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Volumn 7, Issue 1, 2012, Pages

Trafficking-deficient G572R-hERG and E637K-hERG activate stress and clearance pathways in endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; COMPLEMENTARY DNA; POTASSIUM CHANNEL HERG; PROTEASOME; PROTEASOME INHIBITOR; UBIQUITIN; ACTIVATING TRANSCRIPTION FACTOR 6; ERG1 POTASSIUM CHANNEL; MUTANT PROTEIN;

EID: 84855380889     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029885     Document Type: Article
Times cited : (24)

References (26)
  • 1
    • 0033378863 scopus 로고    scopus 로고
    • Inherited long QT syndromes: a paradigm for understanding arrhythmogenesis
    • Roden DM, Spooner PM, (1999) Inherited long QT syndromes: a paradigm for understanding arrhythmogenesis. J Cardiovasc Electrophysiol 10: 1664-1683.
    • (1999) J Cardiovasc Electrophysiol , vol.10 , pp. 1664-1683
    • Roden, D.M.1    Spooner, P.M.2
  • 2
    • 38049146378 scopus 로고    scopus 로고
    • Clinical practice. Long-QT syndrome
    • Roden DM, (2008) Clinical practice. Long-QT syndrome. N Engl J Med 358: 169-176.
    • (2008) N Engl J Med , vol.358 , pp. 169-176
    • Roden, D.M.1
  • 3
    • 0028914969 scopus 로고
    • A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome
    • Curran ME, Splawski I, Timothy KW, Vincent GM, Green ED, et al. (1995) A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell 80: 795-803.
    • (1995) Cell , vol.80 , pp. 795-803
    • Curran, M.E.1    Splawski, I.2    Timothy, K.W.3    Vincent, G.M.4    Green, E.D.5
  • 4
    • 0029007356 scopus 로고
    • HERG, a human inward rectifier in the voltage-gated potassium channel family
    • Trudeau MC, Warmke JW, Ganetzky B, Robertson GA, (1995) HERG, a human inward rectifier in the voltage-gated potassium channel family. Science 269: 92-95.
    • (1995) Science , vol.269 , pp. 92-95
    • Trudeau, M.C.1    Warmke, J.W.2    Ganetzky, B.3    Robertson, G.A.4
  • 5
    • 0029002969 scopus 로고
    • A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel
    • Sanguinetti MC, Jiang C, Curran ME, Keating MT, (1995) A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel. Cell 81: 299-307.
    • (1995) Cell , vol.81 , pp. 299-307
    • Sanguinetti, M.C.1    Jiang, C.2    Curran, M.E.3    Keating, M.T.4
  • 6
    • 43049112043 scopus 로고    scopus 로고
    • Molecular aspects of the congenital and acquired Long QT Syndrome: clinical implications
    • Saenen JB, Vrints CJ, (2008) Molecular aspects of the congenital and acquired Long QT Syndrome: clinical implications. J Mol Cell Cardiol 44: 633-646.
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 633-646
    • Saenen, J.B.1    Vrints, C.J.2
  • 7
    • 17144415220 scopus 로고    scopus 로고
    • Compendium of cardiac channel mutations in 541 consecutive unrelated patients referred for long QT syndrome genetic testing
    • Tester DJ, Will ML, Haglund CM, Ackerman MJ, (2005) Compendium of cardiac channel mutations in 541 consecutive unrelated patients referred for long QT syndrome genetic testing. Heart Rhythm 2: 507-517.
    • (2005) Heart Rhythm , vol.2 , pp. 507-517
    • Tester, D.J.1    Will, M.L.2    Haglund, C.M.3    Ackerman, M.J.4
  • 8
    • 2442657712 scopus 로고    scopus 로고
    • Four potassium channel mutations account for 73% of the genetic spectrum underlying long-QT syndrome (LQTS) and provide evidence for a strong founder effect in Finland
    • Fodstad H, Swan H, Laitinen P, Piippo K, Paavonen K, et al. (2004) Four potassium channel mutations account for 73% of the genetic spectrum underlying long-QT syndrome (LQTS) and provide evidence for a strong founder effect in Finland. Ann Med 36 (Suppl 1): 53-63.
    • (2004) Ann Med , vol.36 , Issue.SUPPL. 1 , pp. 53-63
    • Fodstad, H.1    Swan, H.2    Laitinen, P.3    Piippo, K.4    Paavonen, K.5
  • 9
    • 0034609531 scopus 로고    scopus 로고
    • Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2
    • Splawski I, Shen J, Timothy KW, Lehmann MH, Priori S, et al. (2000) Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2. Circulation 102: 1178-1185.
    • (2000) Circulation , vol.102 , pp. 1178-1185
    • Splawski, I.1    Shen, J.2    Timothy, K.W.3    Lehmann, M.H.4    Priori, S.5
  • 10
    • 21444453337 scopus 로고    scopus 로고
    • Degradation of trafficking-defective long QT syndrome type II mutant channels by the ubiquitin-proteasome pathway
    • Gong Q, Keeney DR, Molinari M, Zhou Z, (2005) Degradation of trafficking-defective long QT syndrome type II mutant channels by the ubiquitin-proteasome pathway. J Biol Chem 280: 19419-19425.
    • (2005) J Biol Chem , vol.280 , pp. 19419-19425
    • Gong, Q.1    Keeney, D.R.2    Molinari, M.3    Zhou, Z.4
  • 11
    • 33645317063 scopus 로고    scopus 로고
    • hERG potassium channels and cardiac arrhythmia
    • Sanguinetti MC, Tristani-Firouzi M, (2006) hERG potassium channels and cardiac arrhythmia. Nature 440: 463-469.
    • (2006) Nature , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 12
    • 33644851751 scopus 로고    scopus 로고
    • Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism
    • Anderson CL, Delisle BP, Anson BD, Kilby JA, Will ML, et al. (2006) Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism. Circulation 113: 365-373.
    • (2006) Circulation , vol.113 , pp. 365-373
    • Anderson, C.L.1    Delisle, B.P.2    Anson, B.D.3    Kilby, J.A.4    Will, M.L.5
  • 13
    • 0033615646 scopus 로고    scopus 로고
    • Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects
    • Zhou Z, Gong Q, January CT, (1999) Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects. J Biol Chem 274: 31123-31126.
    • (1999) J Biol Chem , vol.274 , pp. 31123-31126
    • Zhou, Z.1    Gong, Q.2    January, C.T.3
  • 14
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H, Okada T, Haze K, Yanagi H, Yura T, et al. (2000) ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 20: 6755-6767.
    • (2000) Mol Cell Biol , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5
  • 15
    • 0043037253 scopus 로고    scopus 로고
    • Endoplasmic reticulum: a primary target in various acute disorders and degenerative diseases of the brain
    • Paschen W, (2003) Endoplasmic reticulum: a primary target in various acute disorders and degenerative diseases of the brain. Cell Calcium 34: 365-383.
    • (2003) Cell Calcium , vol.34 , pp. 365-383
    • Paschen, W.1
  • 16
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K, (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10: 3787-3799.
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 17
    • 0034871249 scopus 로고    scopus 로고
    • Endoproteolysis of the ER stress transducer ATF6 in the presence of functionally inactive presenilins
    • Steiner H, Winkler E, Shearman MS, Prywes R, Haass C, (2001) Endoproteolysis of the ER stress transducer ATF6 in the presence of functionally inactive presenilins. Neurobiol Dis 8: 717-722.
    • (2001) Neurobiol Dis , vol.8 , pp. 717-722
    • Steiner, H.1    Winkler, E.2    Shearman, M.S.3    Prywes, R.4    Haass, C.5
  • 18
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A, (2003) Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4: 181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 19
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A, (1999) Setting the standards: quality control in the secretory pathway. Science 286: 1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 20
    • 0036217325 scopus 로고    scopus 로고
    • Characterization of a novel missense mutation E637K in the pore-S6 loop of HERG in a patient with long QT syndrome
    • Hayashi K, Shimizu M, Ino H, Yamaguchi M, Mabuchi H, et al. (2002) Characterization of a novel missense mutation E637K in the pore-S6 loop of HERG in a patient with long QT syndrome. Cardiovasc Res 54: 67-76.
    • (2002) Cardiovasc Res , vol.54 , pp. 67-76
    • Hayashi, K.1    Shimizu, M.2    Ino, H.3    Yamaguchi, M.4    Mabuchi, H.5
  • 21
    • 77958604381 scopus 로고    scopus 로고
    • Novel characteristics of a trafficking-defective G572R-hERG channel linked to hereditary long QT syndrome
    • Lian J, Huang N, Zhou J, Ge S, Huang X, et al. (2010) Novel characteristics of a trafficking-defective G572R-hERG channel linked to hereditary long QT syndrome. Can J Cardiol 26: 417-422.
    • (2010) Can J Cardiol , vol.26 , pp. 417-422
    • Lian, J.1    Huang, N.2    Zhou, J.3    Ge, S.4    Huang, X.5
  • 22
    • 0032516934 scopus 로고    scopus 로고
    • HERG channel dysfunction in human long QT syndrome. Intracellular transport and functional defects
    • Zhou Z, Gong Q, Epstein ML, January CT, (1998) HERG channel dysfunction in human long QT syndrome. Intracellular transport and functional defects. J Biol Chem 273: 21061-21066.
    • (1998) J Biol Chem , vol.273 , pp. 21061-21066
    • Zhou, Z.1    Gong, Q.2    Epstein, M.L.3    January, C.T.4
  • 23
    • 3242717751 scopus 로고    scopus 로고
    • Pharmacological rescue of trafficking defective HERG channels formed by coassembly of wild-type and long QT mutant N470D subunits
    • Gong Q, Anderson CL, January CT, Zhou Z, (2004) Pharmacological rescue of trafficking defective HERG channels formed by coassembly of wild-type and long QT mutant N470D subunits. Am J Physiol Heart Circ Physiol 287: H652-658.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Gong, Q.1    Anderson, C.L.2    January, C.T.3    Zhou, Z.4
  • 25
    • 2542488276 scopus 로고    scopus 로고
    • Activation of mammalian unfolded protein response is compatible with the quality control system operating in the endoplasmic reticulum
    • Nadanaka S, Yoshida H, Kano F, Murata M, Mori K, (2004) Activation of mammalian unfolded protein response is compatible with the quality control system operating in the endoplasmic reticulum. Mol Biol Cell 15: 2537-2548.
    • (2004) Mol Biol Cell , vol.15 , pp. 2537-2548
    • Nadanaka, S.1    Yoshida, H.2    Kano, F.3    Murata, M.4    Mori, K.5
  • 26
    • 2442464375 scopus 로고    scopus 로고
    • Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG
    • Ficker E, Dennis AT, Wang L, Brown AM, (2003) Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG. Circ Res 92: e87-100.
    • (2003) Circ Res , vol.92
    • Ficker, E.1    Dennis, A.T.2    Wang, L.3    Brown, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.