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Volumn 288, Issue 8, 2013, Pages 5278-5290

Interplay between calmodulin and phosphatidylinositol 4,5-bisphosphate in Ca2+-induced inactivation of transient receptor potential vanilloid 6 channels

Author keywords

[No Author keywords available]

Indexed keywords

PATCH CLAMP EXPERIMENTS; PHOSPHATIDYLINOSITOL 4 ,5-BISPHOSPHATE; TRANSIENT RECEPTOR POTENTIAL VANILLOID;

EID: 84874314704     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.409482     Document Type: Article
Times cited : (52)

References (39)
  • 3
    • 0037163111 scopus 로고    scopus 로고
    • Fast and slow inactivation kinetics of the ca2+ channels ecac1 and ecac2 (trpv5 and trpv6). Role of the intracellular loop located between transmembrane segments 2 and 3
    • Nilius, B., Prenen, J., Hoenderop, J. G., Vennekens, R., Hoefs, S., Weidema, A. F., Droogmans, G., and Bindels, R. J. (2002) Fast and slow inactivation kinetics of the Ca2+ channels ECaC1 and ECaC2 (TRPV5 and TRPV6). Role of the intracellular loop located between transmembrane segments 2 and 3. J. Biol. Chem. 277, 30852-30858
    • (2002) J. Biol. Chem. , vol.277 , pp. 30852-30858
    • Nilius, B.1    Prenen, J.2    Hoenderop, J.G.3    Vennekens, R.4    Hoefs, S.5    Weidema, A.F.6    Droogmans, G.7    Bindels, R.J.8
  • 4
    • 62149151730 scopus 로고    scopus 로고
    • Phospholipase c-mediated regulation of transient receptor potential vanilloid 6 channels. Implications in active intestinal ca2+ transport
    • Thyagarajan, B., Benn, B. S., Christakos, S., and Rohacs, T. (2009) Phospholipase C-mediated regulation of transient receptor potential vanilloid 6 channels. Implications in active intestinal Ca2+ transport. Mol. Pharmacol. 75, 608-616
    • (2009) Mol. Pharmacol. , vol.75 , pp. 608-616
    • Thyagarajan, B.1    Benn, B.S.2    Christakos, S.3    Rohacs, T.4
  • 5
    • 48249116482 scopus 로고    scopus 로고
    • Pip2 is a necessary cofactor for ion channel function. How and why?
    • Suh, B. C., and Hille, B. (2008) PIP2 is a necessary cofactor for ion channel function. How and why? Annu. Rev. Biophys. 37, 175-195
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 175-195
    • Suh, B.C.1    Hille, B.2
  • 6
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of pip2 with ion channels and transporters
    • Hilgemann, D. W., Feng, S., and Nasuhoglu, C. (2001) The complex and intriguing lives of PIP2 with ion channels and transporters. Sci. STKE. 2001, re19
    • (2001) Sci. STKE. , vol.2001
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 7
    • 34548642323 scopus 로고    scopus 로고
    • Dynamic changes in phosphoinositide levels control ion channel activity
    • Logothetis, D. E., and Nilius, B. (2007) Dynamic changes in phosphoinositide levels control ion channel activity. Pflugers Arch. 455, 1-3
    • (2007) Pflugers Arch. , vol.455 , pp. 1-3
    • Logothetis, D.E.1    Nilius, B.2
  • 8
    • 67349183758 scopus 로고    scopus 로고
    • Phosphoinositide regulation of non-canonical transient receptor potential channels
    • Rohacs, T. (2009) Phosphoinositide regulation of non-canonical transient receptor potential channels. Cell Calcium 45, 554-565
    • (2009) Cell Calcium , vol.45 , pp. 554-565
    • Rohacs, T.1
  • 9
    • 55549104701 scopus 로고    scopus 로고
    • Transient receptor potential channels meet phosphoinositides
    • Nilius, B., Owsianik, G., and Voets, T. (2008) Transient receptor potential channels meet phosphoinositides. EMBO J. 27, 2809-2816
    • (2008) EMBO J. , vol.27 , pp. 2809-2816
    • Nilius, B.1    Owsianik, G.2    Voets, T.3
  • 10
    • 47249114957 scopus 로고    scopus 로고
    • Hydrolysis of phosphatidylinositol 4,5-bisphosphate mediates calcium-induced inactivation of trpv6 channels
    • Thyagarajan, B., Lukacs, V., and Rohacs, T. (2008) Hydrolysis of phosphatidylinositol 4,5-bisphosphate mediates calcium-induced inactivation of TRPV6 channels. J. Biol. Chem. 283, 14980-14987
    • (2008) J. Biol. Chem. , vol.283 , pp. 14980-14987
    • Thyagarajan, B.1    Lukacs, V.2    Rohacs, T.3
  • 11
    • 17844373771 scopus 로고    scopus 로고
    • Pi(45)p2 regulates the activation and desensitization of trpm8 channels through the trp domain
    • Rohács, T., Lopes, C. M., Michailidis, I., and Logothetis, D. E. (2005) PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain. Nat. Neurosci. 8, 626-634
    • (2005) Nat Neurosci , vol.8 , pp. 626-634
    • Rohács, T.1    Lopes, C.M.2    Michailidis, I.3    Logothetis, D.E.4
  • 12
    • 80355148470 scopus 로고    scopus 로고
    • Intracellular atp supports trpv6 activity via lipid kinases and the generation of ptdins(4,5)p2
    • Zakharian, E., Cao, C., and Rohacs, T. (2011) Intracellular ATP supports TRPV6 activity via lipid kinases and the generation of PtdIns(4,5)P2. FASEB J. 25, 3915-3928
    • (2011) FASEB J. , vol.25 , pp. 3915-3928
    • Zakharian, E.1    Cao, C.2    Rohacs, T.3
  • 13
    • 27644488050 scopus 로고    scopus 로고
    • Pip2 activates trpv5 and releases its inhibition by intracellular mg2+
    • Lee, J., Cha, S. K., Sun, T. J., and Huang, C. L. (2005) PIP2 activates TRPV5 and releases its inhibition by intracellular Mg2+. J. Gen. Physiol. 126, 439-451
    • (2005) J. Gen. Physiol. , vol.126 , pp. 439-451
    • Lee, J.1    Cha, S.K.2    Sun, T.J.3    Huang, C.L.4
  • 14
  • 17
    • 3142704668 scopus 로고    scopus 로고
    • Regulation of the mouse epithelial ca2+ channel trpv6 by the ca2 β-sensor calmodulin
    • Lambers, T. T., Weidema, A. F., Nilius, B., Hoenderop, J. G., and Bindels, R. J. (2004) Regulation of the mouse epithelial Ca2+ channel TRPV6 by the Ca2 β-sensor calmodulin. J. Biol. Chem. 279, 28855-28861
    • (2004) J. Biol. Chem. , vol.279 , pp. 28855-28861
    • Lambers, T.T.1    Weidema, A.F.2    Nilius, B.3    Hoenderop, J.G.4    Bindels, R.J.5
  • 18
    • 84864719970 scopus 로고    scopus 로고
    • The trpv5/6 calcium channels contain multiple calmodulin binding sites with differential binding properties
    • Kovalevskaya, N. V., Bokhovchuk, F. M., and Vuister, G. W. (2012) The TRPV5/6 calcium channels contain multiple calmodulin binding sites with differential binding properties. J. Struct. Funct. Genomics 13, 91-100
    • (2012) J. Struct. Funct. Genomics , vol.13 , pp. 91-100
    • Kovalevskaya, N.V.1    Bokhovchuk, F.M.2    Vuister, G.W.3
  • 19
    • 78751574306 scopus 로고    scopus 로고
    • Characterization of calmodulin binding domains in trpv2 and trpv5 c-tails
    • Holakovska, B., Grycova, L., Bily, J., and Teisinger, J. (2011) Characterization of calmodulin binding domains in TRPV2 and TRPV5 C-tails. Amino Acids 40, 741-748
    • (2011) Amino Acids , vol.40 , pp. 741-748
    • Holakovska, B.1    Grycova, L.2    Bily, J.3    Teisinger, J.4
  • 20
    • 33847081630 scopus 로고    scopus 로고
    • Integration of phosphoinositide-and calmodulin-mediated regulation of trpc6
    • Kwon, Y., Hofmann, T., and Montell, C. (2007) Integration of phosphoinositide-and calmodulin-mediated regulation of TRPC6. Mol. Cell. 25, 491-503
    • (2007) Mol. Cell. , vol.25 , pp. 491-503
    • Kwon, Y.1    Hofmann, T.2    Montell, C.3
  • 21
    • 0037032988 scopus 로고    scopus 로고
    • Cat1 contributes to the stores-operated calcium current in jurkat t-lymphocytes
    • Cui, J., Bian, J. S., Kagan, A., and McDonald, T. V. (2002) CaT1 contributes to the stores-operated calcium current in Jurkat T-lymphocytes. J. Biol. Chem. 277, 47175-47183
    • (2002) J. Biol. Chem. , vol.277 , pp. 47175-47183
    • Cui, J.1    Bian, J.S.2    Kagan, A.3    McDonald, T.V.4
  • 22
    • 62349105171 scopus 로고    scopus 로고
    • Four ca2+ ions activate trpm2 channels by binding in deep crevices near the pore but intracellularly of the gate
    • Csanády, L., and Törocsik, B. (2009) Four Ca2+ ions activate TRPM2 channels by binding in deep crevices near the pore but intracellularly of the gate. J. Gen. Physiol. 133, 189-203
    • (2009) J. Gen. Physiol. , vol.133 , pp. 189-203
    • Csanády, L.1    Törocsik, B.2
  • 23
    • 77958574020 scopus 로고    scopus 로고
    • Apractical guide to the preparation of ca2+ buffers
    • Bers, D. M., Patton, C. W., and Nuccitelli, R. (2010)Apractical guide to the preparation of Ca2+ buffers. Methods Cell Biol. 99, 1-26
    • (2010) Methods Cell Biol. , vol.99 , pp. 1-26
    • Bers, D.M.1    Patton, C.W.2    Nuccitelli, R.3
  • 25
    • 47249152762 scopus 로고    scopus 로고
    • Ca2+ microdomains near plasma membrane ca2+ channels. Impact on cell function
    • Parekh, A. B. (2008) Ca2+ microdomains near plasma membrane Ca2+ channels. Impact on cell function. J. Physiol. 586, 3043-3054
    • (2008) J. Physiol. , vol.586 , pp. 3043-3054
    • Parekh, A.B.1
  • 27
    • 0033548680 scopus 로고    scopus 로고
    • The relationship between the free concentrations of ca2+ and ca2 β-calmodulin in intact cells
    • Persechini, A., and Cronk, B. (1999) The relationship between the free concentrations of Ca2+ and Ca2 β-calmodulin in intact cells. J. Biol. Chem. 274, 6827-6830
    • (1999) J. Biol. Chem. , vol.274 , pp. 6827-6830
    • Persechini, A.1    Cronk, B.2
  • 29
    • 0036199229 scopus 로고    scopus 로고
    • Calmodulin as an ion channel subunit
    • Saimi, Y., and Kung, C. (2002) Calmodulin as an ion channel subunit. Annu. Rev. Physiol. 64, 289-311
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 289-311
    • Saimi, Y.1    Kung, C.2
  • 30
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A., and Ikura, M. (1995) Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 31
    • 24644460439 scopus 로고    scopus 로고
    • Multiple roles of calmodulin and other ca2 β-binding proteins in the functional regulation of trp channels
    • Zhu, M. X. (2005) Multiple roles of calmodulin and other Ca2 β-binding proteins in the functional regulation of TRP channels. Pflugers Arch. 451, 105-115
    • (2005) Pflugers Arch. , vol.451 , pp. 105-115
    • Zhu, M.X.1
  • 32
    • 34548658196 scopus 로고    scopus 로고
    • Regulation of transient receptor potential (trp) channels by phosphoinositides
    • Rohacs, T., and Nilius, B. (2007) Regulation of transient receptor potential (TRP) channels by phosphoinositides. Pflugers Arch. 455, 157-168
    • (2007) Pflugers Arch. , vol.455 , pp. 157-168
    • Rohacs, T.1    Nilius, B.2
  • 33
    • 34548614145 scopus 로고    scopus 로고
    • Molecular characteristics of phosphoinositide binding
    • Rosenhouse-Dantsker, A., and Logothetis, D. E. (2007) Molecular characteristics of phosphoinositide binding. Pflugers Arch. 455, 45-53
    • (2007) Pflugers Arch. , vol.455 , pp. 45-53
    • Rosenhouse-Dantsker, A.1    Logothetis, D.E.2
  • 34
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy. The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun, D. (1998) Binding, gating, affinity and efficacy. The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 125, 924-947
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 35
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin, S., and Murray, D. (2005) Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438, 605-611
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 36
    • 0037071897 scopus 로고    scopus 로고
    • Alterations in conserved kir channel-pip2 interactions underlie channelopathies
    • Lopes, C. M., Zhang, H., Rohacs, T., Jin, T., Yang, J., and Logothetis, D. E. (2002) Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies. Neuron 34, 933-944
    • (2002) Neuron , vol.34 , pp. 933-944
    • Lopes, C.M.1    Zhang, H.2    Rohacs, T.3    Jin, T.4    Yang, J.5    Logothetis, D.E.6
  • 38
    • 80053485088 scopus 로고    scopus 로고
    • + channel and gating regulation by g proteins, pip2, and sodium
    • + channel and gating regulation by G proteins, PIP2, and sodium. Cell 147, 199-208
    • (2011) Cell , vol.147 , pp. 199-208
    • Whorton, M.R.1    MacKinnon, R.2


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