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Volumn 287, Issue 42, 2012, Pages 35612-35620

Canonical transient receptor potential (TRPC) 1 acts as a negative regulator for vanilloid TRPV6-mediated Ca2+ influx

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; CANONICAL TRANSIENT RECEPTOR POTENTIALS; CO-EXPRESSION; COLOCALIZATION; CURRENT-VOLTAGE RELATIONSHIP; CYTOSOLIC; FUNCTIONAL INTERACTION; HEK293 CELLS; HOMOMERIC CHANNELS; IN-LINE; IN-VIVO; INTRACELLULAR RETENTION; N-TERMINALS; NEGATIVE REGULATORS;

EID: 84867412996     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.400952     Document Type: Article
Times cited : (40)

References (52)
  • 2
    • 77956272001 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family
    • Wu, L. J., Sweet, T. B., and Clapham, D. E. (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
  • 5
    • 79953138859 scopus 로고    scopus 로고
    • Heteromerization of TRP channel subunits: Extending functional diversity
    • Cheng, W., Sun, C., and Zheng, J. (2010) Heteromerization of TRP channel subunits: extending functional diversity. Protein Cell 1, 802-810
    • (2010) Protein Cell , vol.1 , pp. 802-810
    • Cheng, W.1    Sun, C.2    Zheng, J.3
  • 6
    • 33847026059 scopus 로고    scopus 로고
    • Assembly domains in TRP channels
    • Schindl, R., and Romanin, C. (2007) Assembly domains in TRP channels. Biochem. Soc. Trans. 35, 84-85
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 84-85
    • Schindl, R.1    Romanin, C.2
  • 7
    • 23844527412 scopus 로고    scopus 로고
    • Functional role of TRPC proteins in native systems: Implications from knockout and knock-down studies
    • DOI 10.1113/jphysiol.2005.092999
    • Freichel, M., Vennekens, R., Olausson, J., Stolz, S., Philipp, S. E., Weissgerber, P., and Flockerzi, V. (2005) Functional role of TRPC proteins in native systems: implications from knockout and knock-down studies. J. Physiol. 567, 59-66 (Pubitemid 41167305)
    • (2005) Journal of Physiology , vol.567 , Issue.1 , pp. 59-66
    • Freichel, M.1    Vennekens, R.2    Olausson, J.3    Stolz, S.4    Philipp, S.E.5    Weissgerber, P.6    Flockerzi, V.7
  • 8
    • 0037832459 scopus 로고    scopus 로고
    • TRPC1 store-operated cationic channel subunit
    • DOI 10.1016/S0143-4160(03)00054-X
    • Beech, D. J., Xu, S. Z., McHugh, D., and Flemming, R. (2003) TRPC1 store-operated cationic channel subunit. Cell Calcium 33, 433-440 (Pubitemid 36748665)
    • (2003) Cell Calcium , vol.33 , Issue.5-6 , pp. 433-440
    • Beech, D.J.1    Xu, S.Z.2    McHugh, D.3    Flemming, R.4
  • 9
    • 0035051978 scopus 로고    scopus 로고
    • TRPC1 and TRPC5 form a novel cation channel in mammalian brain
    • DOI 10.1016/S0896-6273(01)00240-9
    • Strübing, C., Krapivinsky, G., Krapivinsky, L., and Clapham, D. E. (2001) TRPC1 and TRPC5 form a novel cation channel in mammalian brain. Neuron 29, 645-655 (Pubitemid 32323938)
    • (2001) Neuron , vol.29 , Issue.3 , pp. 645-655
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 12
    • 20444364145 scopus 로고    scopus 로고
    • Molecular analysis of a store-operated and 2-acetyl-sn-glycerol-sensitive non-selective cation channel: Heteromeric assembly of TRPC1-TRPC3
    • DOI 10.1074/jbc.C400492200
    • Liu, X., Bandyopadhyay, B. C., Singh, B. B., Groschner, K., and Ambudkar, I. S. (2005) Molecular analysis of a store-operated and 2-acetyl-sn-glycerol- sensitive non-selective cation channel. Heteromeric assembly of TRPC1-TRPC3. J. Biol. Chem. 280, 21600-21606 (Pubitemid 40805728)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21600-21606
    • Liu, X.1    Bandyopadhyay, B.C.2    Singh, B.B.3    Groschner, K.4    Ambudkar, I.S.5
  • 13
    • 0141755156 scopus 로고    scopus 로고
    • Formation of novel TRPC channels by complex subunit interactions in embryonic brain
    • DOI 10.1074/jbc.M306705200
    • Strübing, C., Krapivinsky, G., Krapivinsky, L., and Clapham, D. E. (2003) Formation of novel TRPC channels by complex subunit interactions in embryonic brain. J. Biol. Chem. 278, 39014-39019 (Pubitemid 37221803)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 39014-39019
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 14
    • 84856293010 scopus 로고    scopus 로고
    • Transient receptor potential channel 1 (TRPC1) reduces calcium permeability in heteromeric channel complexes
    • Storch, U., Forst, A. L., Philipp, M., Gudermann, T., and Mederos y Schnitzler, M. (2012) Transient receptor potential channel 1 (TRPC1) reduces calcium permeability in heteromeric channel complexes. J. Biol. Chem. 287, 3530-3540
    • (2012) J. Biol. Chem. , vol.287 , pp. 3530-3540
    • Storch, U.1    Forst, A.L.2    Philipp, M.3    Gudermann, T.4    Mederos Y Schnitzler, M.5
  • 16
    • 43049117188 scopus 로고    scopus 로고
    • Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits
    • DOI 10.1038/embor.2008.29, PII EMBOR200829
    • Bai, C. X., Giamarchi, A., Rodat-Despoix, L., Padilla, F., Downs, T., Tsiokas, L., and Delmas, P. (2008) Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits. EMBO Rep. 9, 472-479 (Pubitemid 351627286)
    • (2008) EMBO Reports , vol.9 , Issue.5 , pp. 472-479
    • Bai, C.-X.1    Giamarchi, A.2    Rodat-Despoix, L.3    Padilla, F.4    Downs, T.5    Tsiokas, L.6    Delmas, P.7
  • 17
    • 72149113587 scopus 로고    scopus 로고
    • The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement
    • Kobori, T., Smith, G. D., Sandford, R., and Edwardson, J. M. (2009) The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement. J. Biol. Chem. 284, 35507-35513
    • (2009) J. Biol. Chem. , vol.284 , pp. 35507-35513
    • Kobori, T.1    Smith, G.D.2    Sandford, R.3    Edwardson, J.M.4
  • 19
    • 39749115631 scopus 로고    scopus 로고
    • Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels
    • DOI 10.1021/bi702109w
    • Phelps, C. B., Huang, R. J., Lishko, P. V., Wang, R. R., and 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
  • 20
    • 33847394506 scopus 로고    scopus 로고
    • Thermosensitive TRPV channel subunits coassemble into heteromeric channels with intermediate conductance and gating properties
    • DOI 10.1085/jgp.200709731
    • Cheng, W., Yang, F., Takanishi, C. L., and Zheng, J. (2007) Thermosensitive TRPV channel subunits coassemble into heteromeric channels with intermediate conductance and gating properties. J. Gen. Physiol. 129, 191-207 (Pubitemid 46333922)
    • (2007) Journal of General Physiology , vol.129 , Issue.3 , pp. 191-207
    • Cheng, W.1    Yang, F.2    Takanishi, C.L.3    Zheng, J.4
  • 21
    • 77950876498 scopus 로고    scopus 로고
    • Functional role of vanilloid transient receptor potential 4-canonical transient receptor potential 1 complex in flow-induced Ca2+ influx
    • Ma, X., Qiu, S., Luo, J., Ma, Y., Ngai, C. Y., Shen, B., Wong, C. O., Huang, Y., and Yao, X. (2010) Functional role of vanilloid transient receptor potential 4-canonical transient receptor potential 1 complex in flow-induced Ca2+ influx. Arterioscler. Thromb. Vasc. Biol. 30, 851-858
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 851-858
    • Ma, X.1    Qiu, S.2    Luo, J.3    Ma, Y.4    Ngai, C.Y.5    Shen, B.6    Wong, C.O.7    Huang, Y.8    Yao, X.9
  • 22
    • 66049108304 scopus 로고    scopus 로고
    • TRPC1 and TRPC6 channels cooperate with TRPV4 to mediate mechanical hyperalgesia and nociceptor sensitization
    • Alessandri-Haber, N., Dina, O. A., Chen, X., and Levine, J. D. (2009) TRPC1 and TRPC6 channels cooperate with TRPV4 to mediate mechanical hyperalgesia and nociceptor sensitization. J. Neurosci. 29, 6217-6228
    • (2009) J. Neurosci. , vol.29 , pp. 6217-6228
    • Alessandri-Haber, N.1    Dina, O.A.2    Chen, X.3    Levine, J.D.4
  • 24
    • 18444365257 scopus 로고    scopus 로고
    • Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1β
    • DOI 10.1016/S0014-5793(02)02971-X, PII S001457930202971X
    • Engelke, M., Friedrich, O., Budde, P., Schäfer, C., Niemann, U., Zitt, C., Jüngling, E., Rocks, O., Lückhoff, A., and Frey, J. (2002) Structural domains required for channel function of the mouse transient receptor potential protein homologue TRP1β. FEBS Lett. 523, 193-199 (Pubitemid 34786085)
    • (2002) FEBS Letters , vol.523 , Issue.1-3 , pp. 193-199
    • Engelke, M.1    Friedrich, O.2    Budde, P.3    Schafer, C.4    Niemann, U.5    Zitt, C.6    Jungling, E.7    Rocks, O.8    Luckhoff, A.9    Frey, J.10
  • 25
    • 33846012551 scopus 로고    scopus 로고
    • Intracellular coiled-coil domain engaged in subunit interaction and assembly of melastatin-related transient receptor potential channel 2
    • DOI 10.1074/jbc.M607591200
    • Mei, Z. Z., Xia, R., Beech, D. J., and Jiang, L. H. (2006) Intracellular coiled-coil domain engaged in subunit interaction and assembly of melastatin-related transient receptor potential channel 2. J. Biol. Chem. 281, 38748-38756 (Pubitemid 46042002)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38748-38756
    • Mei, Z.-Z.1    Xia, R.2    Beech, D.J.3    Jiang, L.-H.4
  • 26
    • 69549095712 scopus 로고    scopus 로고
    • Requirement for the N-terminal coiled-coil domain for expression and function, but not subunit interaction of, the ADPR-activated TRPM2 channel
    • Mei, Z. Z., and Jiang, L. H. (2009) Requirement for the N-terminal coiled-coil domain for expression and function, but not subunit interaction of, the ADPR-activated TRPM2 channel. J. Membr. Biol. 230, 93-99
    • (2009) J. Membr. Biol. , vol.230 , pp. 93-99
    • Mei, Z.Z.1    Jiang, L.H.2
  • 27
    • 33745877323 scopus 로고    scopus 로고
    • Coiled Coils Direct Assembly of a Cold-Activated TRP Channel
    • DOI 10.1016/j.neuron.2006.06.023, PII S0896627306005034
    • Tsuruda, P. R., Julius, D., and Minor, D. L., Jr. (2006) Coiled coils direct assembly of a cold-activated TRP channel. Neuron 51, 201-212 (Pubitemid 44041868)
    • (2006) Neuron , vol.51 , Issue.2 , pp. 201-212
    • Tsuruda, P.R.1    Julius, D.2    Minor Jr., D.L.3
  • 29
    • 70350452754 scopus 로고    scopus 로고
    • Orai1 internalization and STIM1 clustering inhibition modulate SOCE inactivation during meiosis
    • Yu, F., Sun, L., and Machaca, K. (2009) Orai1 internalization and STIM1 clustering inhibition modulate SOCE inactivation during meiosis. Proc. Natl. Acad. Sci. U.S.A. 106, 17401-17406
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17401-17406
    • Yu, F.1    Sun, L.2    Machaca, K.3
  • 31
    • 39049086672 scopus 로고    scopus 로고
    • The first ankyrin-like repeat is the minimum indispensable key structure for functional assembly of homo- and heteromeric TRPC4/TRPC5 channels
    • DOI 10.1016/j.ceca.2007.05.015, PII S0143416007001169
    • Schindl, R., Frischauf, I., Kahr, H., Fritsch, R., Krenn, M., Derndl, A., Vales, E., Muik, M., Derler, I., Groschner, K., and Romanin, C. (2008) The first ankyrin-like repeat is the minimum indispensable key structure for functional assembly of homo- and heteromeric TRPC4/TRPC5 channels. Cell Calcium 43, 260-269 (Pubitemid 351248306)
    • (2008) Cell Calcium , vol.43 , Issue.3 , pp. 260-269
    • Schindl, R.1    Frischauf, I.2    Kahr, H.3    Fritsch, R.4    Krenn, M.5    Derndl, A.6    Vales, E.7    Muik, M.8    Derler, I.9    Groschner, K.10    Romanin, C.11
  • 32
    • 33644969008 scopus 로고    scopus 로고
    • Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking
    • Arniges, M., Fernández-Fernández, J. M., Albrecht, N., Schaefer, M., and Valverde, M. A. (2006) Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking. J. Biol. Chem. 281, 1580-1586
    • (2006) J. Biol. Chem. , vol.281 , pp. 1580-1586
    • Arniges, M.1    Fernández-Fernández, J.M.2    Albrecht, N.3    Schaefer, M.4    Valverde, M.A.5
  • 33
    • 4444263598 scopus 로고    scopus 로고
    • 2+-selective transient receptor potential v channel architecture and function require a specific ankyrin repeat
    • 2+-selective transient receptor potential V channel architecture and function require a specific ankyrin repeat. J. Biol. Chem. 279, 34456-34463
    • (2004) J. Biol. Chem. , vol.279 , pp. 34456-34463
    • Erler, I.1    Hirnet, D.2    Wissenbach, U.3    Flockerzi, V.4    Niemeyer, B.A.5
  • 36
    • 33847044378 scopus 로고    scopus 로고
    • Molecular determinants of TRP channel assembly
    • Lepage, P. K., and Boulay, G. (2007) Molecular determinants of TRP channel assembly. Biochem. Soc. Trans. 35, 81-83
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 81-83
    • Lepage, P.K.1    Boulay, G.2
  • 38
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., Marty, A., Neher, E., Sakmann, B., and Sigworth, F. J. (1981) Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 391, 85-100
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 39
    • 80052758533 scopus 로고    scopus 로고
    • Role of the transient receptor potential vanilloid 5 (TRPV5) protein N terminus in channel activity, tetramerization, and trafficking
    • de Groot, T., van der Hagen, E. A., Verkaart, S., te Boekhorst, V. A., Bindels, R. J., and Hoenderop, J. G. (2011) Role of the transient receptor potential vanilloid 5 (TRPV5) protein N terminus in channel activity, tetramerization, and trafficking. J. Biol. Chem. 286, 32132-32139
    • (2011) J. Biol. Chem. , vol.286 , pp. 32132-32139
    • De Groot, T.1    Van Der Hagen, E.A.2    Verkaart, S.3    Te Boekhorst, V.A.4    Bindels, R.J.5    Hoenderop, J.G.6
  • 40
    • 66549127486 scopus 로고    scopus 로고
    • Dynamic interaction of hTRPC6 with the Orai1-STIM1 complex or hTRPC3 mediates its role in capacitative or non-capacitative Ca(2+) entry pathways
    • Jardin, I., Gómez, L. J., Salido, G. M., and Rosado, J. A. (2009) Dynamic interaction of hTRPC6 with the Orai1-STIM1 complex or hTRPC3 mediates its role in capacitative or non-capacitative Ca(2+) entry pathways. Biochem. J. 420, 267-276
    • (2009) Biochem. J. , vol.420 , pp. 267-276
    • Jardin, I.1    Gómez, L.J.2    Salido, G.M.3    Rosado, J.A.4
  • 43
    • 38049045102 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate enhances store-operated calcium entry through hTRPC6 channel in human platelets
    • Jardín, I., Redondo, P. C., Salido, G. M., and Rosado, J. A. (2008) Phosphatidylinositol 4,5-bisphosphate enhances store-operated calcium entry through hTRPC6 channel in human platelets. Biochim. Biophys. Acta 1783, 84-97
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 84-97
    • Jardín, I.1    Redondo, P.C.2    Salido, G.M.3    Rosado, J.A.4
  • 45
    • 0037178836 scopus 로고    scopus 로고
    • 2+ channel) channels
    • DOI 10.1074/jbc.M203700200
    • Schindl, R., Kahr, H., Graz, I., Groschner, K., and Romanin, C. (2002) Store depletion-activated CaT1 currents in rat basophilic leukemia mast cells are inhibited by 2-aminoethoxydiphenyl borate. Evidence for a regulatory component that controls activation of both CaT1 and CRAC (Ca(2+) release-activated Ca(2+) channel) channels. J. Biol. Chem. 277, 26950-26958 (Pubitemid 34951705)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26950-26958
    • Schindl, R.1    Kahr, H.2    Graz, I.3    Groschner, K.4    Romanin, C.5
  • 48
    • 39749178391 scopus 로고    scopus 로고
    • Regulation of the cellular localization and function of human transient receptor potential channel 1 by other members of the TRPC family
    • DOI 10.1016/j.ceca.2007.07.004, PII S0143416007001352
    • Alfonso, S., Benito, O., Alicia, S., Angélica, Z., Patricia, G., Diana, K., Vaca, L., and Luis, V. (2008) Regulation of the cellular localization and function of human transient receptor potential channel 1 by other members of the TRPC family. Cell Calcium 43, 375-387 (Pubitemid 351305721)
    • (2008) Cell Calcium , vol.43 , Issue.4 , pp. 375-387
    • Alfonso, S.1    Benito, O.2    Alicia, S.3    Angelica, Z.4    Patricia, G.5    Diana, K.6    Luis, V.7
  • 52
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia, Z., and Liu, Y. (2001) Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402 (Pubitemid 32917186)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2


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