메뉴 건너뛰기




Volumn 18, Issue 3, 1998, Pages 1580-1589

The Rho family G proteins play a critical role in muscle differentiation

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MESSENGER RNA; MYOGENIN;

EID: 0031910828     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.3.1580     Document Type: Article
Times cited : (134)

References (94)
  • 1
    • 0028176713 scopus 로고
    • p21 Ras as a governor of global gene expression
    • Abdellatif, M., W. R. MacLellan, and M. D. Schneider. 1994. p21 Ras as a governor of global gene expression. J. Biol. Chem. 269:15423-15426.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15423-15426
    • Abdellatif, M.1    MacLellan, W.R.2    Schneider, M.D.3
  • 3
    • 0020459571 scopus 로고
    • Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro
    • Bader, D., T. Masaki, and D. A. Fischman. 1982. Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro. J. Cell Biol. 95:763-770.
    • (1982) J. Cell Biol. , vol.95 , pp. 763-770
    • Bader, D.1    Masaki, T.2    Fischman, D.A.3
  • 4
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia, S., B. Derijard, R. J. Davis, and R. A. Cerione. 1995. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J. Biol. Chem. 270:27995-27998.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Derijard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 5
    • 0028796735 scopus 로고
    • The mouse MRF4 promoter is trans-activated directly and indirectly by muscle-specific transcription factors
    • Black, B. L., J. F. Martin, and E. N. Olson. 1995. The mouse MRF4 promoter is trans-activated directly and indirectly by muscle-specific transcription factors. J. Biol. Chem. 270:2889-2892.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2889-2892
    • Black, B.L.1    Martin, J.F.2    Olson, E.N.3
  • 7
    • 0024453704 scopus 로고
    • A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts
    • Braun, T., G. Buschhausen-Denker, E. Bober, E. Tannich, and H. H. Arnold. 1989. A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts. EMBO J. 8:701-709.
    • (1989) EMBO J. , vol.8 , pp. 701-709
    • Braun, T.1    Buschhausen-Denker, G.2    Bober, E.3    Tannich, E.4    Arnold, H.H.5
  • 8
    • 0025098314 scopus 로고
    • Myf-6, a new member of the human gene family of myogenic determination factors: Evidence for a gene cluster on chromosome
    • Braun, T., E. Bober, N. Winter, R. Rosenthal, and H. H. Arnold. 1990. Myf-6, a new member of the human gene family of myogenic determination factors: evidence for a gene cluster on chromosome. EMBO J. 9:821-831.
    • (1990) EMBO J. , vol.9 , pp. 821-831
    • Braun, T.1    Bober, E.2    Winter, N.3    Rosenthal, R.4    Arnold, H.H.5
  • 9
    • 0025909860 scopus 로고
    • Transforming growth factor β represses the actions of myogenin through a mechanism independent of DNA binding
    • Brennan, T. J., D. G. Edmondson, L. Li, and E. N. Olson. 1991. Transforming growth factor β represses the actions of myogenin through a mechanism independent of DNA binding. Proc. Natl. Acad. Sci. USA 88:3822-3826.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3822-3826
    • Brennan, T.J.1    Edmondson, D.G.2    Li, L.3    Olson, E.N.4
  • 10
    • 0028287953 scopus 로고
    • The myogenin gene is activated during myocyte differentiation by pre-existing, not newly synthesized transcription factor MEF-2
    • Buchberger, A., K. Ragge, and H. H. Arnold. 1994. The myogenin gene is activated during myocyte differentiation by pre-existing, not newly synthesized transcription factor MEF-2. J. Biol. Chem. 269:17289-17296.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17289-17296
    • Buchberger, A.1    Ragge, K.2    Arnold, H.H.3
  • 11
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P., P. Boquet, P. Maduale, M. R. Popoff, E. J. Rubin, and D. M. Gill. 1989. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8:1087-1092.
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Maduale, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 12
    • 0027226234 scopus 로고
    • Separable regulatory elements governing myogenin transcription in mouse embryogenesis
    • Cheng, T.-C., M. C. Wallace, J. P. Merlie, and E. N. Olson. 1993. Separable regulatory elements governing myogenin transcription in mouse embryogenesis. Science 261:215-218.
    • (1993) Science , vol.261 , pp. 215-218
    • Cheng, T.-C.1    Wallace, M.C.2    Merlie, J.P.3    Olson, E.N.4
  • 13
    • 0029890229 scopus 로고    scopus 로고
    • The 70 kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1
    • Chou, M. M., and J. Blenis. 1996. The 70 kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1. Cell 85:573-583.
    • (1996) Cell , vol.85 , pp. 573-583
    • Chou, M.M.1    Blenis, J.2
  • 14
    • 0025173793 scopus 로고
    • A combination of closely associated positive and negative cis-acting promoter elements regulates transcription of the skeletal alpha-actin gene
    • Chow, K. L., and R. J. Schwartz. 1990. A combination of closely associated positive and negative cis-acting promoter elements regulates transcription of the skeletal alpha-actin gene. Mol. Cell. Biol. 10:528-538.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 528-538
    • Chow, K.L.1    Schwartz, R.J.2
  • 15
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso, O. A., M. Chiariello, J.-C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and J. S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81:1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.-C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 16
    • 0025943376 scopus 로고
    • Myogenin induces muscle-specific enhancer binding factor MEF-2 independently of other muscle-specific gene products
    • Cserjesi, P., and E. N. Olson. 1991. Myogenin induces muscle-specific enhancer binding factor MEF-2 independently of other muscle-specific gene products. Mol. Cell. Biol. 11:4854-4862.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4854-4862
    • Cserjesi, P.1    Olson, E.N.2
  • 17
    • 0023663888 scopus 로고
    • Expression of a single transfected cDNA converts fibroblasts to myoblasts
    • Davis, R. L., H. Weintraub, and A. B. Lassar. 1987. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 51:987-1000.
    • (1987) Cell , vol.51 , pp. 987-1000
    • Davis, R.L.1    Weintraub, H.2    Lassar, A.B.3
  • 18
    • 0024673511 scopus 로고
    • A gene with homology to the myc similarity region of MyoD1 is expressed during myogenesis and is sufficient to activate the muscle differentiation program
    • Edmondson, D. G., and E. N. Olson. 1989. A gene with homology to the myc similarity region of MyoD1 is expressed during myogenesis and is sufficient to activate the muscle differentiation program. Genes Dev. 3:628-640.
    • (1989) Genes Dev. , vol.3 , pp. 628-640
    • Edmondson, D.G.1    Olson, E.N.2
  • 19
    • 0026673591 scopus 로고
    • Analysis of the myogenin promoter reveals an indirect pathway for positive autoregulation mediated by the muscle-specific enhancer factor MEF-2
    • Edmondson, D. G., T.-C. Cheng, P. Cserjesi, T. Chakraborty, and E. N. Olson. 1992. Analysis of the myogenin promoter reveals an indirect pathway for positive autoregulation mediated by the muscle-specific enhancer factor MEF-2. Mol. Cell. Biol. 12:3665-3677.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3665-3677
    • Edmondson, D.G.1    Cheng, T.-C.2    Cserjesi, P.3    Chakraborty, T.4    Olson, E.N.5
  • 20
    • 0026795509 scopus 로고
    • SV40 large T inhibits myogenic differentiation partially through inducing c-jun
    • Endo, T. 1992. SV40 large T inhibits myogenic differentiation partially through inducing c-jun. J. Biochem. 112:321-329.
    • (1992) J. Biochem. , vol.112 , pp. 321-329
    • Endo, T.1
  • 21
    • 0027481216 scopus 로고
    • Alpha 5 integrin is a critical component of adhesion plaques in myogenesis
    • Enomoto, M. I., D. Boettiger, and A. S. Menko. 1993. Alpha 5 integrin is a critical component of adhesion plaques in myogenesis. Dev. Biol. 155:180-197.
    • (1993) Dev. Biol. , vol.155 , pp. 180-197
    • Enomoto, M.I.1    Boettiger, D.2    Menko, A.S.3
  • 22
    • 0025073547 scopus 로고
    • Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-hinding proteins
    • Fukumoto, Y., K. Kaibuchi, Y. Hori, H. Fujioka, S. Araki, T. Ueda, A. Kikuchi, and Y. Takai. 1990. Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-hinding proteins. Oncogene 5:1321-1328.
    • (1990) Oncogene , vol.5 , pp. 1321-1328
    • Fukumoto, Y.1    Kaibuchi, K.2    Hori, Y.3    Fujioka, H.4    Araki, S.5    Ueda, T.6    Kikuchi, A.7    Takai, Y.8
  • 23
    • 0024366273 scopus 로고
    • A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes
    • Gossett, L. A., D. J. Kelvin, E. A. Sternberg, and E. N. Olson. 1989. A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes. Mol. Cell. Biol. 9:5022-5033.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5022-5033
    • Gossett, L.A.1    Kelvin, D.J.2    Sternberg, E.A.3    Olson, E.N.4
  • 24
    • 0029868335 scopus 로고    scopus 로고
    • Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins
    • Groisman, R., H. Masutani, M. P. Leibovitch, P. Robin, I. Soudant, D. Trouche, and A. Harel-Bellan. 1996. Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. J. Biol. Chem. 271:5258-5264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5258-5264
    • Groisman, R.1    Masutani, H.2    Leibovitch, M.P.3    Robin, P.4    Soudant, I.5    Trouche, D.6    Harel-Bellan, A.7
  • 25
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. 1994. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10:31-54.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 26
    • 0027258162 scopus 로고
    • Muscle deficiency and neonatal death in mice with a targetted mutation in the myogenin gene
    • Hasty, P., A. Bradley, J. H. Morris, D. G. Edmondson, J. M. Venuti, E. N. Olson, and W. H. Klein. 1993. Muscle deficiency and neonatal death in mice with a targetted mutation in the myogenin gene. Nature 364:501-506.
    • (1993) Nature , vol.364 , pp. 501-506
    • Hasty, P.1    Bradley, A.2    Morris, J.H.3    Edmondson, D.G.4    Venuti, J.M.5    Olson, E.N.6    Klein, W.H.7
  • 28
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill, C. S., J. Wynne, and R. Treisman. 1995. The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 81:1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 30
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP-ribosylation of the small GTP-binding protein Rho
    • Jalink, K., E. J. van Corven, T. Hengeveld, N. Morii, S. Narumiya, and W. H. Moolenaar. 1994. Inhibition of lysophosphatidate-and thrombin-induced neurite retraction and neuronal cell rounding by ADP-ribosylation of the small GTP-binding protein Rho. J. Cell Biol. 126:801-810.
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 31
    • 0028047014 scopus 로고
    • Activation of the myogenic lineage by MEF2A, a factor that induces and cooperates with MyoD
    • Kaushal, S., J. W. Schneider, B. Nadal-Ginard, and V. Mahdavi. 1994. Activation of the myogenic lineage by MEF2A, a factor that induces and cooperates with MyoD. Science 266:1236-1240.
    • (1994) Science , vol.266 , pp. 1236-1240
    • Kaushal, S.1    Schneider, J.W.2    Nadal-Ginard, B.3    Mahdavi, V.4
  • 32
    • 0028072097 scopus 로고
    • Blasticidin S deaminase gene from Aspergillus terreus (BSD): A new drug resistance gene for transfection of mammalian cells
    • Kimura, M., A. Takatsuki, and I. Yamaguchi. 1994. Blasticidin S deaminase gene from Aspergillus terreus (BSD): a new drug resistance gene for transfection of mammalian cells. Biochim. Biophys. Acta 1219:653-659.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 653-659
    • Kimura, M.1    Takatsuki, A.2    Yamaguchi, I.3
  • 33
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/ GTP exchange protein (rho GDI)
    • Kishi, K., T. Sasaki, S. Kuroda, T. Itoh, and Y. Takai. 1993. Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/ GTP exchange protein (rho GDI). J. Cell Biol. 120:1187-1195.
    • (1993) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 34
    • 0028980337 scopus 로고
    • Val inhibits myogenesis without altering the DNA binding or transcriptional activities of the myogenic basic helix-loop-helix factors
    • Val inhibits myogenesis without altering the DNA binding or transcriptional activities of the myogenic basic helix-loop-helix factors. Mol. Cell. Biol. 15:5205-5213.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5205-5213
    • Kong, Y.1    Johnson, S.E.2    Taparowsky, E.J.3    Konieczny, S.F.4
  • 35
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., S. Ahmed, A. Best, and L. Lim. 1995. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 36
    • 0024370528 scopus 로고
    • Transformation by activated ras or fos prevents myogenesis by inhibiting expression of MyoD1
    • Lassar, A. B., M. J. Thayer, R. W. Overell, and H. Weintraub. 1989. Transformation by activated ras or fos prevents myogenesis by inhibiting expression of MyoD1. Cell 58:659-667.
    • (1989) Cell , vol.58 , pp. 659-667
    • Lassar, A.B.1    Thayer, M.J.2    Overell, R.W.3    Weintraub, H.4
  • 37
    • 0027049533 scopus 로고
    • FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains
    • Li, L., J. Zhou, G. James, R. Heller-Harrison, M. P. Czech, and E. N. Olson. 1992. FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains. Cell 71:1181-1194.
    • (1992) Cell , vol.71 , pp. 1181-1194
    • Li, L.1    Zhou, J.2    James, G.3    Heller-Harrison, R.4    Czech, M.P.5    Olson, E.N.6
  • 38
    • 0028917564 scopus 로고
    • Requirement of MADS domain transcription factor D-MEF2 for muscle formation in Drosophila
    • Lilly, B., B. Zhao, G. Ranganayakulu, B. M. Paterson, R. A. Schulz, and E. N. Olson. 1995. Requirement of MADS domain transcription factor D-MEF2 for muscle formation in Drosophila. Science 267:688-693.
    • (1995) Science , vol.267 , pp. 688-693
    • Lilly, B.1    Zhao, B.2    Ranganayakulu, G.3    Paterson, B.M.4    Schulz, R.A.5    Olson, E.N.6
  • 39
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi, I., Y. Hamaguchi, H. Fujimoto, N. Morii, M. Mishima, and S. Narumiya. 1993. A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote 1:325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 40
    • 0029054218 scopus 로고
    • The role of the CANNTG promoter element (E box) and the myocyte-enhancer-binding-factor-2 (MEF-2) site in the transcriptional regulation of the chick myogenin gene
    • Malik, S., C.-F. Huang, and J. Schmidt. 1995. The role of the CANNTG promoter element (E box) and the myocyte-enhancer-binding-factor-2 (MEF-2) site in the transcriptional regulation of the chick myogenin gene. Eur. J. Biochem. 230:88-96.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 88-96
    • Malik, S.1    Huang, C.-F.2    Schmidt, J.3
  • 41
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., T. Leung, H. Salihuddin, Z. S. Zhao, and L. Lim. 1994. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367:40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 42
    • 0029056399 scopus 로고
    • A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20
    • Martin, G. A., G. Bollag, F. McCormick, and A. Abo. 1995. A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20. EMBO J. 14:1970-1978.
    • (1995) EMBO J. , vol.14 , pp. 1970-1978
    • Martin, G.A.1    Bollag, G.2    McCormick, F.3    Abo, A.4
  • 43
    • 0027243922 scopus 로고
    • Myocyte enhancer factor (MEF) 2C: A tissue-restricted member of the MEF-2 family of transcription factors
    • Martin, J. F., J. J. Schwarz, and E. N. Olson. 1993. Myocyte enhancer factor (MEF) 2C: a tissue-restricted member of the MEF-2 family of transcription factors. Proc. Natl. Acad. Sci. USA 90:5282-5286.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5282-5286
    • Martin, J.F.1    Schwarz, J.J.2    Olson, E.N.3
  • 45
    • 0023649186 scopus 로고
    • Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation
    • Menko, A. S., and D. Boettiger. 1987. Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation. Cell 51:51-57.
    • (1987) Cell , vol.51 , pp. 51-57
    • Menko, A.S.1    Boettiger, D.2
  • 46
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., A. Lin, F.-X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.-X.3    Abo, A.4    Karin, M.5
  • 47
    • 0025057997 scopus 로고
    • Herculin, a fourth member of the MyoD family of myogenic regulatory genes
    • Miner, J. H., and B. Wold. 1990. Herculin, a fourth member of the MyoD family of myogenic regulatory genes. Proc. Natl. Acad. Sci. USA 87:1089-1093.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1089-1093
    • Miner, J.H.1    Wold, B.2
  • 48
    • 0022727606 scopus 로고
    • Upstream regions of the human cardiac actin gene that modulate its transcription in muscle cells: Presence of an evolutionarily conserved repeated motif
    • Minty, A., and L. Kedes. 1986. Upstream regions of the human cardiac actin gene that modulate its transcription in muscle cells: presence of an evolutionarily conserved repeated motif. Mol. Cell. Biol. 6:2125-2136.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2125-2136
    • Minty, A.1    Kedes, L.2
  • 49
    • 0023392399 scopus 로고
    • Duplicated CArG box domains have positive and mutually dependent regulatory roles in expression of the human α-cardiac actin gene
    • Miwa, T., and L. Kedes. 1987. Duplicated CArG box domains have positive and mutually dependent regulatory roles in expression of the human α-cardiac actin gene. Mol. Cell. Biol. 7:2803-2813.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2803-2813
    • Miwa, T.1    Kedes, L.2
  • 50
    • 0024454749 scopus 로고
    • The CArG promoter sequence is necessary for muscle-specific transcription of the cardiac actin gene in Xenopus embryos
    • Mohun, T. J., M. V. Taylor, N. Garrett, and J. B. Gurdon. 1989. The CArG promoter sequence is necessary for muscle-specific transcription of the cardiac actin gene in Xenopus embryos. EMBO J. 8:1153-1161.
    • (1989) EMBO J. , vol.8 , pp. 1153-1161
    • Mohun, T.J.1    Taylor, M.V.2    Garrett, N.3    Gurdon, J.B.4
  • 51
    • 0029590104 scopus 로고
    • Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins
    • Molkentin, J. D., B. L. Black, J. F. Martin, and E. N. Olson. 1995. Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins. Cell 83:1125-1136.
    • (1995) Cell , vol.83 , pp. 1125-1136
    • Molkentin, J.D.1    Black, B.L.2    Martin, J.F.3    Olson, E.N.4
  • 52
    • 0030015713 scopus 로고    scopus 로고
    • Phosphorylation of the MADS-box transcription factor MEF2C enhances its DNA binding activity
    • Molkentin, J. D., L. Li, and E. N. Olson. 1996. Phosphorylation of the MADS-box transcription factor MEF2C enhances its DNA binding activity. J. Biol. Chem. 271:17199-17204.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17199-17204
    • Molkentin, J.D.1    Li, L.2    Olson, E.N.3
  • 53
    • 0026700090 scopus 로고
    • A rho gene product in human blood platelets. II. Effects of the ADP-ribosylation by botulinum C3 ADP-rihosyltransferase on platelet aggregation
    • Morii, N., T. Teru-uchi, T. Tominaga, N. Kumagai, S. Kozaki, F. Ushikubi, and S. Narumiya. 1992. A rho gene product in human blood platelets. II. Effects of the ADP-ribosylation by botulinum C3 ADP-rihosyltransferase on platelet aggregation. J. Biol. Chem. 267:20921-20926.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20921-20926
    • Morii, N.1    Teru-uchi, T.2    Tominaga, T.3    Kumagai, N.4    Kozaki, S.5    Ushikubi, F.6    Narumiya, S.7
  • 55
    • 0027297310 scopus 로고
    • Myogenin gene disruption results in perinatal lethality because of severe muscle defect
    • Nabeshima, Y., K. Hanaoka, M. Hayasaka, E. Esumi, S. Li, I. Nonaka, and Y.-I. Nabeshima. 1993. Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 364:532-535.
    • (1993) Nature , vol.364 , pp. 532-535
    • Nabeshima, Y.1    Hanaoka, K.2    Hayasaka, M.3    Esumi, E.4    Li, S.5    Nonaka, I.6    Nabeshima, Y.-I.7
  • 56
    • 0028900130 scopus 로고
    • Myogenin and MEF2 function synergistically to activate the MRF4 promoter during myogenesis
    • Naidu, P. S., D. C. Ludolph, R. Q. To, T. J. Hinterberger, and S. F. Konieczny. 1995. Myogenin and MEF2 function synergistically to activate the MRF4 promoter during myogenesis. Mol. Cell. Biol. 15:2707-2718.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2707-2718
    • Naidu, P.S.1    Ludolph, D.C.2    To, R.Q.3    Hinterberger, T.J.4    Konieczny, S.F.5
  • 57
    • 0028258943 scopus 로고
    • rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells
    • Nishiyama, T., T. Sasaki, K. Takaishi, M. Kato, H. Yaku, K. Araki, Y. Matsuura, and Y. Takai. 1994. rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor-and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. Mol. Cell. Biol. 14:2447-2456.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5    Araki, K.6    Matsuura, Y.7    Takai, Y.8
  • 58
    • 0028157729 scopus 로고
    • Regulation and function of the Rho subfamily of small GTPases
    • Nobes, C., and A. Hall. 1994. Regulation and function of the Rho subfamily of small GTPases. Curr. Opin. Genet. Dev. 4:77-81.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 77-81
    • Nobes, C.1    Hall, A.2
  • 59
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 60
    • 0025120750 scopus 로고
    • The MyoD family, a paradigm for development?
    • Olson, E. N. 1990. The MyoD family, a paradigm for development? Genes Dev. 4:1454-1461.
    • (1990) Genes Dev. , vol.4 , pp. 1454-1461
    • Olson, E.N.1
  • 61
    • 0028808913 scopus 로고
    • Regulation of muscle differentiation by the MEF2 family of MADS box transcription factors
    • Olson, E. N., M. Perry, and R. A. Schulz. 1995. Regulation of muscle differentiation by the MEF2 family of MADS box transcription factors. Dev. Biol. 172:2-14.
    • (1995) Dev. Biol. , vol.172 , pp. 2-14
    • Olson, E.N.1    Perry, M.2    Schulz, R.A.3
  • 62
    • 15844391229 scopus 로고    scopus 로고
    • Serum response factor mediates AP-1-dependent induction of the skeletal α-actin promoter in ventricular myocytes
    • Paradis, P., W. R. MacLellan, N. S. Belaguli, R. J. Schwartz, and M. D. Schneider. 1996. Serum response factor mediates AP-1-dependent induction of the skeletal α-actin promoter in ventricular myocytes. J. Biol. Chem. 271:10827-10833.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10827-10833
    • Paradis, P.1    MacLellan, W.R.2    Belaguli, N.S.3    Schwartz, R.J.4    Schneider, M.D.5
  • 64
    • 0025840260 scopus 로고
    • Human SRF-related proteins: DNA-binding properties and potential regulatory targets
    • Pollock, R., and R. Treisman. 1991. Human SRF-related proteins: DNA-binding properties and potential regulatory targets. Genes Dev. 5:2327-2341.
    • (1991) Genes Dev. , vol.5 , pp. 2327-2341
    • Pollock, R.1    Treisman, R.2
  • 65
    • 0024410471 scopus 로고
    • Identification of two nuclear factor-binding domains on the chicken cardiac actin promoter: Implications for regulation of the gene
    • Quitschke, W. W., L. DePonti-Zilli, Z. Y. Lin, and B. M. Paterson. 1989. Identification of two nuclear factor-binding domains on the chicken cardiac actin promoter: implications for regulation of the gene. Mol. Cell. Biol. 9:3218-3230.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3218-3230
    • Quitschke, W.W.1    DePonti-Zilli, L.2    Lin, Z.Y.3    Paterson, B.M.4
  • 66
    • 0028841777 scopus 로고
    • A series of mutations in the D-MEF2 transcription factor reveal multiple functions in larval and adult myogenesis in Drosophila
    • Ranganayakula, G., B. Zhao, A. Dokidis, J. D. Molkentin, and E. N. Olson. 1995. A series of mutations in the D-MEF2 transcription factor reveal multiple functions in larval and adult myogenesis in Drosophila. Dev. Biol. 171:169-181.
    • (1995) Dev. Biol. , vol.171 , pp. 169-181
    • Ranganayakula, G.1    Zhao, B.2    Dokidis, A.3    Molkentin, J.D.4    Olson, E.N.5
  • 67
    • 0024821376 scopus 로고
    • Identification of MRF4: A new member of the muscle regulatory factor gene family
    • Rhodes, S. J., and S. F. Konieczny. 1989. Identification of MRF4: a new member of the muscle regulatory factor gene family. Genes Dev. 3:2050-2061.
    • (1989) Genes Dev. , vol.3 , pp. 2050-2061
    • Rhodes, S.J.1    Konieczny, S.F.2
  • 68
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 69
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 70
    • 0026708853 scopus 로고
    • Roles for the integrin VLA-4 and its counter receptor VCAM-1 in myogenesis
    • Rosen, G. D., J. R. Sanes, R. LaChance, J. M. Cunningham, J. Roman, and D. C. Dean. 1992. Roles for the integrin VLA-4 and its counter receptor VCAM-1 in myogenesis. Cell 69:1107-1119.
    • (1992) Cell , vol.69 , pp. 1107-1119
    • Rosen, G.D.1    Sanes, J.R.2    LaChance, R.3    Cunningham, J.M.4    Roman, J.5    Dean, D.C.6
  • 71
    • 0023779031 scopus 로고
    • Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin, E. J., D. M. Gill, P. Boquet, and M. R. Popoff. 1988. Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell. Biol. 8:418-426.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 72
    • 0025133383 scopus 로고
    • Muscle-specific expression of the cardiac α-actin gene requires MyoD1, CArG-box binding factor, and Sp1
    • Sartorelli, V., K. A. Webster, and L. Kedes. 1990. Muscle-specific expression of the cardiac α-actin gene requires MyoD1, CArG-box binding factor, and Sp1. Genes Dev. 4:1811-1822.
    • (1990) Genes Dev. , vol.4 , pp. 1811-1822
    • Sartorelli, V.1    Webster, K.A.2    Kedes, L.3
  • 73
    • 0027477931 scopus 로고
    • Myogenic regulatory factors: Dissecting their role and regulation during vertebrate embryogenesis
    • Sassoon, D. A. 1993. Myogenic regulatory factors: dissecting their role and regulation during vertebrate embryogenesis. Dev. Biol. 156:11-23.
    • (1993) Dev. Biol. , vol.156 , pp. 11-23
    • Sassoon, D.A.1
  • 74
    • 0029664439 scopus 로고    scopus 로고
    • Integrin alpha subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation
    • Sastry, S. K., M. Lakonishok, D. A. Thomas, J. Muschler, and A. F. Horwitz. 1996. Integrin alpha subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation. J. Cell Biol. 133:169-184.
    • (1996) J. Cell Biol. , vol.133 , pp. 169-184
    • Sastry, S.K.1    Lakonishok, M.2    Thomas, D.A.3    Muschler, J.4    Horwitz, A.F.5
  • 75
    • 0027470176 scopus 로고
    • Different structural organization of Ras and Rho effector domains
    • Self, A. J., H. F. Paterson, and A. Hall. 1993. Different structural organization of Ras and Rho effector domains. Oncogene 8:655-661.
    • (1993) Oncogene , vol.8 , pp. 655-661
    • Self, A.J.1    Paterson, H.F.2    Hall, A.3
  • 79
    • 0027391509 scopus 로고
    • Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility
    • Takaishi, K., A. Kikuchi, K. Kuroda, K. Kotani, T. Sasaki, and Y. Takai. 1993. Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility. Mol. Cell. Biol. 13:72-79.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 72-79
    • Takaishi, K.1    Kikuchi, A.2    Kuroda, K.3    Kotani, K.4    Sasaki, T.5    Takai, Y.6
  • 80
    • 0027952703 scopus 로고
    • Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility
    • Takaishi, K., T. Sasaki, M. Kato, W. Yamochi, S. Kuroda, T. Nakamura, M. Takeichi, and Y. Takai. 1994. Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility. Oncogene 9:273-279.
    • (1994) Oncogene , vol.9 , pp. 273-279
    • Takaishi, K.1    Sasaki, T.2    Kato, M.3    Yamochi, W.4    Kuroda, S.5    Nakamura, T.6    Takeichi, M.7    Takai, Y.8
  • 81
    • 0024400402 scopus 로고
    • Muscle-specific (CArG) and serum responsive (SRE) promoter elements are functionally interchangeable in Xenopus embryos and mouse fibroblasts
    • Taylor, M., R. Treisman, N. Garrett, and T. Mohun. 1989. Muscle-specific (CArG) and serum responsive (SRE) promoter elements are functionally interchangeable in Xenopus embryos and mouse fibroblasts. Development 106:67-78.
    • (1989) Development , vol.106 , pp. 67-78
    • Taylor, M.1    Treisman, R.2    Garrett, N.3    Mohun, T.4
  • 83
    • 0025889701 scopus 로고
    • A MyoD1-independent muscle specific enhancer controls the expression of the β-myosin heavy chain gene in skeletal and cardiac muscle cells
    • Thompson, W. R., B. Nadal-Ginard, and V. Mahdavi. 1991. A MyoD1-independent muscle specific enhancer controls the expression of the β-myosin heavy chain gene in skeletal and cardiac muscle cells. J. Biol. Chem. 266:22678-22688.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22678-22688
    • Thompson, W.R.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 84
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., L. C. Cantley, and C. L. Carpenter. 1995. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:17656-17659.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 85
    • 0027471215 scopus 로고
    • Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP-ribosylation of the small molecular weight GTP-binding protein, rho
    • Tominaga, T., K. Sugie, M. Hirata, N. Morii, J. Fukata, A. Uchida, H. Imura, and S. Narumiya. 1993. Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP-ribosylation of the small molecular weight GTP-binding protein, rho. J. Cell Biol. 120:1529-1537.
    • (1993) J. Cell Biol. , vol.120 , pp. 1529-1537
    • Tominaga, T.1    Sugie, K.2    Hirata, M.3    Morii, N.4    Fukata, J.5    Uchida, A.6    Imura, H.7    Narumiya, S.8
  • 86
    • 17544377292 scopus 로고    scopus 로고
    • ADP-ribosylation of the G protein Rho inhibits integrin regulation of tumor cell growth
    • Udagawa, T., and B. W. McIntyre. 1996. ADP-ribosylation of the G protein Rho inhibits integrin regulation of tumor cell growth. J. Biol. Chem. 271:12542-12548.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12542-12548
    • Udagawa, T.1    McIntyre, B.W.2
  • 89
    • 0027738464 scopus 로고
    • The MyoD family and myogenesis: Redundancy, networks, and thresholds
    • Weintraub, H. 1993. The MyoD family and myogenesis: redundancy, networks, and thresholds. Cell 75:1241-1244.
    • (1993) Cell , vol.75 , pp. 1241-1244
    • Weintraub, H.1
  • 90
    • 0024576880 scopus 로고
    • Myogenin, a factor regulating myogenesis, has a domain homologous to MyoD
    • Wright, W. E., D. A. Sassoon, and V. K. Lin. 1989. Myogenin, a factor regulating myogenesis, has a domain homologous to MyoD. Cell 56:607-617.
    • (1989) Cell , vol.56 , pp. 607-617
    • Wright, W.E.1    Sassoon, D.A.2    Lin, V.K.3
  • 91
    • 0027280575 scopus 로고
    • ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of cell cycle
    • Yamamoto, M., N. Marui, T. Sakai, N. Morii, S. Kozaki, K. Ikai, S. Imamura, and S. Narumiya. 1993. ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of cell cycle. Oncogene 8:1449-1455.
    • (1993) Oncogene , vol.8 , pp. 1449-1455
    • Yamamoto, M.1    Marui, N.2    Sakai, T.3    Morii, N.4    Kozaki, S.5    Ikai, K.6    Imamura, S.7    Narumiya, S.8
  • 92
    • 0028228614 scopus 로고
    • Growth site localization of rhol small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae
    • Yamochi, W., K. Tanaka, H. Nonaka, A. Maeda, T. Musha, and Y. Takai. 1994. Growth site localization of rhol small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae. J. Cell Biol. 125:1077-1093.
    • (1994) J. Cell Biol. , vol.125 , pp. 1077-1093
    • Yamochi, W.1    Tanaka, K.2    Nonaka, H.3    Maeda, A.4    Musha, T.5    Takai, Y.6
  • 93
    • 0027227469 scopus 로고
    • The regulation of myogenin gene expression during the embryonic development of the mouse
    • Yee, S. P., and P. W. Rigby. 1993. The regulation of myogenin gene expression during the embryonic development of the mouse. Genes Dev. 7:1277-1289.
    • (1993) Genes Dev. , vol.7 , pp. 1277-1289
    • Yee, S.P.1    Rigby, P.W.2
  • 94
    • 0028338545 scopus 로고
    • Activation of phosphoinositide-3 kinase activity by Cdc42Hs binding to p85
    • Zheng, Y., S. Bagrodia, and R. A. Cerione. 1994. Activation of phosphoinositide-3 kinase activity by Cdc42Hs binding to p85. J. Biol. Chem. 269:18727-18730.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.