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Volumn 6, Issue , 2016, Pages

TRPV1 function is modulated by Cdk5-mediated phosphorylation: Insights into the molecular mechanism of nociception

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CAPSAICIN; CDK5 PROTEIN, MOUSE; CYCLIN DEPENDENT KINASE 5; TRPV1 PROTEIN, MOUSE; VANILLOID RECEPTOR;

EID: 84959101680     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep22007     Document Type: Article
Times cited : (32)

References (36)
  • 1
    • 0032970173 scopus 로고    scopus 로고
    • Vanilloid (Capsaicin) receptors and mechanisms
    • Szallasi, A. & Blumberg, P. M. Vanilloid (Capsaicin) receptors and mechanisms. Pharmacol. Rev. 51, 159-212 (1999).
    • (1999) Pharmacol. Rev. , vol.51 , pp. 159-212
    • Szallasi, A.1    Blumberg, P.M.2
  • 2
    • 0030777012 scopus 로고    scopus 로고
    • The capsaicin receptor: A heat-activated ion channel in the pain pathway
    • Caterina, M. J. et al. The capsaicin receptor: a heat-activated ion channel in the pain pathway. Nature 389, 816-824 (1997).
    • (1997) Nature , vol.389 , pp. 816-824
    • Caterina, M.J.1
  • 4
    • 79952745941 scopus 로고    scopus 로고
    • The biophysical and molecular basis of TRPV1 proton gating
    • Aneiros, E. et al. The biophysical and molecular basis of TRPV1 proton gating. EMBO J. 30, 994-1002 (2011).
    • (2011) EMBO J , vol.30 , pp. 994-1002
    • Aneiros, E.1
  • 5
    • 0033614984 scopus 로고    scopus 로고
    • Vanilloid receptors on sensory nerves mediate the vasodilator action of anandamide
    • Zygmunt, P. M. et al. Vanilloid receptors on sensory nerves mediate the vasodilator action of anandamide. Nature 400, 452-457 (1999).
    • (1999) Nature , vol.400 , pp. 452-457
    • Zygmunt, P.M.1
  • 6
    • 4644320317 scopus 로고    scopus 로고
    • Posttranslational mechanisms of peripheral sensitization
    • Bhave, G. & Gereau, R. W. Posttranslational mechanisms of peripheral sensitization. J. Neurobiol. 61, 88-106 (2004).
    • (2004) J. Neurobiol , vol.61 , pp. 88-106
    • Bhave, G.1    Gereau, R.W.2
  • 7
    • 33847104189 scopus 로고    scopus 로고
    • Inflammatory mediators modulating the transient receptor potential vanilloid 1 receptor: Therapeutic targets to treat inflammatory and neuropathic pain
    • Ma, W. & Quirion, R. Inflammatory mediators modulating the transient receptor potential vanilloid 1 receptor: therapeutic targets to treat inflammatory and neuropathic pain. Expert Opin. Ther. Targets 11, 307-320 (2007).
    • (2007) Expert Opin. Ther. Targets , vol.11 , pp. 307-320
    • Ma, W.1    Quirion, R.2
  • 8
    • 0032529562 scopus 로고    scopus 로고
    • The cAMP transduction cascade mediates the prostaglandin E2 enhancement of the capsaicin-elicited current in rat sensory neurons: Whole-cell and single-channel studies
    • Lopshire, J. C. & Nicol, G. D. The cAMP transduction cascade mediates the prostaglandin E2 enhancement of the capsaicin-elicited current in rat sensory neurons: whole-cell and single-channel studies. J. Neurosci. 18, 6081-6092 (1998).
    • (1998) J. Neurosci , vol.18 , pp. 6081-6092
    • Lopshire, J.C.1    Nicol, G.D.2
  • 9
    • 0034977496 scopus 로고    scopus 로고
    • The vanilloid receptor (VR1)-mediated effects of anandamide are potently enhanced by the cAMP-dependent protein kinase
    • De Petrocellis, L. et al. The vanilloid receptor (VR1)-mediated effects of anandamide are potently enhanced by the cAMP-dependent protein kinase. J. Neurochem. 77, 1660-1663 (2001).
    • (2001) J. Neurochem. , vol.77 , pp. 1660-1663
    • De Petrocellis, L.1
  • 10
    • 33646498289 scopus 로고    scopus 로고
    • Relative roles of protein kinase A and protein kinase C in modulation of transient receptor potential vanilloid type 1 receptor responsiveness in rat sensory neurons in vitro and peripheral nociceptors in vivo
    • Varga, A. et al. Relative roles of protein kinase A and protein kinase C in modulation of transient receptor potential vanilloid type 1 receptor responsiveness in rat sensory neurons in vitro and peripheral nociceptors in vivo. Neuroscience 140, 645-657 (2006).
    • (2006) Neuroscience , vol.140 , pp. 645-657
    • Varga, A.1
  • 11
    • 0033166535 scopus 로고    scopus 로고
    • Specific involvement of PKC-ε in sensitization of the neuronal response to painful heat
    • Cesare, P., Dekker, L. V., Sardini, A., Parker, P. J. & McNaughton, P. A. Specific involvement of PKC-ε in sensitization of the neuronal response to painful heat. Neuron 23, 617-624 (1999).
    • (1999) Neuron , vol.23 , pp. 617-624
    • Cesare, P.1    Dekker, L.V.2    Sardini, A.3    Parker, P.J.4    McNaughton, P.A.5
  • 12
    • 0034700494 scopus 로고    scopus 로고
    • Induction of vanilloid receptor channel activity by protein kinase C
    • Premkumar, L. S. & Ahern, G. P. Induction of vanilloid receptor channel activity by protein kinase C. Nature 408, 985-90 (2000).
    • (2000) Nature , vol.408 , pp. 985-990
    • Premkumar, L.S.1    Ahern, G.P.2
  • 13
    • 0035425705 scopus 로고    scopus 로고
    • Protein kinase C activation potentiates gating of the vanilloid receptor VR1 by capsaicin, protons, heat and anandamide
    • Vellani, V., Mapplebeck, S., Moriondo, A., Davis, J. B. & McNaughton, P. A. Protein kinase C activation potentiates gating of the vanilloid receptor VR1 by capsaicin, protons, heat and anandamide. J. Physiol. 534, 813-825 (2001).
    • (2001) J. Physiol. , vol.534 , pp. 813-825
    • Vellani, V.1    Mapplebeck, S.2    Moriondo, A.3    Davis, J.B.4    McNaughton, P.A.5
  • 14
    • 1342346561 scopus 로고    scopus 로고
    • Phosphorylation of Vanilloid Receptor 1 by Ca 2+/Calmodulin-dependent Kinase II Regulates Its Vanilloid Binding
    • Jung, J. et al. Phosphorylation of Vanilloid Receptor 1 by Ca 2+/Calmodulin-dependent Kinase II Regulates Its Vanilloid Binding. J. Biol. Chem. 279, 7048-7054 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 7048-7054
    • Jung, J.1
  • 15
    • 3242659099 scopus 로고    scopus 로고
    • Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase
    • Jin, X. et al. Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase. Am. J. Physiol. Cell Physiol. 287, C558-C563 (2004).
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287 , pp. C558-C563
    • Jin, X.1
  • 16
    • 0030956114 scopus 로고    scopus 로고
    • The role of calcium in the desensitization of capsaicin responses in rat dorsal root ganglion neurons
    • Koplas, P. A., Rosenberg, R. L. & Oxford, G. S. The role of calcium in the desensitization of capsaicin responses in rat dorsal root ganglion neurons. J. Neurosci. 17, 3525-3537 (1997).
    • (1997) J. Neurosci , vol.17 , pp. 3525-3537
    • Koplas, P.A.1    Rosenberg, R.L.2    Oxford, G.S.3
  • 17
    • 33846293924 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 modulates nociceptive signaling through direct phosphorylation of transient receptor potential vanilloid 1
    • Pareek, T. K. et al. Cyclin-dependent kinase 5 modulates nociceptive signaling through direct phosphorylation of transient receptor potential vanilloid 1. Proc. Natl. Acad. Sci. USA 104, 660-665 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 660-665
    • Pareek, T.K.1
  • 18
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-12 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 19
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-8 (2013).
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 20
    • 0346118925 scopus 로고    scopus 로고
    • Desensitization of Capsaicin-activated Currents in the Vanilloid Receptor TRPV1 Is Decreased by the Cyclic AMP-dependent Protein Kinase Pathway
    • Mohapatra, D. P. & Nau, C. Desensitization of Capsaicin-activated Currents in the Vanilloid Receptor TRPV1 Is Decreased by the Cyclic AMP-dependent Protein Kinase Pathway. J. Biol. Chem. 278, 50080-50090 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50080-50090
    • Mohapatra, D.P.1    Nau, C.2
  • 21
    • 77956807049 scopus 로고    scopus 로고
    • Modulation of single-channel properties of TRPV1 by phosphorylation
    • Studer, M. & McNaughton, P. a. Modulation of single-channel properties of TRPV1 by phosphorylation. J. Physiol. 588, 3743-3756 (2010).
    • (2010) J. Physiol. , vol.588 , pp. 3743-3756
    • Studer, M.1    McNaughton, P.A.2
  • 22
    • 84877594044 scopus 로고    scopus 로고
    • TGF-β1 sensitizes TRPV1 through Cdk5 signaling in odontoblast-like cells
    • Utreras, E. et al. TGF-β1 sensitizes TRPV1 through Cdk5 signaling in odontoblast-like cells. Mol. Pain 9, 1-14 (2013).
    • (2013) Mol. Pain , vol.9 , pp. 1-14
    • Utreras, E.1
  • 23
    • 0037104657 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation
    • Bhave, G. et al. cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation. Neuron 35, 721-731 (2002).
    • (2002) Neuron , vol.35 , pp. 721-731
    • Bhave, G.1
  • 24
    • 0037134417 scopus 로고    scopus 로고
    • Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cε and identification of two target serine residues
    • Numazaki, M., Tominaga, T., Toyooka, H. & Tominaga, M. Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cε and identification of two target serine residues. J. Biol. Chem. 277, 13375-13378 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13375-13378
    • Numazaki, M.1    Tominaga, T.2    Toyooka, H.3    Tominaga, M.4
  • 25
    • 29244484493 scopus 로고    scopus 로고
    • NGF rapidly increases membrane expression of TRPV1 heat-gated ion channels
    • Zhang, X., Huang, J. & McNaughton, P. A. NGF rapidly increases membrane expression of TRPV1 heat-gated ion channels. EMBO J. 24, 4211-4223 (2005).
    • (2005) EMBO J , vol.24 , pp. 4211-4223
    • Zhang, X.1    Huang, J.2    McNaughton, P.A.3
  • 26
    • 84941948652 scopus 로고    scopus 로고
    • Phosphorylation of TRPV1 by cyclin-dependent kinase 5 promotes TRPV1 surface localization, leading to inflammatory thermal hyperalgesia
    • Liu, J., Du, J., Yang, Y. & Wang, Y. Phosphorylation of TRPV1 by cyclin-dependent kinase 5 promotes TRPV1 surface localization, leading to inflammatory thermal hyperalgesia. Exp. Neurol. 273, 253-262 (2015).
    • (2015) Exp. Neurol. , vol.273 , pp. 253-262
    • Liu, J.1    Du, J.2    Yang, Y.3    Wang, Y.4
  • 27
    • 84867624240 scopus 로고    scopus 로고
    • Cyclin-Dependent Kinase 5 Controls TRPV1 Membrane Trafficking and the Heat Sensitivity of Nociceptors through KIF13B
    • Xing, B.-M. et al. Cyclin-Dependent Kinase 5 Controls TRPV1 Membrane Trafficking and the Heat Sensitivity of Nociceptors through KIF13B. J. Neurosci. 32, 14709-14721 (2012).
    • (2012) J. Neurosci , vol.32 , pp. 14709-14721
    • Xing, B.-M.1
  • 28
    • 84907183896 scopus 로고    scopus 로고
    • TRPV1: A Potential Drug Target for Treating Various Diseases
    • Brito, R., Sheth, S., Mukherjea, D., Rybak, L. P. & Ramkumar, V. TRPV1: A Potential Drug Target for Treating Various Diseases. Cells 3, 517-45 (2014).
    • (2014) Cells , vol.3 , pp. 517-545
    • Brito, R.1    Sheth, S.2    Mukherjea, D.3    Rybak, L.P.4    Ramkumar, V.5
  • 29
    • 84947800807 scopus 로고    scopus 로고
    • A combined coarse-grained and all-atom simulation of TRPV1 channel gating and heat activation
    • Zheng, W. & Qin, F. A combined coarse-grained and all-atom simulation of TRPV1 channel gating and heat activation. J. Gen. Physiol. 145, 443-456 (2015).
    • (2015) J. Gen. Physiol. , vol.145 , pp. 443-456
    • Zheng, W.1    Qin, F.2
  • 30
    • 0031018336 scopus 로고    scopus 로고
    • Mice lacking p35, a neuronal specific activator of Cdk5, display cortical lamination defects, seizures, and adult lethality
    • Chae, T. et al. Mice lacking p35, a neuronal specific activator of Cdk5, display cortical lamination defects, seizures, and adult lethality. Neuron 18, 29-42 (1997).
    • (1997) Neuron , vol.18 , pp. 29-42
    • Chae, T.1
  • 31
    • 13444265883 scopus 로고    scopus 로고
    • Increased activity of cyclin-dependent kinase 5 leads to attenuation of cocaine-mediated dopamine signaling
    • Takahashi, S. et al. Increased activity of cyclin-dependent kinase 5 leads to attenuation of cocaine-mediated dopamine signaling. Proc. Natl. Acad. Sci. USA 102, 1737-1742 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1737-1742
    • Takahashi, S.1
  • 32
    • 0020525719 scopus 로고
    • Ethical guidelines for investigations of experimental pain in conscious animals
    • Zimmermann, M. Ethical guidelines for investigations of experimental pain in conscious animals. Pain 16, 109-10 (1983).
    • (1983) Pain , vol.16 , pp. 109-110
    • Zimmermann, M.1
  • 33
    • 84894664138 scopus 로고    scopus 로고
    • Use of the Operant Orofacial Pain Assessment Device (OPAD) to Measure Changes in Nociceptive Behavior
    • Anderson, E. M. et al. Use of the Operant Orofacial Pain Assessment Device (OPAD) to Measure Changes in Nociceptive Behavior. J. Vis. Exp. 76, 1-6 (2013).
    • (2013) J. Vis. Exp. , vol.76 , pp. 1-6
    • Anderson, E.M.1
  • 34
    • 21844465712 scopus 로고    scopus 로고
    • Use of a novel thermal operant behavioral assay for characterization of orofacial pain sensitivity
    • Neubert, J. K. et al. Use of a novel thermal operant behavioral assay for characterization of orofacial pain sensitivity. Pain 116, 386-395 (2005).
    • (2005) Pain , vol.116 , pp. 386-395
    • Neubert, J.K.1
  • 35
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F. L. & van der Eb, A. J. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52, 456-467 (1973).
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 36
    • 84886879679 scopus 로고    scopus 로고
    • Pirt Functions as an Endogenous Regulator of TRPM8
    • Tang, Z. et al. Pirt Functions as an Endogenous Regulator of TRPM8. Nat. Commun. 4, 2179-2195 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2179-2195
    • Tang, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.