메뉴 건너뛰기




Volumn 114, Issue 6, 2014, Pages 982-992

Role for myosin-V motor proteins in the selective delivery of Kv channel isoforms to the membrane surface of cardiac myocytes

Author keywords

arrhythmias; cardiac; connexin 43; heart; Kv1.5 potassium channel

Indexed keywords

CONNEXIN 43; MYOSIN V; MYOSIN VA; MYOSIN VB; PHALLOIDIN; POTASSIUM CHANNEL KV1.5; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG;

EID: 84897097835     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.114.302711     Document Type: Article
Times cited : (29)

References (68)
  • 1
    • 0030069247 scopus 로고    scopus 로고
    • Differences between outward currents of human atrial and subepicardial ventricular myocytes
    • Amos GJ, Wettwer E, Metzger F, Li Q, Himmel HM, Ravens U. Differences between outward currents of human atrial and subepicardial ventricular myocytes. J Physiol. 1996;491(Pt 1):31-50.
    • (1996) J Physiol. , vol.491 , Issue.PART 1 , pp. 31-50
    • Amos, G.J.1    Wettwer, E.2    Metzger, F.3    Li, Q.4    Himmel, H.M.5    Ravens, U.6
  • 2
    • 45849100896 scopus 로고    scopus 로고
    • Safety considerations in the pharmacological management of atrial fbrillation
    • Camm AJ. Safety considerations in the pharmacological management of atrial fbrillation. Int J Cardiol. 2008;127:299-306.
    • (2008) Int J Cardiol. , vol.127 , pp. 299-306
    • Camm, A.J.1
  • 3
    • 3042857292 scopus 로고    scopus 로고
    • Advances in antiarrhythmic drug treatment of atrial fbrillation: Where do we stand now?
    • Camm AJ, Savelieva I. Advances in antiarrhythmic drug treatment of atrial fbrillation: where do we stand now? Heart Rhythm. 2004;1:244-246.
    • (2004) Heart Rhythm. , vol.1 , pp. 244-246
    • Camm, A.J.1    Savelieva, I.2
  • 4
    • 0029082517 scopus 로고
    • Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue
    • Mays DJ, Foose JM, Philipson LH, Tamkun MM. Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue. J Clin Invest. 1995;96:282-292.
    • (1995) J Clin Invest. , vol.96 , pp. 282-292
    • Mays, D.J.1    Foose, J.M.2    Philipson, L.H.3    Tamkun, M.M.4
  • 6
    • 33645729137 scopus 로고    scopus 로고
    • Antiarrhythmic drugs for maintaining sinus rhythm after cardioversion of atrial fbrillation: A systematic review of randomized controlled trials
    • Lafuente-Lafuente C, Mouly S, Longás-Tejero MA, Mahé I, Bergmann JF. Antiarrhythmic drugs for maintaining sinus rhythm after cardioversion of atrial fbrillation: a systematic review of randomized controlled trials. Arch Intern Med. 2006;166:719-728.
    • (2006) Arch Intern Med. , vol.166 , pp. 719-728
    • Lafuente-Lafuente, C.1    Mouly, S.2    Longás-Tejero, M.A.3    Mahé, I.4    Bergmann, J.F.5
  • 7
    • 0031003283 scopus 로고    scopus 로고
    • Antisense oligodeoxynucleo-tides directed against Kv1.5 mRNA specifcally inhibit ultrarapid delayed rectifer K+ current in cultured adult human atrial myocytes
    • Feng J, Wible B, Li GR, Wang Z, Nattel S. Antisense oligodeoxynucleo- tides directed against Kv1.5 mRNA specifcally inhibit ultrarapid delayed rectifer K+ current in cultured adult human atrial myocytes. Circ Res. 1997;80:572-579.
    • (1997) Circ Res. , vol.80 , pp. 572-579
    • Feng, J.1    Wible, B.2    Li, G.R.3    Wang, Z.4    Nattel, S.5
  • 9
    • 33646852387 scopus 로고    scopus 로고
    • Over-expression of Kv1.5 in rat cardiomyocytes extremely shortens the duration of the action potential and causes rapid excitation
    • Tanabe Y, Hatada K, Naito N, Aizawa Y, Chinushi M, Nawa H, Aizawa Y. Over-expression of Kv1.5 in rat cardiomyocytes extremely shortens the duration of the action potential and causes rapid excitation. Biochem Biophys Res Commun. 2006;345:1116-1121.
    • (2006) Biochem Biophys Res Commun. , vol.345 , pp. 1116-1121
    • Tanabe, Y.1    Hatada, K.2    Naito, N.3    Aizawa, Y.4    Chinushi, M.5    Nawa, H.6    Aizawa, Y.7
  • 10
    • 0030949658 scopus 로고    scopus 로고
    • Outward K+ current densities and Kv1.5 expression are reduced in chronic human atrial fbrillation
    • Van Wagoner DR, Pond AL, McCarthy PM, Trimmer JS, Nerbonne JM. Outward K+ current densities and Kv1.5 expression are reduced in chronic human atrial fbrillation. Circ Res. 1997;80:772-781.
    • (1997) Circ Res. , vol.80 , pp. 772-781
    • Van Wagoner, D.R.1    Pond, A.L.2    McCarthy, P.M.3    Trimmer, J.S.4    Nerbonne, J.M.5
  • 11
    • 56149117926 scopus 로고    scopus 로고
    • New drugs targeting the cardiac ultra-rapid delayed-rectifer current (I Kur): Rationale, pharmacology and evidence for potential therapeutic value
    • Ford JW, Milnes JT. New drugs targeting the cardiac ultra-rapid delayed-rectifer current (I Kur): rationale, pharmacology and evidence for potential therapeutic value. J Cardiovasc Pharmacol. 2008;52:105-120.
    • (2008) J Cardiovasc Pharmacol. , vol.52 , pp. 105-120
    • Ford, J.W.1    Milnes, J.T.2
  • 17
    • 0029848995 scopus 로고    scopus 로고
    • Electrical remodeling in atrial fbril-lation. Time course and mechanisms
    • Goette A, Honeycutt C, Langberg JJ. Electrical remodeling in atrial fbril-lation. Time course and mechanisms. Circulation. 1996;94:2968-2974.
    • (1996) Circulation. , vol.94 , pp. 2968-2974
    • Goette, A.1    Honeycutt, C.2    Langberg, J.J.3
  • 18
    • 34547986066 scopus 로고    scopus 로고
    • Should i stay or should i go?': Myosin v function in organelle traffcking
    • Desnos C, Huet S, Darchen F. 'Should I stay or should I go?': myosin V function in organelle traffcking. Biol Cell. 2007;99:411-423.
    • (2007) Biol Cell. , vol.99 , pp. 411-423
    • Desnos, C.1    Huet, S.2    Darchen, F.3
  • 20
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range vesicle transport
    • Langford GM. Myosin-V, a versatile motor for short-range vesicle transport. Traffc. 2002;3:859-865.
    • (2002) Traffc. , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 21
    • 0033280225 scopus 로고    scopus 로고
    • Cooperation between microtubule-and actin-based motor proteins
    • Brown SS. Cooperation between microtubule-and actin-based motor proteins. Annu Rev Cell Dev Biol. 1999;15:63-80.
    • (1999) Annu Rev Cell Dev Biol. , vol.15 , pp. 63-80
    • Brown, S.S.1
  • 22
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science. 1998;279:519-526.
    • (1998) Science. , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 23
    • 70350501513 scopus 로고    scopus 로고
    • Single molecule imaging reveals differences in microtubule track selection between Kinesin motors
    • Cai D, McEwen DP, Martens JR, Meyhofer E, Verhey KJ. Single molecule imaging reveals differences in microtubule track selection between Kinesin motors. PLoS Biol. 2009;7:e1000216.
    • (2009) PLoS Biol. , vol.7
    • Cai, D.1    McEwen, D.P.2    Martens, J.R.3    Meyhofer, E.4    Verhey, K.J.5
  • 25
    • 24044494280 scopus 로고    scopus 로고
    • Kv1.5 surface expression is modulated by retrograde traffcking of newly endocytosed channels by the dynein motor
    • Choi WS, Khurana A, Mathur R, Viswanathan V, Steele DF, Fedida D. Kv1.5 surface expression is modulated by retrograde traffcking of newly endocytosed channels by the dynein motor. Circ Res. 2005;97:363-371.
    • (2005) Circ Res. , vol.97 , pp. 363-371
    • Choi, W.S.1    Khurana, A.2    Mathur, R.3    Viswanathan, V.4    Steele, D.F.5    Fedida, D.6
  • 27
    • 0036156336 scopus 로고    scopus 로고
    • Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein ty-rosine phosphatase requires an intact cytoskeleton
    • Mason HS, Latten MJ, Godoy LD, Horowitz B, Kenyon JL. Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein ty-rosine phosphatase requires an intact cytoskeleton. Mol Pharmacol. 2002;61:285-293.
    • (2002) Mol Pharmacol. , vol.61 , pp. 285-293
    • Mason, H.S.1    Latten, M.J.2    Godoy, L.D.3    Horowitz, B.4    Kenyon, J.L.5
  • 29
    • 0034640199 scopus 로고    scopus 로고
    • Fedida D. Alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells
    • Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D. alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Lett. 2000;473:188-194.
    • (2000) FEBS Lett. , vol.473 , pp. 188-194
    • Maruoka, N.D.1    Steele, D.F.2    Au, B.P.3    Dan, P.4    Zhang, X.5    Moore, E.D.6
  • 30
    • 0037966553 scopus 로고    scopus 로고
    • SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism
    • Eldstrom J, Choi WS, Steele DF, Fedida D. SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism. FEBS Lett. 2003;547:205-211.
    • (2003) FEBS Lett. , vol.547 , pp. 205-211
    • Eldstrom, J.1    Choi, W.S.2    Steele, D.F.3    Fedida, D.4
  • 31
  • 33
    • 0035370622 scopus 로고    scopus 로고
    • A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2
    • Cukovic D, Lu GW, Wible B, Steele DF, Fedida D. A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2. FEBS Lett. 2001;498:87-92.
    • (2001) FEBS Lett. , vol.498 , pp. 87-92
    • Cukovic, D.1    Lu, G.W.2    Wible, B.3    Steele, D.F.4    Fedida, D.5
  • 34
    • 79958007658 scopus 로고    scopus 로고
    • Cortactin is required for N-cadherin regulation of Kv1.5 channel function
    • Cheng L, Yung A, Covarrubias M, Radice GL. Cortactin is required for N-cadherin regulation of Kv1.5 channel function. J Biol Chem. 2011;286:20478-20489.
    • (2011) J Biol Chem. , vol.286 , pp. 20478-20489
    • Cheng, L.1    Yung, A.2    Covarrubias, M.3    Radice, G.L.4
  • 36
    • 84862784582 scopus 로고    scopus 로고
    • Actin cytoskeleton rest stops regulate anterograde traffc of connexin 43 vesicles to the plasma membrane
    • Smyth JW, Vogan JM, Buch PJ, Zhang SS, Fong TS, Hong TT, Shaw RM. Actin cytoskeleton rest stops regulate anterograde traffc of connexin 43 vesicles to the plasma membrane. Circ Res. 2012;110:978-989.
    • (2012) Circ Res. , vol.110 , pp. 978-989
    • Smyth, J.W.1    Vogan, J.M.2    Buch, P.J.3    Zhang, S.S.4    Fong, T.S.5    Hong, T.T.6    Shaw, R.M.7
  • 38
  • 41
    • 84887608899 scopus 로고    scopus 로고
    • Autoregulation of connexin43 gap junction formation by internally translated isoforms
    • Smyth JW, Shaw RM. Autoregulation of connexin43 gap junction formation by internally translated isoforms. Cell Rep. 2013;5:611-618.
    • (2013) Cell Rep. , vol.5 , pp. 611-618
    • Smyth, J.W.1    Shaw, R.M.2
  • 43
    • 0037832404 scopus 로고    scopus 로고
    • Myosin v walks hand-over-hand: Single fuorophore imaging with 1.5-nm localization
    • Yildiz A, Forkey JN, McKinney SA, Ha T, Goldman YE, Selvin PR. Myosin V walks hand-over-hand: single fuorophore imaging with 1.5-nm localization. Science. 2003;300:2061-2065.
    • (2003) Science. , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 45
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale RD, Milligan RA. The way things move: looking under the hood of molecular motor proteins. Science. 2000;288:88-95.
    • (2000) Science. , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 47
    • 4644314874 scopus 로고    scopus 로고
    • Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis
    • Song BD, Leonard M, Schmid SL. Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis. J Biol Chem. 2004;279:40431-40436.
    • (2004) J Biol Chem. , vol.279 , pp. 40431-40436
    • Song, B.D.1    Leonard, M.2    Schmid, S.L.3
  • 48
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich O, Reinsch S, Urbé S, Zerial M, Parton RG. Rab11 regulates recycling through the pericentriolar recycling endosome. J Cell Biol. 1996;135:913-924.
    • (1996) J Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbé, S.3    Zerial, M.4    Parton, R.G.5
  • 49
    • 0032568657 scopus 로고    scopus 로고
    • Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes
    • Ren M, Xu G, Zeng J, De Lemos-Chiarandini C, Adesnik M, Sabatini DD. Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes. Proc Natl Acad Sci USA. 1998;95:6187-6192.
    • (1998) Proc Natl Acad Sci USA. , vol.95 , pp. 6187-6192
    • Ren, M.1    Xu, G.2    Zeng, J.3    De Lemos-Chiarandini, C.4    Adesnik, M.5    Sabatini, D.D.6
  • 51
    • 33645071056 scopus 로고    scopus 로고
    • CFTR, chloride concentration and cell volume: Could mammalian protein histidine phosphorylation play a latent role?
    • Treharne KJ, Crawford RM, Mehta A. CFTR, chloride concentration and cell volume: could mammalian protein histidine phosphorylation play a latent role? Exp Physiol. 2006;91:131-139.
    • (2006) Exp Physiol. , vol.91 , pp. 131-139
    • Treharne, K.J.1    Crawford, R.M.2    Mehta, A.3
  • 55
    • 34347236923 scopus 로고    scopus 로고
    • Mechanisms of cardiac potassium channel traffcking
    • Steele DF, Eldstrom J, Fedida D. Mechanisms of cardiac potassium channel traffcking. J Physiol. 2007;582:17-26.
    • (2007) J Physiol. , vol.582 , pp. 17-26
    • Steele, D.F.1    Eldstrom, J.2    Fedida, D.3
  • 56
    • 0034627836 scopus 로고    scopus 로고
    • PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering
    • Tiffany AM, Manganas LN, Kim E, Hsueh YP, Sheng M, Trimmer JS. PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering. J Cell Biol. 2000;148:147-158.
    • (2000) J Cell Biol. , vol.148 , pp. 147-158
    • Tiffany, A.M.1    Manganas, L.N.2    Kim, E.3    Hsueh, Y.P.4    Sheng, M.5    Trimmer, J.S.6
  • 57
    • 2442515348 scopus 로고    scopus 로고
    • A multiprotein traffcking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifer Kir2 potassium channels
    • Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA. A multiprotein traffcking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifer Kir2 potassium channels. J Biol Chem. 2004;279:19051-19063.
    • (2004) J Biol Chem. , vol.279 , pp. 19051-19063
    • Leonoudakis, D.1    Conti, L.R.2    Radeke, C.M.3    McGuire, L.M.4    Vandenberg, C.A.5
  • 58
    • 0034548877 scopus 로고    scopus 로고
    • Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein flamin
    • Petrecca K, Miller DM, Shrier A. Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein flamin. J Neurosci. 2000;20:8736-8744.
    • (2000) J Neurosci. , vol.20 , pp. 8736-8744
    • Petrecca, K.1    Miller, D.M.2    Shrier, A.3
  • 59
    • 0037064067 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin
    • Hattan D, Nesti E, Cachero TG, Morielli AD. Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin. J Biol Chem. 2002;277:38596-38606.
    • (2002) J Biol Chem. , vol.277 , pp. 38596-38606
    • Hattan, D.1    Nesti, E.2    Cachero, T.G.3    Morielli, A.D.4
  • 60
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions
    • Shaw RM, Fay AJ, Puthenveedu MA, von Zastrow M, Jan YN, Jan LY. Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions. Cell. 2007;128:547-560.
    • (2007) Cell. , vol.128 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3    Von Zastrow, M.4    Jan, Y.N.5    Jan, L.Y.6
  • 63
    • 2442480250 scopus 로고    scopus 로고
    • Calpain inhibition prevents pacing-induced cellular remodeling in a HL-1 myocyte model for atrial fbrillation
    • Brundel BJ, Kampinga HH, Henning RH. Calpain inhibition prevents pacing-induced cellular remodeling in a HL-1 myocyte model for atrial fbrillation. Cardiovasc Res. 2004;62:521-528.
    • (2004) Cardiovasc Res. , vol.62 , pp. 521-528
    • Brundel, B.J.1    Kampinga, H.H.2    Henning, R.H.3
  • 65
    • 0032498523 scopus 로고    scopus 로고
    • Breakdown and release of myoflament proteins during ischemia and ischemia/reper-fusion in rat hearts: Identifcation of degradation products and effects on the pCa-force relation
    • Van Eyk JE, Powers F, Law W, Larue C, Hodges RS, Solaro RJ. Breakdown and release of myoflament proteins during ischemia and ischemia/reper-fusion in rat hearts: identifcation of degradation products and effects on the pCa-force relation. Circ Res. 1998;82:261-271.
    • (1998) Circ Res. , vol.82 , pp. 261-271
    • Van Eyk, J.E.1    Powers, F.2    Law, W.3    Larue, C.4    Hodges, R.S.5    Solaro, R.J.6
  • 66
    • 0029845682 scopus 로고    scopus 로고
    • Inhomogeneous disappearance of myoflament-related cyto-skeletal proteins in stunned myocardium of guinea pig
    • Matsumura Y, Saeki E, Inoue M, Hori M, Kamada T, Kusuoka H. Inhomogeneous disappearance of myoflament-related cyto-skeletal proteins in stunned myocardium of guinea pig. Circ Res. 1996;79:447-454.
    • (1996) Circ Res. , vol.79 , pp. 447-454
    • Matsumura, Y.1    Saeki, E.2    Inoue, M.3    Hori, M.4    Kamada, T.5    Kusuoka, H.6
  • 67
    • 0025868336 scopus 로고
    • Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain
    • Goll DE, Dayton WR, Singh I, Robson RM. Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain. J Biol Chem. 1991;266:8501-8510.
    • (1991) J Biol Chem. , vol.266 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.