메뉴 건너뛰기




Volumn 143, Issue 3, 2014, Pages 361-375

Mutation of I696 and W697 in the TRP box of vanilloid receptor subtype i modulates allosteric channel activation

Author keywords

[No Author keywords available]

Indexed keywords

AGENTS ACTING ON THE PERIPHERAL NERVOUS AND NEUROMUSCULAR SYSTEMS; CAPSAICIN; TRPV1 RECEPTOR; VANILLOID RECEPTOR;

EID: 84894485922     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201311070     Document Type: Article
Times cited : (37)

References (41)
  • 1
    • 0142059776 scopus 로고    scopus 로고
    • Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1)
    • Bhave, G., H.J. Hu, K.S. Glauner, W. Zhu, H. Wang, D.J. Brasier, G.S. Oxford, and R.W. Gereau IV. 2003. Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1). Proc. Natl. Acad. Sci. USA. 100:12480-12485. http://dx.doi.org/10.1073/pnas.2032100100
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 12480-12485
    • Bhave, G.1    Hu, H.J.2    Glauner, K.S.3    Zhu, W.4    Wang, H.5    Brasier, D.J.6    Oxford, G.S.7    Gereau, R.W.8
  • 2
    • 7444240741 scopus 로고    scopus 로고
    • Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8
    • Brauchi, S., P. Orio, and R. Latorre. 2004. Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8. Proc. Natl. Acad. Sci. USA. 101:15494- 15499. http://dx.doi.org/10.1073/pnas.0406773101
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101
    • Brauchi, S.1    Orio, P.2    Latorre, R.3
  • 3
    • 33646899582 scopus 로고    scopus 로고
    • A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels
    • Brauchi, S., G. Orta, M. Salazar, E. Rosenmann, and R. Latorre. 2006. A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels. J. Neurosci. 26:4835-4840. http://dx.doi.org/10.1523/JNEUROSCI.5080-05.2006
    • (2006) J. Neurosci. , vol.26 , pp. 4835-4840
    • Brauchi, S.1    Orta, G.2    Salazar, M.3    Rosenmann, E.4    Latorre, R.5
  • 5
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E., M. Liao, Y. Cheng, and D. Julius. 2013. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature. 504:113-118. http://dx.doi.org/10.1038/nature12823
    • (2013) Nature. , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 6
    • 0034926291 scopus 로고    scopus 로고
    • The vanilloid receptor: a molecular gateway to the pain pathway
    • Caterina, M.J., and D. Julius. 2001. The vanilloid receptor: a molecular gateway to the pain pathway. Annu. Rev. Neurosci. 24:487-517. http://dx.doi.org/10.1146/annurev.neuro.24.1.487
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 487-517
    • Caterina, M.J.1    Julius, D.2
  • 7
    • 84872226412 scopus 로고    scopus 로고
    • Free-energy relationships in ion channels activated by voltage and ligand
    • Chowdhury, S., and B. Chanda. 2013. Free-energy relationships in ion channels activated by voltage and ligand. J. Gen. Physiol. 141:11-28. http://dx.doi.org/10.1085/jgp.201210860
    • (2013) J. Gen. Physiol. , vol.141 , pp. 11-28
    • Chowdhury, S.1    Chanda, B.2
  • 8
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham, D.E. 2003. TRP channels as cellular sensors. Nature. 426:517-524. http://dx.doi.org/10.1038/nature02196
    • (2003) Nature. , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 9
    • 83755207202 scopus 로고    scopus 로고
    • A thermodynamic framework for understanding temperature sensing by transient receptor potential (TRP) channels
    • Clapham, D.E., and C. Miller. 2011. A thermodynamic framework for understanding temperature sensing by transient receptor potential (TRP) channels. Proc. Natl. Acad. Sci. USA. 108:19492-19497. http://dx.doi.org/10.1073/pnas.1117485108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 19492-19497
    • Clapham, D.E.1    Miller, C.2
  • 10
    • 33846491396 scopus 로고    scopus 로고
    • Regulation of TRP channels by N-linked glycosylation
    • Cohen, D.M. 2006. Regulation of TRP channels by N-linked glycosylation. Semin. Cell Dev. Biol. 17:630-637. http://dx.doi.org/ 10.1016/j.semcdb.2006.11.007
    • (2006) Semin. Cell Dev. Biol. , vol.17 , pp. 630-637
    • Cohen, D.M.1
  • 11
    • 53849108437 scopus 로고    scopus 로고
    • Molecular modeling of the full-length human TRPV1 channel in closed and desensitized states
    • Fernández-Ballester, G., and A. Ferrer-Montiel. 2008. Molecular modeling of the full-length human TRPV1 channel in closed and desensitized states. J. Membr. Biol. 223:161-172. http://dx.doi.org/ 10.1007/s00232-008-9123-7
    • (2008) J. Membr. Biol. , vol.223 , pp. 161-172
    • Fernández-Ballester, G.1    Ferrer-Montiel, A.2
  • 14
    • 77952886805 scopus 로고    scopus 로고
    • Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain
    • Grandl, J., S.E. Kim, V. Uzzell, B. Bursulaya, M. Petrus, M. Bandell, and A. Patapoutian. 2010. Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain. Nat. Neurosci. 13:708-714. http://dx.doi.org/10.1038/nn.2552
    • (2010) Nat. Neurosci. , vol.13 , pp. 708-714
    • Grandl, J.1    Kim, S.E.2    Uzzell, V.3    Bursulaya, B.4    Petrus, M.5    Bandell, M.6    Patapoutian, A.7
  • 15
    • 0036714915 scopus 로고    scopus 로고
    • Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels
    • Horrigan, F.T., and R.W. Aldrich. 2002. Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels. J. Gen. Physiol. 120:267- 305. http://dx.doi.org/10.1085/jgp.20028605
    • (2002) J. Gen. Physiol. , vol.120
    • Horrigan, F.T.1    Aldrich, R.W.2
  • 16
    • 84878130527 scopus 로고    scopus 로고
    • The role of allosteric coupling on thermal activation of thermo-TRP channels
    • Jara-Oseguera, A., and L.D. Islas. 2013. The role of allosteric coupling on thermal activation of thermo-TRP channels. Biophys. J. 104:2160-2169. http://dx.doi.org/10.1016/j.bpj.2013.03.055
    • (2013) Biophys. J. , vol.104 , pp. 2160-2169
    • Jara-Oseguera, A.1    Islas, L.D.2
  • 17
    • 1342346561 scopus 로고    scopus 로고
    • Phosphorylation of Vanilloid Receptor 1 by Ca2+/Calmodulin-Dependent Kinase II Regulates Its Vanilloid Binding
    • Jung, J., J.S. Shin, S.Y. Lee, S.W. Hwang, J. Koo, H. Cho, and U. Oh. 2004. Phosphorylation of Vanilloid Receptor 1 by Ca2+/Calmodulin-Dependent Kinase II Regulates Its Vanilloid Binding. J. Biol. Chem. 279:7048-7054. http://dx.doi.org/10.1074/jbc.M311448200
    • (2004) J. Biol. Chem. , vol.279 , pp. 7048-7054
    • Jung, J.1    Shin, J.S.2    Lee, S.Y.3    Hwang, S.W.4    Koo, J.5    Cho, H.6    Oh, U.7
  • 18
    • 59649096789 scopus 로고    scopus 로고
    • Kv Channel Gating Requires a Compatible S4-S5 Linker and Bottom Part of S6, Constrained by Non-interacting Residues
    • Labro, A.J., A.L. Raes, A. Grottesi, D. Van Hoorick, M.S. Sansom, and D.J. Snyders. 2008. Kv Channel Gating Requires a Compatible S4-S5 Linker and Bottom Part of S6, Constrained by Non-interacting Residues. J. Gen. Physiol. 132:667-680. http://dx.doi.org/10.1085/jgp.200810048
    • (2008) J. Gen. Physiol. , vol.132 , pp. 667-680
    • Labro, A.J.1    Raes, A.L.2    Grottesi, A.3    Van Hoorick, D.4    Sansom, M.S.5    Snyders, D.J.6
  • 19
    • 78650959213 scopus 로고    scopus 로고
    • The S4-S5 linker of KCNQ1 channels forms a structural scaffold with the S6 segment controlling gate closure
    • Labro, A.J., I.R. Boulet, F.S. Choveau, E. Mayeur, T. Bruyns, G. Loussouarn, A.L. Raes, and D.J. Snyders. 2011. The S4-S5 linker of KCNQ1 channels forms a structural scaffold with the S6 segment controlling gate closure. J. Biol. Chem. 286:717-725. http:// dx.doi.org/10.1074/jbc.M110.146977
    • (2011) J. Biol. Chem. , vol.286 , pp. 717-725
    • Labro, A.J.1    Boulet, I.R.2    Choveau, F.S.3    Mayeur, E.4    Bruyns, T.5    Loussouarn, G.6    Raes, A.L.7    Snyders, D.J.8
  • 20
    • 34547953765 scopus 로고    scopus 로고
    • ThermoTRP channels as modular proteins with allosteric gating
    • Latorre, R., S. Brauchi, G. Orta, C. Zaelzer, and G. Vargas. 2007. ThermoTRP channels as modular proteins with allosteric gating. Cell Calcium. 42:427-438. http://dx.doi.org/10.1016/j.ceca.2007.04.004
    • (2007) Cell Calcium. , vol.42 , pp. 427-438
    • Latorre, R.1    Brauchi, S.2    Orta, G.3    Zaelzer, C.4    Vargas, G.5
  • 21
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., E. Cao, D. Julius, and Y. Cheng. 2013. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature. 504:107-112. http://dx.doi.org/10.1038/nature12822
    • (2013) Nature. , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 22
    • 84863251177 scopus 로고    scopus 로고
    • Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted syndrome
    • Lin, Z., Q. Chen, M. Lee, X. Cao, J. Zhang, D. Ma, L. Chen, X. Hu, H. Wang, X. Wang, et al. 2012. Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted syndrome. Am. J. Hum. Genet. 90:558-564. http://dx.doi.org/10.1016/j.ajhg.2012.02.006
    • (2012) Am. J. Hum. Genet. , vol.90 , pp. 558-564
    • Lin, Z.1    Chen, Q.2    Lee, M.3    Cao, X.4    Zhang, J.5    Ma, D.6    Chen, L.7    Hu, X.8    Wang, H.9    Wang, X.10
  • 23
    • 33744534577 scopus 로고    scopus 로고
    • Increased sensitivity of desensitized TRPV1 by PMA occurs through PKCepsilonmediated phosphorylation at S800
    • Mandadi, S., T. Tominaga, M. Numazaki, N. Murayama, N. Saito, P.J. Armati, B.D. Roufogalis, and M. Tominaga. 2006. Increased sensitivity of desensitized TRPV1 by PMA occurs through PKCepsilonmediated phosphorylation at S800. Pain. 123:106-116. http:// dx.doi.org/10.1016/j.pain.2006.02.016
    • (2006) Pain. , vol.123 , pp. 106-116
    • Mandadi, S.1    Tominaga, T.2    Numazaki, M.3    Murayama, N.4    Saito, N.5    Armati, P.J.6    Roufogalis, B.D.7    Tominaga, M.8
  • 24
    • 36649016621 scopus 로고    scopus 로고
    • Voltage is a partial activator of rat thermosensitive TRP channels
    • Matta, J.A., and G.P. Ahern. 2007. Voltage is a partial activator of rat thermosensitive TRP channels. J. Physiol. 585:469-482. http://dx.doi.org/10.1113/jphysiol.2007.144287
    • (2007) J. Physiol. , vol.585 , pp. 469-482
    • Matta, J.A.1    Ahern, G.P.2
  • 25
    • 79952683619 scopus 로고    scopus 로고
    • The transient receptor potential family of ion channels
    • Nilius, B., and G. Owsianik. 2011. The transient receptor potential family of ion channels. Genome Biol. 12:218. http://dx.doi.org/10.1186/gb-2011-12-3-218
    • (2011) Genome Biol. , vol.12 , pp. 218
    • Nilius, B.1    Owsianik, G.2
  • 26
  • 27
    • 33846913452 scopus 로고    scopus 로고
    • Capsaicin receptor: TRPV1 a promiscuous TRP channel
    • Pingle, S.C., J.A. Matta, and G.P. Ahern. 2007. Capsaicin receptor: TRPV1 a promiscuous TRP channel. Handbook Exp. Pharmacol. 179:155-171. http://dx.doi.org/10.1007/978-3-540-34891-7_9
    • (2007) Handbook Exp. Pharmacol. , vol.179 , pp. 155-171
    • Pingle, S.C.1    Matta, J.A.2    Ahern, G.P.3
  • 28
    • 0034700494 scopus 로고    scopus 로고
    • Induction of vanilloid receptor channel activity by protein kinase C
    • Premkumar, L.S., and G.P. Ahern. 2000. Induction of vanilloid receptor channel activity by protein kinase C. Nature. 408:985-990. http://dx.doi.org/10.1038/35050121
    • (2000) Nature. , vol.408 , pp. 985-990
    • Premkumar, L.S.1    Ahern, G.P.2
  • 29
    • 77956807049 scopus 로고    scopus 로고
    • Modulation of single-channel properties of TRPV1 by phosphorylation
    • Studer, M., and P.A. McNaughton. 2010. Modulation of single-channel properties of TRPV1 by phosphorylation. J. Physiol. 588:3743- 3756. http://dx.doi.org/10.1113/jphysiol.2010.190611
    • (2010) J. Physiol. , vol.588
    • Studer, M.1    McNaughton, P.A.2
  • 30
    • 79953218015 scopus 로고    scopus 로고
    • Localization of the PIP2 sensor of TRPV1 ion channels
    • Ufret-Vincenty, C.A., R.M. Klein, L. Hua, J. Angueyra, and S.E. Gordon. 2011. Localization of the PIP2 sensor of TRPV1 ion channels. J. Biol. Chem. 286:9688-9698. http://dx.doi.org/10.1074/ jbc.M110.192526
    • (2011) J. Biol. Chem. , vol.286 , pp. 9688-9698
    • Ufret-Vincenty, C.A.1    Klein, R.M.2    Hua, L.3    Angueyra, J.4    Gordon, S.E.5
  • 33
    • 34548632601 scopus 로고    scopus 로고
    • TRP channels
    • Venkatachalam, K., and C. Montell. 2007. TRP channels. Annu. Rev. Biochem. 76:387-417. http://dx.doi.org/10.1146/annurev.biochem.75.103004.142819
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 387-417
    • Venkatachalam, K.1    Montell, C.2
  • 34
    • 84862845558 scopus 로고    scopus 로고
    • Quantifying and modeling the temperature-dependent gating of TRP channels
    • Voets, T. 2012. Quantifying and modeling the temperature-dependent gating of TRP channels. Rev. Physiol. Biochem. Pharmacol. 162:91-119.
    • (2012) Rev. Physiol. Biochem. Pharmacol. , vol.162 , pp. 91-119
    • Voets, T.1
  • 35
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold-and heat-sensitive TRP channels
    • Voets, T., G. Droogmans, U. Wissenbach, A. Janssens, V. Flockerzi, and B. Nilius. 2004. The principle of temperature-dependent gating in cold-and heat-sensitive TRP channels. Nature. 430:748- 754. http://dx.doi.org/10.1038/nature02732
    • (2004) Nature. , vol.430
    • Voets, T.1    Droogmans, G.2    Wissenbach, U.3    Janssens, A.4    Flockerzi, V.5    Nilius, B.6
  • 36
    • 84879075593 scopus 로고    scopus 로고
    • Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel-an overview of the current mutational data
    • Winter, Z., A. Buhala, F. Ötvös, K. Jósvay, C. Vizler, G. Dombi, G. Szakonyi, and Z. Oláh. 2013. Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel-an overview of the current mutational data. Mol. Pain. 9:30. http://dx.doi.org/10.1186/1744-8069-9-30
    • (2013) Mol. Pain. , vol.9 , pp. 30
    • Winter, Z.1    Buhala, A.2    Ötvös, F.3    Jósvay, K.4    Vizler, C.5    Dombi, G.6    Szakonyi, G.7    Oláh, Z.8
  • 37
    • 21344439776 scopus 로고    scopus 로고
    • Characterization of rat transient receptor potential vanilloid 1 receptors lacking the N-glycosylation site N604
    • Wirkner, K., H. Hognestad, R. Jahnel, F. Hucho, and P. Illes. 2005. Characterization of rat transient receptor potential vanilloid 1 receptors lacking the N-glycosylation site N604. Neuroreport. 16:997- 1001. http://dx.doi.org/10.1097/00001756-200506210-00023
    • (2005) Neuroreport. , vol.16
    • Wirkner, K.1    Hognestad, H.2    Jahnel, R.3    Hucho, F.4    Illes, P.5
  • 39
    • 77951035804 scopus 로고    scopus 로고
    • Thermosensitive TRP channel pore turret is part of the temperature activation pathway
    • Yang, F., Y. Cui, K. Wang, and J. Zheng. 2010. Thermosensitive TRP channel pore turret is part of the temperature activation pathway. Proc. Natl. Acad. Sci. USA. 107:7083-7088. http://dx.doi.org/ 10.1073/pnas.1000357107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 7083-7088
    • Yang, F.1    Cui, Y.2    Wang, K.3    Zheng, J.4
  • 40
    • 77955667059 scopus 로고    scopus 로고
    • Kinetic and energetic analysis of thermally activated TRPV1 channels
    • Yao, J., B. Liu, and F. Qin. 2010a. Kinetic and energetic analysis of thermally activated TRPV1 channels. Biophys. J. 99:1743-1753. http://dx.doi.org/10.1016/j.bpj.2010.07.022
    • (2010) Biophys. J. , vol.99 , pp. 1743-1753
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 41
    • 77956295112 scopus 로고    scopus 로고
    • Pore turret of thermal TRP channels is not essential for temperature sensing
    • Yao, J., B. Liu, and F. Qin. 2010b. Pore turret of thermal TRP channels is not essential for temperature sensing. Proc. Natl. Acad. Sci. USA. 107:E125. http://dx.doi.org/10.1073/pnas.1008272107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107
    • Yao, J.1    Liu, B.2    Qin, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.