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Volumn 367, Issue 3, 2008, Pages 687-692

Lysosome mediated Kir2.1 breakdown directly influences inward rectifier current density

Author keywords

Chloroquine; Degradation; Inward rectifier; Kir2.1; Lysosome

Indexed keywords

AMMONIUM CHLORIDE; CADHERIN; CHLOROQUINE; INWARDLY RECTIFYING POTASSIUM CHANNEL; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR2.1; LEUPEPTIN; UNCLASSIFIED DRUG;

EID: 38649085314     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.12.168     Document Type: Article
Times cited : (40)

References (30)
  • 1
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft F.M. From molecule to malady. Nature 440 (2006) 440-447
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 2
    • 14644400497 scopus 로고    scopus 로고
    • K1) controls cardiac excitability and is involved in arrhythmogenesis
    • K1) controls cardiac excitability and is involved in arrhythmogenesis. Heart Rhythm 2 (2005) 316-324
    • (2005) Heart Rhythm , vol.2 , pp. 316-324
    • Dhamoon, A.S.1    Jalife, J.2
  • 3
    • 0030606298 scopus 로고    scopus 로고
    • Regions responsible for the assembly of inwardly rectifying potassium channels
    • Tinker A., Jan Y.N., and Jan L.Y. Regions responsible for the assembly of inwardly rectifying potassium channels. Cell 87 (1996) 857-868
    • (1996) Cell , vol.87 , pp. 857-868
    • Tinker, A.1    Jan, Y.N.2    Jan, L.Y.3
  • 6
    • 0037975497 scopus 로고    scopus 로고
    • Functional role of inward rectifier current in heart probed by Kir2.1 overexpression and dominant-negative suppression
    • Miake J., Marbán E., and Nuss H.B. Functional role of inward rectifier current in heart probed by Kir2.1 overexpression and dominant-negative suppression. J. Clin. Invest. 111 (2003) 1529-1536
    • (2003) J. Clin. Invest. , vol.111 , pp. 1529-1536
    • Miake, J.1    Marbán, E.2    Nuss, H.B.3
  • 8
    • 0037383482 scopus 로고    scopus 로고
    • K1 in the mouse heart leads to altered cardiac excitability
    • K1 in the mouse heart leads to altered cardiac excitability. J. Mol. Cell. Cardiol. 35 (2003) 367-378
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 367-378
    • McLerie, M.1    Lopatin, A.N.2
  • 10
    • 34347236923 scopus 로고    scopus 로고
    • Mechanisms of cardiac potassium channel trafficking
    • Steele D.F., Eldstrom J., and Fedida D. Mechanisms of cardiac potassium channel trafficking. J. Physiol. 582 (2007) 17-26
    • (2007) J. Physiol. , vol.582 , pp. 17-26
    • Steele, D.F.1    Eldstrom, J.2    Fedida, D.3
  • 11
    • 0035846990 scopus 로고    scopus 로고
    • Role of ER export signals in controlling surface potassium channel numbers
    • Ma D., Zerangue N., Lin Y.-F., Collins A., Yu M., Jan Y.N., and Jan L.Y. Role of ER export signals in controlling surface potassium channel numbers. Science 291 (2001) 316-319
    • (2001) Science , vol.291 , pp. 316-319
    • Ma, D.1    Zerangue, N.2    Lin, Y.-F.3    Collins, A.4    Yu, M.5    Jan, Y.N.6    Jan, L.Y.7
  • 13
    • 0037593865 scopus 로고    scopus 로고
    • Surface expression of inward rectifier potassium is controlled by selective golgi export
    • Stockklausner C., and Klöcker N. Surface expression of inward rectifier potassium is controlled by selective golgi export. J. Biol. Chem. 278 (2003) 17000-17005
    • (2003) J. Biol. Chem. , vol.278 , pp. 17000-17005
    • Stockklausner, C.1    Klöcker, N.2
  • 14
    • 19444368039 scopus 로고    scopus 로고
    • Selective golgi export of Kir2.1 controls the stoichiometry of functional Kir2.x channel heteromers
    • Hofherr A., Fakler B., and Klöcker N. Selective golgi export of Kir2.1 controls the stoichiometry of functional Kir2.x channel heteromers. J. Cell Sci. 118 (2005) 1935-1943
    • (2005) J. Cell Sci. , vol.118 , pp. 1935-1943
    • Hofherr, A.1    Fakler, B.2    Klöcker, N.3
  • 17
    • 0142211278 scopus 로고    scopus 로고
    • Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1
    • Sampson L.J., Leyland M.L., and Dart C. Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1. J. Biol. Chem. 278 (2003) 41988-41997
    • (2003) J. Biol. Chem. , vol.278 , pp. 41988-41997
    • Sampson, L.J.1    Leyland, M.L.2    Dart, C.3
  • 20
    • 33646851612 scopus 로고    scopus 로고
    • Chronic inhibition of cardiac Kir2.1 and hERG potassium channels by celastrol with dual effects on both ion conductivity and protein trafficking
    • Sun H., Liu X., Xiong Q., Shikano S., and Li M. Chronic inhibition of cardiac Kir2.1 and hERG potassium channels by celastrol with dual effects on both ion conductivity and protein trafficking. J. Biol. Chem. 281 (2006) 5877-5884
    • (2006) J. Biol. Chem. , vol.281 , pp. 5877-5884
    • Sun, H.1    Liu, X.2    Xiong, Q.3    Shikano, S.4    Li, M.5
  • 21
    • 38849111329 scopus 로고    scopus 로고
    • M.A.G. van der Heyden, M.E. Smits, M.A. Vos, Drugs and trafficking of ion channels: a new pro-arrhythmic threat on the horizon? Br. J. Pharmacol. doi: 10.1038/sj.bjp.0707618.
  • 22
    • 0035003359 scopus 로고    scopus 로고
    • Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel
    • Tong Y., Brandt G.S., Li M., Shapovalov G., Slimko E., Karschin A., Dougherty D.A., and Lester H.A. Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel. J. Gen. Physiol. 117 (2001) 103-118
    • (2001) J. Gen. Physiol. , vol.117 , pp. 103-118
    • Tong, Y.1    Brandt, G.S.2    Li, M.3    Shapovalov, G.4    Slimko, E.5    Karschin, A.6    Dougherty, D.A.7    Lester, H.A.8
  • 23
    • 0018763480 scopus 로고
    • Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin
    • Seglen P.O., Grinde B., and Solheim A.E. Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin. Eur. J. Biochem. 95 (1979) 215-225
    • (1979) Eur. J. Biochem. , vol.95 , pp. 215-225
    • Seglen, P.O.1    Grinde, B.2    Solheim, A.E.3
  • 24
    • 0020022916 scopus 로고
    • Mechanisms of intracellular protein breakdown
    • Hershko A., and Ciechanover A. Mechanisms of intracellular protein breakdown. Ann. Rev. Biochem. 51 (1982) 335-364
    • (1982) Ann. Rev. Biochem. , vol.51 , pp. 335-364
    • Hershko, A.1    Ciechanover, A.2
  • 25
    • 0036566039 scopus 로고    scopus 로고
    • Endolysosomal proteolysis and its regulation
    • Pillay C.S., Elliot E., and Dennison C. Endolysosomal proteolysis and its regulation. Biochem. J. 363 (2002) 417-429
    • (2002) Biochem. J. , vol.363 , pp. 417-429
    • Pillay, C.S.1    Elliot, E.2    Dennison, C.3
  • 27
    • 0037053340 scopus 로고    scopus 로고
    • Identification of a familial hyperinsulinism-causing mutation in the sulfonylurea receptor 1 that prevents normal trafficking and function of KATP channels
    • Taschenberger G., Mougey A., Shen S., Lester L.B., LaFranchi S., and Shyng S.-L. Identification of a familial hyperinsulinism-causing mutation in the sulfonylurea receptor 1 that prevents normal trafficking and function of KATP channels. J. Biol. Chem. 277 (2002) 17139-17146
    • (2002) J. Biol. Chem. , vol.277 , pp. 17139-17146
    • Taschenberger, G.1    Mougey, A.2    Shen, S.3    Lester, L.B.4    LaFranchi, S.5    Shyng, S.-L.6
  • 29
    • 34447568519 scopus 로고    scopus 로고
    • Cardiotoxicity of antimalarial drugs
    • White N.J. Cardiotoxicity of antimalarial drugs. Lancet Infect. Dis. 7 (2007) 549-558
    • (2007) Lancet Infect. Dis. , vol.7 , pp. 549-558
    • White, N.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.