메뉴 건너뛰기




Volumn 126, Issue 6, 2005, Pages 541-549

Long polyamines act as cofactors in PIP2 activation of inward rectifier potassium (Kir2.1) channels

Author keywords

[No Author keywords available]

Indexed keywords

DIAMINE; NEOMYCIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; POLYAMINE DERIVATIVE; POTASSIUM; POTASSIUM CHANNEL; SPERMINE; SULFONYLUREA RECEPTOR;

EID: 28244444116     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200509380     Document Type: Article
Times cited : (34)

References (43)
  • 6
    • 0031055885 scopus 로고    scopus 로고
    • Anionic phospholipids activate ATP-sensitive potassium channels
    • Fan, Z., and J.C. Makielski. 1997. Anionic phospholipids activate ATP-sensitive potassium channels. J. Biol. Chem. 272:5388-5395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5388-5395
    • Fan, Z.1    Makielski, J.C.2
  • 9
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • Hilgemann, D.W., S. Feng, and C. Nasuhoglu. 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
  • 12
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ
    • Huang, C.L., S. Feng, and D.W. Hilgemann. 1998. Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ. Nature. 391:803-806.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 15
    • 0033545972 scopus 로고    scopus 로고
    • Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism
    • Liou, H.H., S.S. Zhou, and C.L. Huang. 1999. Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism. Proc. Natl. Acad. Sci. USA. 96:5820-5825.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5820-5825
    • Liou, H.H.1    Zhou, S.S.2    Huang, C.L.3
  • 16
    • 0020083449 scopus 로고
    • Aminoglycoside inhibition of a renal phosphatidylinositol phospholipase C
    • Lipsky, J.J., and P.S. Lietman. 1982. Aminoglycoside inhibition of a renal phosphatidylinositol phospholipase C. J. Pharmacol. Exp. Ther. 220:287-292.
    • (1982) J. Pharmacol. Exp. Ther. , vol.220 , pp. 287-292
    • Lipsky, J.J.1    Lietman, P.S.2
  • 17
    • 0027984375 scopus 로고
    • Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification
    • Lopatin, A.N., E.N. Makhina, and C.G. Nichols. 1994. Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification. Nature. 372:366-369.
    • (1994) Nature , vol.372 , pp. 366-369
    • Lopatin, A.N.1    Makhina, E.N.2    Nichols, C.G.3
  • 18
    • 0037071897 scopus 로고    scopus 로고
    • Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies
    • Lopes, C.M., H. Zhang, T. Rohacs, T. Jin, J. Yang, and D.E. Logothetis. 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
  • 21
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 a resolution
    • Nishida, M., and R. MacKinnon. 2002. Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution. Cell. 111:957-965.
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2
  • 22
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • Pegan, S., C. Arrabit, W. Zhou, W. Kwiatkowski, A. Collins, P.A. Slesinger, and S. Choe. 2005. Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nat. Neurosci. 8:279-287.
    • (2005) Nat. Neurosci. , vol.8 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6    Choe, S.7
  • 23
    • 20644445415 scopus 로고    scopus 로고
    • Regulation of the ATP-sensitive K channel Kir6.2 by ATP and PIP2
    • Ribalet, B., S.A. John, L.H. Xie, and J.N. Weiss. 2005. Regulation of the ATP-sensitive K channel Kir6.2 by ATP and PIP2. J. Mol. Cell. Cardiol. 39:71-77.
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 71-77
    • Ribalet, B.1    John, S.A.2    Xie, L.H.3    Weiss, J.N.4
  • 25
    • 0037518226 scopus 로고    scopus 로고
    • PIP2 modulation of ATP and pH sensitivity in Kir channels: A tale of an active and a silent PIP2 site in the N terminus
    • Schulze, D., T. Krauter, H. Fritzenschaft, M. Soom, and T. Baukrowitz. 2003. PIP2 modulation of ATP and pH sensitivity in Kir channels: a tale of an active and a silent PIP2 site in the N terminus. J. Biol. Chem. 278:10500-10505.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10500-10505
    • Schulze, D.1    Krauter, T.2    Fritzenschaft, H.3    Soom, M.4    Baukrowitz, T.5
  • 27
    • 0033756604 scopus 로고    scopus 로고
    • Structural determinants of PIP(2) regulation of inward rectifier K(ATP) channels
    • Shyng, S.L., C.A. Cukras, J. Harwood, and C.G. Nichols. 2000. Structural determinants of PIP(2) regulation of inward rectifier K(ATP) channels. J. Gen. Physiol. 116:599-608.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 599-608
    • Shyng, S.L.1    Cukras, C.A.2    Harwood, J.3    Nichols, C.G.4
  • 28
    • 0032491439 scopus 로고    scopus 로고
    • Membrane phospholipid control of nucleotide sensitivity of KATP channels
    • Shyng, S.L., and C.G. Nichols. 1998. Membrane phospholipid control of nucleotide sensitivity of KATP channels. Science. 282:1138-1141.
    • (1998) Science , vol.282 , pp. 1138-1141
    • Shyng, S.L.1    Nichols, C.G.2
  • 29
    • 0023755690 scopus 로고
    • Phorbol ester and neomycin dissociate bradykinin receptor-mediated arachidonic acid release and polyphosphoinositide hydrolysis in Madin-Darby canine kidney cells. Evidence that bradykinin mediates noninterdependent activation of phospholipases A2 and C
    • Slivka, S.R., and P.A. Insel. 1988. Phorbol ester and neomycin dissociate bradykinin receptor-mediated arachidonic acid release and polyphosphoinositide hydrolysis in Madin-Darby canine kidney cells. Evidence that bradykinin mediates noninterdependent activation of phospholipases A2 and C. J. Biol. Chem. 263:14640-14647.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14640-14647
    • Slivka, S.R.1    Insel, P.A.2
  • 30
    • 0035831491 scopus 로고    scopus 로고
    • ATP modulation of ATP-sensitive potassium channel ATP sensitivity varies with the type of SUR subunit
    • Song, D.K., and F.M. Ashcroft. 2001. ATP modulation of ATP-sensitive potassium channel ATP sensitivity varies with the type of SUR subunit. J. Biol. Chem. 276:7143-7149.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7143-7149
    • Song, D.K.1    Ashcroft, F.M.2
  • 31
    • 0035830482 scopus 로고    scopus 로고
    • Multiple PIP2 binding sites in Kir2.1 inwardly rectifying potassium channels
    • Soom, M., R. Schonherr, Y. Kubo, C. Kirsch, R. Klinger, and S.H. Heinemann. 2001. Multiple PIP2 binding sites in Kir2.1 inwardly rectifying potassium channels. FEBS Lett. 490:49-53.
    • (2001) FEBS Lett. , vol.490 , pp. 49-53
    • Soom, M.1    Schonherr, R.2    Kubo, Y.3    Kirsch, C.4    Klinger, R.5    Heinemann, S.H.6
  • 33
    • 0342576800 scopus 로고
    • Inward rectification of a potassium channel in cardiac ventricular cells depends on internal magnesium ions
    • Vandenberg, C.A. 1987. Inward rectification of a potassium channel in cardiac ventricular cells depends on internal magnesium ions. Proc. Natl. Acad. Sci. USA. 84:2560-2564.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2560-2564
    • Vandenberg, C.A.1
  • 36
    • 0033593007 scopus 로고    scopus 로고
    • Phospholipase C-linked receptors regulate the ATP-sensitive potassium channel by means of phosphatidylinositol 4,5-bisphosphate metabolism
    • Xie, L.H., M. Horie, and M. Takano. 1999a. Phospholipase C-linked receptors regulate the ATP-sensitive potassium channel by means of phosphatidylinositol 4,5-bisphosphate metabolism. Proc. Natl. Acad. Sci. USA. 96:15292-15297.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 15292-15297
    • Xie, L.H.1    Horie, M.2    Takano, M.3
  • 37
    • 0036020151 scopus 로고    scopus 로고
    • Spermine block of the strong inward rectifier potassium channel Kir2.1: Dual roles of surface charge screening and pore block
    • Xie, L.H., S.A. John, and J.N. Weiss. 2002. Spermine block of the strong inward rectifier potassium channel Kir2.1: dual roles of surface charge screening and pore block. J. Gen. Physiol. 120:53-66.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 53-66
    • Xie, L.H.1    John, S.A.2    Weiss, J.N.3
  • 38
    • 0038267590 scopus 로고    scopus 로고
    • Inward rectification by polyamines in mouse Kir2.1 channels: Synergy between blocking components
    • Xie, L.H., S.A. John, and J.N. Weiss. 2003. Inward rectification by polyamines in mouse Kir2.1 channels: synergy between blocking components. J. Physiol. 550:67-82.
    • (2003) J. Physiol. , vol.550 , pp. 67-82
    • Xie, L.H.1    John, S.A.2    Weiss, J.N.3
  • 39
    • 0033082993 scopus 로고    scopus 로고
    • Wortmannin, an inhibitor of phosphatidylinositol kinases, blocks the MgATP-dependent recovery of Kir6.2/SUR2A channels
    • Xie, L.H., M. Takano, M. Kakei, M. Okamura, and A. Noma. 1999b. Wortmannin, an inhibitor of phosphatidylinositol kinases, blocks the MgATP-dependent recovery of Kir6.2/SUR2A channels. J. Physiol. 514:655-665.
    • (1999) J. Physiol. , vol.514 , pp. 655-665
    • Xie, L.H.1    Takano, M.2    Kakei, M.3    Okamura, M.4    Noma, A.5
  • 41
    • 0022976813 scopus 로고
    • The binding of polyamines to phospholipid bilayers
    • Yung, M.W., and C. Green. 1986. The binding of polyamines to phospholipid bilayers. Biochem. Pharmacol. 35:4037-4041.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 4037-4041
    • Yung, M.W.1    Green, C.2
  • 42
    • 0038607909 scopus 로고    scopus 로고
    • Protein kinase C inhibits ROMK1 channel activity via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism
    • Zeng, W.Z., X.J. Li, D.W. Hilgemann, and C.L. Huang. 2003. Protein kinase C inhibits ROMK1 channel activity via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism. J. Biol. Chem. 278:16852-16856.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16852-16856
    • Zeng, W.Z.1    Li, X.J.2    Hilgemann, D.W.3    Huang, C.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.