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Volumn 314, Issue 5, 2008, Pages 1177-1191

Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes

Author keywords

Actin; Heart; Kelch; Myofibrillogenesis; Myosin; actinin

Indexed keywords

CYTOSKELETON PROTEIN; DETERGENT; PROTEIN KRP1; UNCLASSIFIED DRUG;

EID: 39649095167     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.12.009     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 0033961690 scopus 로고    scopus 로고
    • The kelch repeat superfamily of proteins: propellers of cell function
    • Adams J., Kelso R., and Cooley L. The kelch repeat superfamily of proteins: propellers of cell function. Trends Cell Biol. 10 (2000) 17-24
    • (2000) Trends Cell Biol. , vol.10 , pp. 17-24
    • Adams, J.1    Kelso, R.2    Cooley, L.3
  • 2
    • 8544277232 scopus 로고    scopus 로고
    • The BACK domain in BTB-kelch proteins
    • Stogios P.J., and Prive G.G. The BACK domain in BTB-kelch proteins. Trends Biochem. Sci. 29 (2004) 634-637
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 634-637
    • Stogios, P.J.1    Prive, G.G.2
  • 3
    • 2942606074 scopus 로고    scopus 로고
    • Molecular phylogeny of the kelch-repeat superfamily reveals an expansion of BTB/kelch proteins in animals
    • Prag S., and Adams J.C. Molecular phylogeny of the kelch-repeat superfamily reveals an expansion of BTB/kelch proteins in animals. BMC Bioinformatics 4 (2003) 42
    • (2003) BMC Bioinformatics , vol.4 , pp. 42
    • Prag, S.1    Adams, J.C.2
  • 4
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa M., and Xiong Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol. Cell. Biol. 25 (2005) 162-171
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 5
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase
    • Cullinan S.B., Gordan J.D., Jin J., Harper J.W., and Diehl J.A. The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase. Mol. Cell. Biol. 24 (2004) 8477-8486
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 6
    • 33645714061 scopus 로고    scopus 로고
    • The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation
    • Angers S., Thorpe C.J., Biechele T.L., Goldenberg S.J., Zheng N., MacCoss M.J., and Moon R.T. The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation. Nat. Cell Biol. 8 (2006) 348-357
    • (2006) Nat. Cell Biol. , vol.8 , pp. 348-357
    • Angers, S.1    Thorpe, C.J.2    Biechele, T.L.3    Goldenberg, S.J.4    Zheng, N.5    MacCoss, M.J.6    Moon, R.T.7
  • 7
    • 14844282064 scopus 로고    scopus 로고
    • Process elongation of oligodendrocytes is promoted by the kelch-related actin-binding protein Mayven
    • Jiang S., Avraham H.K., Park S.Y., Kim T.A., Bu X., Seng S., and Avraham S. Process elongation of oligodendrocytes is promoted by the kelch-related actin-binding protein Mayven. J. Neurochem. 92 (2005) 1191-1203
    • (2005) J. Neurochem. , vol.92 , pp. 1191-1203
    • Jiang, S.1    Avraham, H.K.2    Park, S.Y.3    Kim, T.A.4    Bu, X.5    Seng, S.6    Avraham, S.7
  • 8
    • 33748189401 scopus 로고    scopus 로고
    • Overexpression of kelch domain containing-2 (mKlhdc2) inhibits differentiation and directed migration of C2C12 myoblasts
    • Neuhaus P., Jaschinsky B., Schneider S., Neuhaus H., Wolter A., Ebelt H., and Braun T. Overexpression of kelch domain containing-2 (mKlhdc2) inhibits differentiation and directed migration of C2C12 myoblasts. Exp. Cell Res. 312 (2006) 3049-3059
    • (2006) Exp. Cell Res. , vol.312 , pp. 3049-3059
    • Neuhaus, P.1    Jaschinsky, B.2    Schneider, S.3    Neuhaus, H.4    Wolter, A.5    Ebelt, H.6    Braun, T.7
  • 10
    • 0034594913 scopus 로고    scopus 로고
    • Krp1, a novel kelch related protein that is involved in pseudopod elongation in transformed cells
    • Spence H.J., Johnston I., Ewart K., Buchanan S.J., Fitzgerald U., and Ozanne B.W. Krp1, a novel kelch related protein that is involved in pseudopod elongation in transformed cells. Oncogene 19 (2000) 1266-1276
    • (2000) Oncogene , vol.19 , pp. 1266-1276
    • Spence, H.J.1    Johnston, I.2    Ewart, K.3    Buchanan, S.J.4    Fitzgerald, U.5    Ozanne, B.W.6
  • 12
    • 30644468046 scopus 로고    scopus 로고
    • AP-1 differentially expressed proteins Krp1 and fibronectin cooperatively enhance Rho-ROCK-independent mesenchymal invasion by altering the function, localization, and activity of nondifferentially expressed proteins
    • Spence H.J., McGarry L., Chew C.S., Carragher N.O., Scott-Carragher L.A., Yuan Z., Croft D.R., Olson M.F., Frame M., and Ozanne B.W. AP-1 differentially expressed proteins Krp1 and fibronectin cooperatively enhance Rho-ROCK-independent mesenchymal invasion by altering the function, localization, and activity of nondifferentially expressed proteins. Mol. Cell. Biol. 26 (2006) 1480-1495
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1480-1495
    • Spence, H.J.1    McGarry, L.2    Chew, C.S.3    Carragher, N.O.4    Scott-Carragher, L.A.5    Yuan, Z.6    Croft, D.R.7    Olson, M.F.8    Frame, M.9    Ozanne, B.W.10
  • 13
    • 0030820989 scopus 로고    scopus 로고
    • Complete cDNA sequence and tissue localization of N-RAP, a novel nebulin-related protein of striated muscle
    • Luo G., Zhang J.Q., Nguyen T.P., Herrera A.H., Paterson B., and Horowits R. Complete cDNA sequence and tissue localization of N-RAP, a novel nebulin-related protein of striated muscle. Cell Motil. Cytoskelet. 38 (1997) 75-90
    • (1997) Cell Motil. Cytoskelet. , vol.38 , pp. 75-90
    • Luo, G.1    Zhang, J.Q.2    Nguyen, T.P.3    Herrera, A.H.4    Paterson, B.5    Horowits, R.6
  • 14
    • 0037672668 scopus 로고    scopus 로고
    • New N-RAP-binding partners α-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly
    • Lu S., Carroll S.L., Herrera A.H., Ozanne B., and Horowits R. New N-RAP-binding partners α-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly. J. Cell Sci. 116 (2003) 2169-2178
    • (2003) J. Cell Sci. , vol.116 , pp. 2169-2178
    • Lu, S.1    Carroll, S.L.2    Herrera, A.H.3    Ozanne, B.4    Horowits, R.5
  • 15
    • 0034285043 scopus 로고    scopus 로고
    • To the heart of myofibril assembly
    • Gregorio C.C., and Antin P.B. To the heart of myofibril assembly. Trends Cell Biol. 10 (2000) 355-362
    • (2000) Trends Cell Biol. , vol.10 , pp. 355-362
    • Gregorio, C.C.1    Antin, P.B.2
  • 17
    • 0021749672 scopus 로고
    • The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes
    • Dlugosz A.A., Antin P.B., Nachmias V.T., and Holtzer H. The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes. J. Cell Biol. 99 (1984) 2268-2278
    • (1984) J. Cell Biol. , vol.99 , pp. 2268-2278
    • Dlugosz, A.A.1    Antin, P.B.2    Nachmias, V.T.3    Holtzer, H.4
  • 20
    • 0033013812 scopus 로고    scopus 로고
    • Myofibrillogenesis in the developing chicken heart: assembly of the z-disk, m-line and thick filaments
    • Ehler E., Rothen B.M., Hämmerle S.P., Komiyama M., and Perriard J.-C. Myofibrillogenesis in the developing chicken heart: assembly of the z-disk, m-line and thick filaments. J. Cell Sci. 112 (1999) 1529-1539
    • (1999) J. Cell Sci. , vol.112 , pp. 1529-1539
    • Ehler, E.1    Rothen, B.M.2    Hämmerle, S.P.3    Komiyama, M.4    Perriard, J.-C.5
  • 21
    • 0035034041 scopus 로고    scopus 로고
    • Assembly of thick, thin, and titin filaments in chick precardiac explants
    • Rudy D.E., Yatskievych T.A., Antin P.B., and Gregorio C.C. Assembly of thick, thin, and titin filaments in chick precardiac explants. Dev. Dyn. 221 (2001) 61-71
    • (2001) Dev. Dyn. , vol.221 , pp. 61-71
    • Rudy, D.E.1    Yatskievych, T.A.2    Antin, P.B.3    Gregorio, C.C.4
  • 22
    • 0033798497 scopus 로고    scopus 로고
    • Myofibrillogenesis and formation of cell contacts mediate the localization of N-RAP in cultured chick cardiomyocytes
    • Carroll S.L., and Horowits R. Myofibrillogenesis and formation of cell contacts mediate the localization of N-RAP in cultured chick cardiomyocytes. Cell Motil. Cytoskelet. 47 (2000) 63-76
    • (2000) Cell Motil. Cytoskelet. , vol.47 , pp. 63-76
    • Carroll, S.L.1    Horowits, R.2
  • 23
    • 17444401402 scopus 로고    scopus 로고
    • N-RAP expression during mouse heart development
    • Lu S., Borst D.E., and Horowits R. N-RAP expression during mouse heart development. Dev. Dyn. 233 (2005) 201-212
    • (2005) Dev. Dyn. , vol.233 , pp. 201-212
    • Lu, S.1    Borst, D.E.2    Horowits, R.3
  • 24
    • 0346656820 scopus 로고    scopus 로고
    • N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes
    • Carroll S., Lu S., Herrera A.H., and Horowits R. N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes. J. Cell Sci. 117 (2004) 105-114
    • (2004) J. Cell Sci. , vol.117 , pp. 105-114
    • Carroll, S.1    Lu, S.2    Herrera, A.H.3    Horowits, R.4
  • 25
    • 0035211075 scopus 로고    scopus 로고
    • Targeting and functional role of N-RAP, a nebulin-related LIM protein, during myofibril assembly in cultured chick cardiomyocytes
    • Carroll S.L., Herrera A.H., and Horowits R. Targeting and functional role of N-RAP, a nebulin-related LIM protein, during myofibril assembly in cultured chick cardiomyocytes. J. Cell Sci. 114 (2001) 4229-4238
    • (2001) J. Cell Sci. , vol.114 , pp. 4229-4238
    • Carroll, S.L.1    Herrera, A.H.2    Horowits, R.3
  • 26
    • 33746674413 scopus 로고    scopus 로고
    • Targeted disruption of N-RAP gene function by RNA interference: a role for N-RAP in myofibril organization
    • Dhume A., Lu S., and Horowits R. Targeted disruption of N-RAP gene function by RNA interference: a role for N-RAP in myofibril organization. Cell Motil. Cytoskelet. 63 (2006) 493-511
    • (2006) Cell Motil. Cytoskelet. , vol.63 , pp. 493-511
    • Dhume, A.1    Lu, S.2    Horowits, R.3
  • 28
    • 0022618497 scopus 로고
    • Development of ultrastructural specializations during the formation of acetylcholine receptor aggregates on cultured myotubes
    • Olek A.J., Ling A., and Daniels M.P. Development of ultrastructural specializations during the formation of acetylcholine receptor aggregates on cultured myotubes. J. Neurosci. 6 (1986) 487-497
    • (1986) J. Neurosci. , vol.6 , pp. 487-497
    • Olek, A.J.1    Ling, A.2    Daniels, M.P.3
  • 29
    • 0027986710 scopus 로고
    • Molecular organization of transverse tubule/sarcoplasmic reticulum junctions during development of excitation-contraction coupling in skeletal muscle
    • Flucher B.E., Andrews S.B., and Daniels M.P. Molecular organization of transverse tubule/sarcoplasmic reticulum junctions during development of excitation-contraction coupling in skeletal muscle. Mol. Biol. Cell 5 (1994) 1105-1118
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1105-1118
    • Flucher, B.E.1    Andrews, S.B.2    Daniels, M.P.3
  • 30
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • Song K.S., Scherer P.E., Tang Z., Okamoto T., Li S., Chafel M., Chu C., Kohtz D.S., and Lisanti M.P. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J. Biol. Chem. 271 (1996) 15160-15165
    • (1996) J. Biol. Chem. , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3    Okamoto, T.4    Li, S.5    Chafel, M.6    Chu, C.7    Kohtz, D.S.8    Lisanti, M.P.9
  • 31
    • 8844235617 scopus 로고    scopus 로고
    • The mitochondrial death pathway and cardiac myocyte apoptosis
    • Crow M.T., Mani K., Nam Y.J., and Kitsis R.N. The mitochondrial death pathway and cardiac myocyte apoptosis. Circ. Res. 95 (2004) 957-970
    • (2004) Circ. Res. , vol.95 , pp. 957-970
    • Crow, M.T.1    Mani, K.2    Nam, Y.J.3    Kitsis, R.N.4
  • 32
    • 0028303532 scopus 로고
    • Developmental pattern of ventricular atrial natriuretic peptide (ANP) expression in chronically hypoxic rats as an indicator of the hypertrophic process
    • McKenzie J.C., Kelley K.B., Merisko-Liversidge E.M., Kennedy J., and Klein R.M. Developmental pattern of ventricular atrial natriuretic peptide (ANP) expression in chronically hypoxic rats as an indicator of the hypertrophic process. J. Mol. Cell. Cardiol. 26 (1994) 753-767
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 753-767
    • McKenzie, J.C.1    Kelley, K.B.2    Merisko-Liversidge, E.M.3    Kennedy, J.4    Klein, R.M.5
  • 33
    • 0024604621 scopus 로고
    • Specific heart granules and natriuretic peptide in the developing myocardium of fetal and neonatal rats and hamsters
    • Navaratnam V., Woodward J.M., and Skepper J.N. Specific heart granules and natriuretic peptide in the developing myocardium of fetal and neonatal rats and hamsters. J. Anat. 163 (1989) 261-273
    • (1989) J. Anat. , vol.163 , pp. 261-273
    • Navaratnam, V.1    Woodward, J.M.2    Skepper, J.N.3
  • 34
    • 0028076161 scopus 로고
    • The IGF-1-IGF-1 receptor system modulates myocyte proliferation but not myocyte cellular hypertrophy in vitro
    • Kajstura J., Cheng W., Reiss K., and Anversa P. The IGF-1-IGF-1 receptor system modulates myocyte proliferation but not myocyte cellular hypertrophy in vitro. Exp. Cell Res. 215 (1994) 273-283
    • (1994) Exp. Cell Res. , vol.215 , pp. 273-283
    • Kajstura, J.1    Cheng, W.2    Reiss, K.3    Anversa, P.4
  • 36
    • 1242284573 scopus 로고    scopus 로고
    • Chaperone-mediated folding and assembly of myosin in striated muscle
    • Srikakulam R., and Winkelmann D.A. Chaperone-mediated folding and assembly of myosin in striated muscle. J. Cell Sci. 117 (2004) 641-652
    • (2004) J. Cell Sci. , vol.117 , pp. 641-652
    • Srikakulam, R.1    Winkelmann, D.A.2
  • 38
    • 0037455559 scopus 로고    scopus 로고
    • Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles
    • Bagnato P., Barone V., Giacomello E., Rossi D., and Sorrentino V. Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles. J. Cell Biol. 160 (2003) 245-253
    • (2003) J. Cell Biol. , vol.160 , pp. 245-253
    • Bagnato, P.1    Barone, V.2    Giacomello, E.3    Rossi, D.4    Sorrentino, V.5
  • 39
    • 4143108034 scopus 로고    scopus 로고
    • Dynamics of obscurin localization during differentiation and remodeling of cardiac myocytes: obscurin as an integrator of myofibrillar structure
    • Borisov A.B., Kontrogianni-Konstantopoulos A., Bloch R.J., Westfall M.V., and Russell M.W. Dynamics of obscurin localization during differentiation and remodeling of cardiac myocytes: obscurin as an integrator of myofibrillar structure. J. Histochem. Cytochem. 52 (2004) 1117-1127
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 1117-1127
    • Borisov, A.B.1    Kontrogianni-Konstantopoulos, A.2    Bloch, R.J.3    Westfall, M.V.4    Russell, M.W.5
  • 40
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • Young P., Ehler E., and Gautel M. Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J. Cell Biol. 154 (2001) 123-136
    • (2001) J. Cell Biol. , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 42
    • 32444435668 scopus 로고    scopus 로고
    • Essential role of obscurin in cardiac myofibrillogenesis and hypertrophic response: evidence from small interfering RNA-mediated gene silencing
    • Borisov A.B., Sutter S.B., Kontrogianni-Konstantopoulos A., Bloch R.J., Westfall M.V., and Russell M.W. Essential role of obscurin in cardiac myofibrillogenesis and hypertrophic response: evidence from small interfering RNA-mediated gene silencing. Histochem. Cell Biol. 125 (2006) 227-238
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 227-238
    • Borisov, A.B.1    Sutter, S.B.2    Kontrogianni-Konstantopoulos, A.3    Bloch, R.J.4    Westfall, M.V.5    Russell, M.W.6
  • 43
    • 4344717801 scopus 로고    scopus 로고
    • Sequential myofibrillar breakdown accompanies mitotic division of mammalian cardiomyocytes
    • Ahuja P., Perriard E., Perriard J.C., and Ehler E. Sequential myofibrillar breakdown accompanies mitotic division of mammalian cardiomyocytes. J. Cell Sci. 117 (2004) 3295-3306
    • (2004) J. Cell Sci. , vol.117 , pp. 3295-3306
    • Ahuja, P.1    Perriard, E.2    Perriard, J.C.3    Ehler, E.4
  • 44
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTB-kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., and Hannink M. Ubiquitination of Keap1, a BTB-kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J. Biol. Chem. 280 (2005) 30091-30099
    • (2005) J. Biol. Chem. , vol.280 , pp. 30091-30099
    • Zhang, D.D.1    Lo, S.C.2    Sun, Z.3    Habib, G.M.4    Lieberman, M.W.5    Hannink, M.6
  • 45
    • 20544438018 scopus 로고    scopus 로고
    • MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination
    • Witt S.H., Granzier H., Witt C.C., and Labeit S. MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination. J. Mol. Biol. 350 (2005) 713-722
    • (2005) J. Mol. Biol. , vol.350 , pp. 713-722
    • Witt, S.H.1    Granzier, H.2    Witt, C.C.3    Labeit, S.4


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