메뉴 건너뛰기




Volumn 288, Issue 49, 2013, Pages 35358-35371

[Ca2+]i elevation and oxidative stress induce KCNQ1 protein translocation from the cytosol to the cell surface and increase slow delayed rectifier (IKs) in cardiac myocytes

Author keywords

[No Author keywords available]

Indexed keywords

CARDIAC MYOCYTES; COLOCALIZATION; DELAYED RECTIFIER; INTRACELLULAR COMPARTMENTS; PROTEIN TRANSLOCATION; STRESS-INDUCED; VENTRICULAR MYOCYTES; VENTRICULAR REPOLARIZATION;

EID: 84890276776     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.504746     Document Type: Article
Times cited : (25)

References (35)
  • 6
    • 67650257916 scopus 로고    scopus 로고
    • Dynamic partnership between KCNQ1 and KCNE1 and influence on cardiac IKs current amplitude by KCNE2
    • Jiang, M., Xu, X., Wang, Y., Toyoda, F., Liu, X.-S., Zhang, M., Robinson, R. B., and Tseng, G.-N. (2009) Dynamic partnership between KCNQ1 and KCNE1 and influence on cardiac IKs current amplitude by KCNE2. J. Biol. Chem. 284, 16452-16462
    • (2009) J. Biol. Chem. , vol.284 , pp. 16452-16462
    • Jiang, M.1    Xu, X.2    Wang, Y.3    Toyoda, F.4    Liu, X.-S.5    Zhang, M.6    Robinson, R.B.7    Tseng, G.-N.8
  • 7
    • 84863023479 scopus 로고    scopus 로고
    • KCNE2 protein is more abundant in ventricles than in atria and can accelerate hERG protein degradation in a phosphorylation-dependent manner
    • Zhang, M., Wang, Y.-H., Jiang, M., Zankov, D. P., Chowdhury, S. R., Kasirajan, V., and Tseng, G.-N. (2012) KCNE2 protein is more abundant in ventricles than in atria and can accelerate hERG protein degradation in a phosphorylation-dependent manner. Am. J. Physiol. Heart Circ. Physiol. 302, H910-H922
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.302
    • Zhang, M.1    Wang, Y.-H.2    Jiang, M.3    Zankov, D.P.4    Chowdhury, S.R.5    Kasirajan, V.6    Tseng, G.-N.7
  • 9
    • 40349091672 scopus 로고    scopus 로고
    • KCNE4 can co-associate with the IKs (KCNQ1-KCNE1) channel complex
    • Manderfield, L. J., and George, A. L. Jr. (2008) KCNE4 can co-associate with the IKs (KCNQ1-KCNE1) channel complex. FEBS J. 275, 1336-1349
    • (2008) FEBS J. , vol.275 , pp. 1336-1349
    • Manderfield, L.J.1    George, J.R.A.L.2
  • 12
    • 0347093353 scopus 로고    scopus 로고
    • KvLQT1 modulates the distribution and biophysical properties of HERG. A novel -subunit interaction between delayed rectifier currents
    • Ehrlich, J. R., Pourrier, M., Weerapura, M., Ethier, N., Marmabachi, A. M., Hébert, T. E., and Nattel, S. (2004) KvLQT1 modulates the distribution and biophysical properties of HERG. A novel -subunit interaction between delayed rectifier currents. J. Biol. Chem. 279, 1233-1241
    • (2004) J. Biol. Chem. , vol.279 , pp. 1233-1241
    • Ehrlich, J.R.1    Pourrier, M.2    Weerapura, M.3    Ethier, N.4    Marmabachi, A.M.5    Hébert, T.E.6    Nattel, S.7
  • 13
    • 11144281295 scopus 로고    scopus 로고
    • Comparison of ion channel distribution and expression in cardiomyocytes of canine pulmonary veins versus left atrium
    • Melnyk, P., Ehrlich, J. R., Pourrier, M., Villeneuve, L., Cha, T. J., and Nattel, S. (2005) Comparison of ion channel distribution and expression in cardiomyocytes of canine pulmonary veins versus left atrium. Cardiovasc. Res. 65, 104-116
    • (2005) Cardiovasc. Res. , vol.65 , pp. 104-116
    • Melnyk, P.1    Ehrlich, J.R.2    Pourrier, M.3    Villeneuve, L.4    Cha, T.J.5    Nattel, S.6
  • 15
    • 33845219551 scopus 로고    scopus 로고
    • KCNE2 is colocalized with KCNQ1 and KCNE1 in cardiac myocytes and may function as a negative modulator of IKs current amplitude in the heart
    • Wu, D.-M., Jiang, M., Zhang, M., Liu, X.-S., Korolkova, Y. V., and Tseng, G.-N. (2006) KCNE2 is colocalized with KCNQ1 and KCNE1 in cardiac myocytes and may function as a negative modulator of IKs current amplitude in the heart. Heart Rhythm 3, 1469-1480
    • (2006) Heart Rhythm , vol.3 , pp. 1469-1480
    • Wu, D.-M.1    Jiang, M.2    Zhang, M.3    Liu, X.-S.4    Korolkova, Y.V.5    Tseng, G.-N.6
  • 16
    • 0035798418 scopus 로고    scopus 로고
    • Specific interaction of the potassium channel -subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system
    • Furukawa, T., Ono, Y., Tsuchiya, H., Katayama, Y., Bang, M.-L., Labeit, D., Labeit, S., Inagaki, N., and Gregorio, C. C. (2001) Specific interaction of the potassium channel -subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system. J. Mol. Biol. 313, 775-784
    • (2001) J. Mol. Biol. , vol.313 , pp. 775-784
    • Furukawa, T.1    Ono, Y.2    Tsuchiya, H.3    Katayama, Y.4    Bang, M.-L.5    Labeit, D.6    Labeit, S.7    Inagaki, N.8    Gregorio, C.C.9
  • 17
    • 77950468071 scopus 로고    scopus 로고
    • Direct observation of individual KCNQ1 potassium channels reveals their distinctive diffusive behavior
    • Mashanov, G. I., Nobles, M., Harmer, S. C., Molloy, J. E., and Tinker, A. (2010) Direct observation of individual KCNQ1 potassium channels reveals their distinctive diffusive behavior. J. Biol. Chem. 285, 3664-3675
    • (2010) J. Biol. Chem. , vol.285 , pp. 3664-3675
    • Mashanov, G.I.1    Nobles, M.2    Harmer, S.C.3    Molloy, J.E.4    Tinker, A.5
  • 19
    • 0035816618 scopus 로고    scopus 로고
    • HCN2 overexpression in newborn and adult ventricular myocytes. Distinct effects on gating and excitability
    • Qu, J., Barbuti, A., Protas, L., Santoro, B., Cohen, I. S., and Robinson, R. B. (2001) HCN2 overexpression in newborn and adult ventricular myocytes. Distinct effects on gating and excitability. Circ. Res. 89, E8-14
    • (2001) Circ. Res. , vol.89
    • Qu, J.1    Barbuti, A.2    Protas, L.3    Santoro, B.4    Cohen, I.S.5    Robinson, R.B.6
  • 20
    • 0033583244 scopus 로고    scopus 로고
    • Mechanisms of altered excitation-contraction coupling in canine tachycardia-induced heart failure,I. Experimental studies
    • O'Rourke, B., Kass, D. A., Tomaselli, G. F., Kääb, S., Tunin, R., and Marbán, E. (1999) Mechanisms of altered excitation-contraction coupling in canine tachycardia-induced heart failure, I. Experimental studies. Circ. Res. 84, 562-570
    • (1999) Circ. Res. , vol.84 , pp. 562-570
    • O'Rourke, B.1    Kass, D.A.2    Tomaselli, G.F.3    Kääb, S.4    Tunin, R.5    Marbán, E.6
  • 21
    • 84864067796 scopus 로고    scopus 로고
    • Dynamic of ion channel expression at the plasma membrane of cardiomyocytes
    • Balse, E., Steele, D. F., Abriel, H., Coulombe, A., Fedida, D., and Hatem, S. N. (2012) Dynamic of ion channel expression at the plasma membrane of cardiomyocytes. Physiol. Rev. 92, 1317-1358
    • (2012) Physiol. Rev. , vol.92 , pp. 1317-1358
    • Balse, E.1    Steele, D.F.2    Abriel, H.3    Coulombe, A.4    Fedida, D.5    Hatem, S.N.6
  • 22
    • 0020075138 scopus 로고
    • Differentiation of rat myocytes in single cell cultures with and without proliferating nonmyocardial cells. Crossstriations, ultrastructure, and chronotropic response to isoproterenol
    • Simpson, P., and Savion, S. (1982) Differentiation of rat myocytes in single cell cultures with and without proliferating nonmyocardial cells. Crossstriations, ultrastructure, and chronotropic response to isoproterenol. Circ. Res. 50, 101-116
    • (1982) Circ. Res. , vol.50 , pp. 101-116
    • Simpson, P.1    Savion, S.2
  • 23
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy, A. K. (2001) Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24, 289-296
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 25
    • 0030780576 scopus 로고    scopus 로고
    • Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores
    • Subramanian, K., and Meyer, T. (1997) Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores. Cell 89, 963-971
    • (1997) Cell , vol.89 , pp. 963-971
    • Subramanian, K.1    Meyer, T.2
  • 26
    • 29344452247 scopus 로고    scopus 로고
    • Pleiotropic AT1 receptor signaling pathways mediating physiological and pathological actions of angiotensin II
    • Hunyady, L., and Catt, K. J. (2006) Pleiotropic AT1 receptor signaling pathways mediating physiological and pathological actions of angiotensin II. Mol. Endocrinol. 20, 953-970
    • (2006) Mol. Endocrinol. , vol.20 , pp. 953-970
    • Hunyady, L.1    Catt, K.J.2
  • 27
    • 81355137930 scopus 로고    scopus 로고
    • The ER in 3D. A multifunctional dynamic membrane network
    • Friedman, J. R., and Voeltz, G. K. (2011) The ER in 3D. A multifunctional dynamic membrane network. Trends Cell Biol. 21, 709-717
    • (2011) Trends Cell Biol. , vol.21 , pp. 709-717
    • Friedman, J.R.1    Voeltz, G.K.2
  • 28
    • 66349100683 scopus 로고    scopus 로고
    • Endoplasmic and sarcoplasmic reticulum in the heart
    • Michalak, M., and Opas, M. (2009) Endoplasmic and sarcoplasmic reticulum in the heart. Trends Cell Biol. 19, 253-259
    • (2009) Trends Cell Biol. , vol.19 , pp. 253-259
    • Michalak, M.1    Opas, M.2
  • 30
    • 0025210005 scopus 로고
    • Calcium-sensitive delayed rectifier potassium current in guinea pig ventricular cells
    • Tohse, N. (1990) Calcium-sensitive delayed rectifier potassium current in guinea pig ventricular cells. Am. J. Physiol. 258, H1200-H1207
    • (1990) Am. J. Physiol. , vol.258
    • Tohse, N.1
  • 31
    • 33646810883 scopus 로고    scopus 로고
    • Calmodulin is essential for cardiac IKs channel gating and assembly. Impaired function in long-QT mutations
    • Shamgar, L., Ma, L., Schmitt, N., Haitin, Y., Peretz, A., Wiener, R., Hirsch, J., Pongs, O., and Attali, B. (2006) Calmodulin is essential for cardiac IKs channel gating and assembly. Impaired function in long-QT mutations. Circ. Res. 98, 1055-1063
    • (2006) Circ. Res. , vol.98 , pp. 1055-1063
    • Shamgar, L.1    Ma, L.2    Schmitt, N.3    Haitin, Y.4    Peretz, A.5    Wiener, R.6    Hirsch, J.7    Pongs, O.8    Attali, B.9
  • 35
    • 73049088536 scopus 로고    scopus 로고
    • Augmented potassium current is a shared phenotype for two genetic defects associated with familial atrial fibrillation
    • Abraham, R. L., Yang, T., Blair, M., Roden, D. M., and Darbar, D. (2010) Augmented potassium current is a shared phenotype for two genetic defects associated with familial atrial fibrillation. J. Mol. Cell Cardiol. 48, 181-190
    • (2010) J. Mol. Cell Cardiol. , vol.48 , pp. 181-190
    • Abraham, R.L.1    Yang, T.2    Blair, M.3    Roden, D.M.4    Darbar, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.