • The discovery of the α-helix and β-sheet, the principal structural features of proteins
    • Eisenberg, D. The discovery of the α-helix and β-sheet, the principal structural features of proteins. Proc. Natl. Acad. Sci. USA 100, 11207-11210 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11207-11210
    • Eisenberg, D.1
  • 30
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L. et al. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195, 659-685 (1987).
    • (1987) J. Mol. Biol , vol.195 , pp. 659-685
    • Cornette, J.L.1
  • 31
    • 0024157070 scopus 로고    scopus 로고
    • Komiya, H., Yeates, T.O., Rees, D.C., Allen, J.P. & Feher, G. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species. Proc. Natl. Acad. Sci. USA 85, 9012-9016 (1988).
    • Komiya, H., Yeates, T.O., Rees, D.C., Allen, J.P. & Feher, G. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species. Proc. Natl. Acad. Sci. USA 85, 9012-9016 (1988).
  • 32
    • 34247528609 scopus 로고    scopus 로고
    • TRP channel knockout mice lose their cool
    • Chung, M.K. & Caterina, M.J. TRP channel knockout mice lose their cool. Neuron 54, 345-347 (2007).
    • (2007) Neuron , vol.54 , pp. 345-347
    • Chung, M.K.1    Caterina, M.J.2
  • 33
    • 24344432708 scopus 로고    scopus 로고
    • Investigating the putative glycine hinge in Shaker potassium channel
    • Ding, S., Ingleby, L., Ahern, C.A. & Horn, R. Investigating the putative glycine hinge in Shaker potassium channel. J. Gen. Physiol. 126, 213-226 (2005).
    • (2005) J. Gen. Physiol , vol.126 , pp. 213-226
    • Ding, S.1    Ingleby, L.2    Ahern, C.A.3    Horn, R.4
  • 34
    • 42149189419 scopus 로고    scopus 로고
    • Gating at the selectivity filter in cyclic nucleotide-gated channels
    • Contreras, J.E., Srikumar, D. & Holmgren, M. Gating at the selectivity filter in cyclic nucleotide-gated channels. Proc. Natl. Acad. Sci. USA 105, 3310-3314 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3310-3314
    • Contreras, J.E.1    Srikumar, D.2    Holmgren, M.3
  • 35
    • 0037904401 scopus 로고    scopus 로고
    • A cysteine scan of the inner vestibule of cyclic nucleotidegated channels reveals architecture and rearrangement of the pore
    • Flynn, G.E. & Zagotta, W.N. A cysteine scan of the inner vestibule of cyclic nucleotidegated channels reveals architecture and rearrangement of the pore. J. Gen. Physiol. 121, 563-582 (2003).
    • (2003) J. Gen. Physiol , vol.121 , pp. 563-582
    • Flynn, G.E.1    Zagotta, W.N.2
  • 37
    • 34447515681 scopus 로고    scopus 로고
    • Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1)
    • Susankova, K., Ettrich, R., Vyklicky, L., Teisinger, J. & Vlachova, V. Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1). J. Neurosci. 27, 7578-7585 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 7578-7585
    • Susankova, K.1    Ettrich, R.2    Vyklicky, L.3    Teisinger, J.4    Vlachova, V.5
  • 39
    • 0038721194 scopus 로고    scopus 로고
    • A tyrosine residue in TM6 of the vanilloid receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents
    • Mohapatra, D.P., Wang, S.Y., Wang, G.K. & Nau, C. A tyrosine residue in TM6 of the vanilloid receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents. Mol. Cell. Neurosci. 23, 314-324 (2003).
    • (2003) Mol. Cell. Neurosci , vol.23 , pp. 314-324
    • Mohapatra, D.P.1    Wang, S.Y.2    Wang, G.K.3    Nau, C.4
  • 42
    • 50249186498 scopus 로고    scopus 로고
    • Pore region of TRPV3 ion channel is specifically required for heat activation
    • Grandl, J. et al. Pore region of TRPV3 ion channel is specifically required for heat activation. Nat. Neurosci. 11, 1007-1013 (2008).
    • (2008) Nat. Neurosci , vol.11 , pp. 1007-1013
    • Grandl, J.1
  • 43
    • 7444240741 scopus 로고    scopus 로고
    • Clues to understanding cold sensation: Thermodynamics and electrophysiological analysis of the cold receptor TRPM8
    • Brauchi, S., Orio, P. & Latorre, R. Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8. Proc. Natl. Acad. Sci. USA 101, 15494-15499 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15494-15499
    • Brauchi, S.1    Orio, P.2    Latorre, R.3
  • 44
    • 25144442315 scopus 로고    scopus 로고
    • Conformational changes of pore helix coupled to gating of TRPV5 by protons
    • Yeh, B.I., Kim, Y.K., Jabbar, W. & Huang, C.L. Conformational changes of pore helix coupled to gating of TRPV5 by protons. EMBO J. 24, 3224-3234 (2005).
    • (2005) EMBO J , vol.24 , pp. 3224-3234
    • Yeh, B.I.1    Kim, Y.K.2    Jabbar, W.3    Huang, C.L.4
  • 46
    • 0030818830 scopus 로고    scopus 로고
    • Selectivity changes during activation of mutant Shaker potassium channels
    • Zheng, J. & Sigworth, F.J. Selectivity changes during activation of mutant Shaker potassium channels. J. Gen. Physiol. 110, 101-117 (1997).
    • (1997) J. Gen. Physiol , vol.110 , pp. 101-117
    • Zheng, J.1    Sigworth, F.J.2
  • 47
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D.M., Cuello, L.G. & Perozo, E. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117, 165-180 (2001).
    • (2001) J. Gen. Physiol , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 48
    • 34547200183 scopus 로고    scopus 로고
    • Dissection of the components for PIP2 activation and thermosensation in TRP channels
    • Brauchi, S. et al. Dissection of the components for PIP2 activation and thermosensation in TRP channels. Proc. Natl. Acad. Sci. USA 104, 10246-10251 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10246-10251
    • Brauchi, S.1
  • 49
    • 0037186092 scopus 로고    scopus 로고
    • Dissecting intersubunit contacts in cyclic nucleotidegated ion channels
    • Rosenbaum, T. & Gordon, S.E. Dissecting intersubunit contacts in cyclic nucleotidegated ion channels. Neuron 33, 703-713 (2002).
    • (2002) Neuron , vol.33 , pp. 703-713
    • Rosenbaum, T.1    Gordon, S.E.2
  • 50
    • 0035023528 scopus 로고    scopus 로고
    • Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels
    • Li-Smerin, Y. & Swartz, K.J. Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels. J. Gen. Physiol. 117, 205-218 (2001).
    • (2001) J. Gen. Physiol , vol.117 , pp. 205-218
    • Li-Smerin, Y.1    Swartz, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.