메뉴 건너뛰기




Volumn 247, Issue 1, 1999, Pages 94-104

Differential biological activities of mammalian Id proteins in muscle cells

Author keywords

Differentiation; Helix loop helix; Id proteins; Myogenesis; Transcription

Indexed keywords

CREATINE KINASE; DNA; HELIX LOOP HELIX PROTEIN; INHIBITOR OF DIFFERENTIATION PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0033602037     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4330     Document Type: Article
Times cited : (44)

References (45)
  • 1
    • 0001032841 scopus 로고
    • The helix-loop-helix motif: Structure and function
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press. p. 861-879
    • Murre C., Baltimore D. The helix-loop-helix motif: Structure and function. Transcriptional Regulation. 1992;Cold Spring Harbor Laboratory Press, Cold Spring Harbor. p. 861-879.
    • (1992) Transcriptional Regulation
    • Murre, C.1    Baltimore, D.2
  • 2
    • 0027435022 scopus 로고
    • Neuronal expression of the regulatory helix-loop-helix factor Id2 gene in mouse
    • Neuman T., Keen A., Zuber M. X., Kristjansson G. I., Gruss P., Nornes H. O. Neuronal expression of the regulatory helix-loop-helix factor Id2 gene in mouse. Dev. Biol. 160:1993;186-195.
    • (1993) Dev. Biol. , vol.160 , pp. 186-195
    • Neuman, T.1    Keen, A.2    Zuber, M.X.3    Kristjansson, G.I.4    Gruss, P.5    Nornes, H.O.6
  • 3
    • 0028784793 scopus 로고
    • Helix-loop-helix transcription factors mediate activation and repression of the p75LNGFR gene
    • Chiaramello A., Neuman K., Palm K., Metsis M., Neuman T. Helix-loop-helix transcription factors mediate activation and repression of the p75LNGFR gene. Mol. Cell. Biol. 15:1995;6036-6044.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6036-6044
    • Chiaramello, A.1    Neuman, K.2    Palm, K.3    Metsis, M.4    Neuman, T.5
  • 4
    • 0029914835 scopus 로고    scopus 로고
    • Transcription of the dominant-negative helix-loop-helix protein Id1 is regulated by a protein complex containing the immediate-early response gene Egr-1
    • Tournay O., Benezra R. Transcription of the dominant-negative helix-loop-helix protein Id1 is regulated by a protein complex containing the immediate-early response gene Egr-1. Mol. Cell. Biol. 16:1996;2418-2430.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2418-2430
    • Tournay, O.1    Benezra, R.2
  • 5
    • 0025238437 scopus 로고
    • The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
    • Benezra R., Davis R. L., Lockshon D., Turner D. L., Weintraub H. The protein Id: A negative regulator of helix-loop-helix DNA binding proteins. Cell. 61:1990;49-59.
    • (1990) Cell , vol.61 , pp. 49-59
    • Benezra, R.1    Davis, R.L.2    Lockshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 7
    • 0025939047 scopus 로고
    • Id proteins Id1 and Id2 selectively inhibit DNA binding by one class of helix-loop-helix proteins
    • Sun X., Copeland N. G., Jenkins N. A., Baltimore D. Id proteins Id1 and Id2 selectively inhibit DNA binding by one class of helix-loop-helix proteins. Mol.Cell. Biol. 11:1991;5603-5611.
    • (1991) Mol.Cell. Biol. , vol.11 , pp. 5603-5611
    • Sun, X.1    Copeland, N.G.2    Jenkins, N.A.3    Baltimore, D.4
  • 8
    • 0028335141 scopus 로고
    • The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3
    • Riechmann V., Cruchten I. V., Sablitzky F. The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3. Nucleic Acids Res. 22:1994;749-755.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 749-755
    • Riechmann, V.1    Cruchten, I.V.2    Sablitzky, F.3
  • 9
    • 0026765031 scopus 로고
    • Overexpression of Id protein inhibits the muscle differentiation program: In vivo association of Id with E2A proteins
    • Jen Y., Weintraub H., Benezra R. Overexpression of Id protein inhibits the muscle differentiation program: In vivo association of Id with E2A proteins. Genes Dev. 6:1992;1466-1479.
    • (1992) Genes Dev. , vol.6 , pp. 1466-1479
    • Jen, Y.1    Weintraub, H.2    Benezra, R.3
  • 10
    • 0029827774 scopus 로고    scopus 로고
    • Muscle cell differentiation is inhibited by the helix-loop-helix protein Id3
    • Melnikova I. N., Christy B. A. Muscle cell differentiation is inhibited by the helix-loop-helix protein Id3. Cell Growth Differ. 7:1996;1067-1079.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1067-1079
    • Melnikova, I.N.1    Christy, B.A.2
  • 11
    • 0029827773 scopus 로고    scopus 로고
    • Regulation of cell differentiation in C2C12 myoblasts by the Id3 helix-loop-helix protein
    • Atherton G. T., Travers H., Deed R., Norton J. D. Regulation of cell differentiation in C2C12 myoblasts by the Id3 helix-loop-helix protein. Cell Growth Differ. 7:1996;1059-1066.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1059-1066
    • Atherton, G.T.1    Travers, H.2    Deed, R.3    Norton, J.D.4
  • 12
    • 12644270610 scopus 로고    scopus 로고
    • The nuclear localization sequences of the BRCA1 protein interact with the importin-alpha subunit of the nuclear transport signal receptor
    • Chen C. F., Li S., Chen Y., Chen P. L., Sharp Z. D., Lee W. H. The nuclear localization sequences of the BRCA1 protein interact with the importin-alpha subunit of the nuclear transport signal receptor. J. Biol. Chem. 271:1996;32863-32868.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32863-32868
    • Chen, C.F.1    Li, S.2    Chen, Y.3    Chen, P.L.4    Sharp, Z.D.5    Lee, W.H.6
  • 13
    • 0023850352 scopus 로고
    • SRα promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat
    • Takebe Y., Seiki M., Fujisawa J.-I., Hoy P., Yokota K., Arai K.-I., Yoshida M., Arai N. SRα promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat. Mol. Cell. Biol. 8:1988;466-472.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 466-472
    • Takebe, Y.1    Seiki, M.2    Fujisawa, J.-I.3    Hoy, P.4    Yokota, K.5    Arai, K.-I.6    Yoshida, M.7    Arai, N.8
  • 14
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham F. L., Van der Eb A. J. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology. 52:1973;456-467.
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 15
    • 0020459571 scopus 로고
    • Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro
    • Bader D., Masaki T., Fishman D. A. Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro. J. Cell Biol. 95:1982;763-770.
    • (1982) J. Cell Biol. , vol.95 , pp. 763-770
    • Bader, D.1    Masaki, T.2    Fishman, D.A.3
  • 16
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J. D., Lebovitz R. M., Roeder R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1983;1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 17
    • 0023779032 scopus 로고
    • The muscle creatine kinase gene is regulated by multiple upstream elements, including a muscle-specific enhancer
    • Jaynes J. B., Johnson J. E., Buskin J. N., Gartside C. L., Hauschka S. D. The muscle creatine kinase gene is regulated by multiple upstream elements, including a muscle-specific enhancer. Mol. Cell. Biol. 8:1988;62-70.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 62-70
    • Jaynes, J.B.1    Johnson, J.E.2    Buskin, J.N.3    Gartside, C.L.4    Hauschka, S.D.5
  • 18
    • 0023553666 scopus 로고
    • A novel rapid assay for chloramphenicol acetyltransferase gene expression
    • Neumann J. R., Morency C. A., Russian K. O. A novel rapid assay for chloramphenicol acetyltransferase gene expression. BioTechniques. 5:1987;444-447.
    • (1987) BioTechniques , vol.5 , pp. 444-447
    • Neumann, J.R.1    Morency, C.A.2    Russian, K.O.3
  • 19
    • 0025176773 scopus 로고
    • Point mutations in the Moloney murine leukemia virus enhancer identify a lymphoid-specific viral core motif and 1,3-phorbol myristate acetate-inducible element
    • Speck N. A., Renjifo B., Hopkins N. Point mutations in the Moloney murine leukemia virus enhancer identify a lymphoid-specific viral core motif and 1,3-phorbol myristate acetate-inducible element. J. Virol. 64:1990;543-550.
    • (1990) J. Virol. , vol.64 , pp. 543-550
    • Speck, N.A.1    Renjifo, B.2    Hopkins, N.3
  • 20
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • Kadonaga J. T., Carner K. R., Masiarz F. R., Tjian R. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell. 51:1987;1079-1090.
    • (1987) Cell , vol.51 , pp. 1079-1090
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 21
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed inEscherichia coliS
    • Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed inEscherichia coliS. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 23
    • 0021332093 scopus 로고
    • Detection of mRNAs in sea urchin embryos by in situ hybridization using asymmetric RNA probes
    • Cox K., DeLeon D., Angerer L., Angerer R. Detection of mRNAs in sea urchin embryos by in situ hybridization using asymmetric RNA probes. Dev. Biol. 101:1984;485-502.
    • (1984) Dev. Biol. , vol.101 , pp. 485-502
    • Cox, K.1    Deleon, D.2    Angerer, L.3    Angerer, R.4
  • 24
    • 0026025871 scopus 로고
    • Functional characterization of developmentally controlled immunoglobulin kappa 3′ enhancer: Regulation by Id, a repressor of helix-loop-helix transcription factors
    • Pongubala J. M. R., Atchison M. L. Functional characterization of developmentally controlled immunoglobulin kappa 3′ enhancer: Regulation by Id, a repressor of helix-loop-helix transcription factors. Mol. Cell. Biol. 11:1991;1040-1047.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1040-1047
    • Pongubala, J.M.R.1    Atchison, M.L.2
  • 26
    • 0025971911 scopus 로고
    • Pancreatic B-cell-type-specific transcription of the insulin gene is mediated by basic-helix-loop-helix DNA-binding proteins
    • Cordle S. R., Henderson E., Masuoka H., Weil P. A., Stein R. Pancreatic B-cell-type-specific transcription of the insulin gene is mediated by basic-helix-loop-helix DNA-binding proteins. Mol. Cell. Biol. 11:1991;1734-1738.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1734-1738
    • Cordle, S.R.1    Henderson, E.2    Masuoka, H.3    Weil, P.A.4    Stein, R.5
  • 27
    • 0027237711 scopus 로고
    • A heterodimer of HEB and an E12-related protein interacts with the CD4 enhancer and regulates its activity in T-cell lines
    • Sawada S., Littman D. R. A heterodimer of HEB and an E12-related protein interacts with the CD4 enhancer and regulates its activity in T-cell lines. Mol. Cell. Biol. 13:1993;5621-5628.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5621-5628
    • Sawada, S.1    Littman, D.R.2
  • 28
    • 0028088556 scopus 로고
    • Constitutive expression of the Id1 gene impairs mouse B cell development
    • Sun X.-H. Constitutive expression of the Id1 gene impairs mouse B cell development. Cell. 79:1994;893-900.
    • (1994) Cell , vol.79 , pp. 893-900
    • Sun, X.-H.1
  • 29
    • 0026582871 scopus 로고
    • Inhibition of myeloid differentiation by helix-loop-helix protein Id
    • Kreider B., Benezra R., Roverea G., Kadesch T. Inhibition of myeloid differentiation by helix-loop-helix protein Id. Science. 255:1992;1700-1702.
    • (1992) Science , vol.255 , pp. 1700-1702
    • Kreider, B.1    Benezra, R.2    Roverea, G.3    Kadesch, T.4
  • 30
    • 0030754089 scopus 로고    scopus 로고
    • Differential interactions of Id proteins with basic-helix-loop-helix transcription factors
    • Langlands K., Yin X., Anand G., Prochownik E. V. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J. Biol. Chem. 272:1997;19785-19793.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19785-19793
    • Langlands, K.1    Yin, X.2    Anand, G.3    Prochownik, E.V.4
  • 31
    • 0022607432 scopus 로고
    • Transcriptional and posttranscriptional control of c-myc during myogenesis: Its mRNA remains inducible in differentiated cells and does not suppress the differentiated phenotype
    • Edno T., Nadal-Ginard B. Transcriptional and posttranscriptional control of c-myc during myogenesis: Its mRNA remains inducible in differentiated cells and does not suppress the differentiated phenotype. Mol. Cell. Biol. 6:1986;1412-1421.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1412-1421
    • Edno, T.1    Nadal-Ginard, B.2
  • 32
    • 0027499060 scopus 로고
    • Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation
    • Gu W., Schneider J. W., Condorelli G., Kaushal S., Mahdavi V., Nadal-Ginard B. Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation. Cell. 72:1993;309-324.
    • (1993) Cell , vol.72 , pp. 309-324
    • Gu, W.1    Schneider, J.W.2    Condorelli, G.3    Kaushal, S.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 33
    • 0028339957 scopus 로고
    • Reversal of terminal differentiation mediated by p107 in Rb -/- muscle cells
    • Schneider J. W., Gu W., Zhu L., Mahdavi V., Nadal-Ginard B. Reversal of terminal differentiation mediated by p107 in Rb -/- muscle cells. Science. 264:1994;1467-1471.
    • (1994) Science , vol.264 , pp. 1467-1471
    • Schneider, J.W.1    Gu, W.2    Zhu, L.3    Mahdavi, V.4    Nadal-Ginard, B.5
  • 34
    • 0025277030 scopus 로고
    • Cell proliferation is inhibited by MyoD1 independently of myogenic differentiation
    • Sorrentino V., Pepperkok R., Davis R. L., Ansorge W., Philipson L. Cell proliferation is inhibited by MyoD1 independently of myogenic differentiation. Nature. 345:1990;813-815.
    • (1990) Nature , vol.345 , pp. 813-815
    • Sorrentino, V.1    Pepperkok, R.2    Davis, R.L.3    Ansorge, W.4    Philipson, L.5
  • 36
    • 0029034451 scopus 로고
    • MyoD-induced expression of p21 inhibits cyclin-dependent kinase activity upon myocyte terminal differentiation
    • Guo K., Wang J., Andres V., Smith R. C., Walsh K. MyoD-induced expression of p21 inhibits cyclin-dependent kinase activity upon myocyte terminal differentiation. Mol. Cell. Biol. 15:1995;3823-3829.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3823-3829
    • Guo, K.1    Wang, J.2    Andres, V.3    Smith, R.C.4    Walsh, K.5
  • 39
    • 0027496935 scopus 로고
    • The p21 cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper J., Adami G., Wei N., Keyomarsi K., Elledge S. The p21 cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell. 75:1993;805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.1    Adami, G.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.5
  • 40
    • 0028928036 scopus 로고
    • Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase
    • Skapek S. X., Rhee J., Spicer D. B., Lassar A. B. Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase. Science. 267:1995;1022-1024.
    • (1995) Science , vol.267 , pp. 1022-1024
    • Skapek, S.X.1    Rhee, J.2    Spicer, D.B.3    Lassar, A.B.4
  • 41
    • 0028303223 scopus 로고
    • The helix-loop-helix protein Id2 enhances cell proliferation and binds to the retinoblastoma protein
    • Iavarone A., Garg P., Lasorella A., Hsu J., Israel M. A. The helix-loop-helix protein Id2 enhances cell proliferation and binds to the retinoblastoma protein. Genes Dev. 8:1994;1270-1284.
    • (1994) Genes Dev. , vol.8 , pp. 1270-1284
    • Iavarone, A.1    Garg, P.2    Lasorella, A.3    Hsu, J.4    Israel, M.A.5
  • 42
    • 0029929792 scopus 로고    scopus 로고
    • Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins
    • Lasorella A., Iavarone A., Israel M. A. Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins. Mol. Cell. Biol. 16:1996;2570-2578.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2570-2578
    • Lasorella, A.1    Iavarone, A.2    Israel, M.A.3
  • 43
    • 0026486629 scopus 로고
    • Id expression during mouse development: A role in morphogenesis
    • Wang Y., Benezra R., Sassoon D. A. Id expression during mouse development: A role in morphogenesis. Dev. Dyn. 194:1992;222-230.
    • (1992) Dev. Dyn. , vol.194 , pp. 222-230
    • Wang, Y.1    Benezra, R.2    Sassoon, D.A.3
  • 44
    • 0027489684 scopus 로고
    • Expression of the helix-loop-helix factor Id during mouse embryonic development
    • Evans S. M., O'Brein T. X. Expression of the helix-loop-helix factor Id during mouse embryonic development. Dev. Biol. 159:1993;485-499.
    • (1993) Dev. Biol. , vol.159 , pp. 485-499
    • Evans, S.M.1    O'Brein, T.X.2
  • 45
    • 0029061511 scopus 로고
    • Mutually exclusive expression of two dominant-negative helix-loop-helix (dnHLH) genes, Id4 and Id3, in the developing brain of the mouse suggests distinct regulatory roles of these dnHLH proteins during cellular proliferation and differentiation of the nervous system
    • Riechmann V., Sablitzky F. Mutually exclusive expression of two dominant-negative helix-loop-helix (dnHLH) genes, Id4 and Id3, in the developing brain of the mouse suggests distinct regulatory roles of these dnHLH proteins during cellular proliferation and differentiation of the nervous system. Cell Growth Differ. 6:1995;837-843.
    • (1995) Cell Growth Differ. , vol.6 , pp. 837-843
    • Riechmann, V.1    Sablitzky, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.