메뉴 건너뛰기




Volumn 1750, Issue 1, 2005, Pages 48-60

NMR and mass spectrometry studies of putative interactions of cell cycle proteins pRb and CDK6 with cell differentiation proteins MyoD and ID-2

Author keywords

CDK6; Complex; Id 2; Interaction; MyoD; Retinoblastoma protein

Indexed keywords

AMINO ACID; CELL CYCLE PROTEIN; CYCLIN DEPENDENT KINASE 6; DNA; HELIX LOOP HELIX PROTEIN; INHIBITOR OF DIFFERENTIATION 2; MYOD PROTEIN; PROTEIN E7; PROTEIN P19; RETINOBLASTOMA PROTEIN; VIRUS LARGE T ANTIGEN;

EID: 20444393161     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.03.012     Document Type: Article
Times cited : (8)

References (54)
  • 1
    • 0030829722 scopus 로고    scopus 로고
    • Cell cycle exit upon myogenic differentiation
    • K. Walsh, and H. Perlman Cell cycle exit upon myogenic differentiation Curr. Opin. Genet. Dev. 7 1997 597 602
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 597-602
    • Walsh, K.1    Perlman, H.2
  • 2
    • 0036180120 scopus 로고    scopus 로고
    • Molecular aspects of the mammalian cell cycle and cancer
    • T. Sandal Molecular aspects of the mammalian cell cycle and cancer Oncologist 7 2002 73 81
    • (2002) Oncologist , vol.7 , pp. 73-81
    • Sandal, T.1
  • 3
    • 0034471262 scopus 로고    scopus 로고
    • ID helix-loop-helix proteins in cell growth, differentiation and tumorigenesis
    • J.D. Norton ID helix-loop-helix proteins in cell growth, differentiation and tumorigenesis J. Cell Sci. 113 Pt. 22 2000 3897 3905
    • (2000) J. Cell Sci. , vol.113 , Issue.22 PART , pp. 3897-3905
    • Norton, J.D.1
  • 4
    • 0025808242 scopus 로고
    • Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo
    • A.B. Lassar, R.L. Davis, W.E. Wright, T. Kadesch, C. Murre, A. Voronova, D. Baltimore, and H. Weintraub Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo Cell 66 1991 305 315
    • (1991) Cell , vol.66 , pp. 305-315
    • Lassar, A.B.1    Davis, R.L.2    Wright, W.E.3    Kadesch, T.4    Murre, C.5    Voronova, A.6    Baltimore, D.7    Weintraub, H.8
  • 5
    • 0033980393 scopus 로고    scopus 로고
    • Helix-loop-helix proteins: Regulators of transcription in eucaryotic organisms
    • M.E. Massari, and C. Murre Helix-loop-helix proteins: regulators of transcription in eucaryotic organisms Mol. Cell. Biol. 20 2000 429 440
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 429-440
    • Massari, M.E.1    Murre, C.2
  • 8
    • 0027499060 scopus 로고
    • Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation
    • W. Gu, J.W. Schneider, G. Condorelli, S. Kaushal, V. Mahdavi, and B. Nadal-Ginard 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
  • 9
    • 0037590194 scopus 로고    scopus 로고
    • Regulation of MyoD activity and muscle cell differentiation by MDM2, pRb, and Sp1
    • C.S. Guo, C. Degnin, T.A. Fiddler, D. Stauffer, and M.J. Thayer Regulation of MyoD activity and muscle cell differentiation by MDM2, pRb, and Sp1 J. Biol. Chem. 278 2003 22615 22622
    • (2003) J. Biol. Chem. , vol.278 , pp. 22615-22622
    • Guo, C.S.1    Degnin, C.2    Fiddler, T.A.3    Stauffer, D.4    Thayer, M.J.5
  • 11
    • 0033558347 scopus 로고    scopus 로고
    • Coupling of the cell cycle and myogenesis through the cyclin D1-dependent interaction of MyoD with cdk4
    • J.M. Zhang, Q. Wei, X. Zhao, and B.M. Paterson Coupling of the cell cycle and myogenesis through the cyclin D1-dependent interaction of MyoD with cdk4 EMBO J. 18 1999 926 933
    • (1999) EMBO J. , vol.18 , pp. 926-933
    • Zhang, J.M.1    Wei, Q.2    Zhao, X.3    Paterson, B.M.4
  • 12
    • 0033572867 scopus 로고    scopus 로고
    • Direct inhibition of G(1) cdk kinase activity by MyoD promotes myoblast cell cycle withdrawal and terminal differentiation
    • J.M. Zhang, X. Zhao, Q. Wei, and B.M. Paterson Direct inhibition of G(1) cdk kinase activity by MyoD promotes myoblast cell cycle withdrawal and terminal differentiation EMBO J. 18 1999 6983 6993
    • (1999) EMBO J. , vol.18 , pp. 6983-6993
    • Zhang, J.M.1    Zhao, X.2    Wei, Q.3    Paterson, B.M.4
  • 13
    • 0029002314 scopus 로고
    • Molecular cloning of ID4, a novel dominant negative helix-loop-helix human gene on chromosome 6p21.3-p22
    • A. Pagliuca, P.C. Bartoli, S. Saccone, G. Della Valle, and L. Lania Molecular cloning of ID4, a novel dominant negative helix-loop-helix human gene on chromosome 6p21.3-p22 Genomics 27 1995 200 203
    • (1995) Genomics , vol.27 , pp. 200-203
    • Pagliuca, A.1    Bartoli, P.C.2    Saccone, S.3    Della Valle, G.4    Lania, L.5
  • 14
    • 0031963681 scopus 로고    scopus 로고
    • Id helix-loop-helix proteins in cell growth and differentiation
    • J.D. Norton, R.W. Deed, G. Craggs, and F. Sablitzky Id helix-loop-helix proteins in cell growth and differentiation Trends Cell Biol. 8 1998 58 65
    • (1998) Trends Cell Biol. , vol.8 , pp. 58-65
    • Norton, J.D.1    Deed, R.W.2    Craggs, G.3    Sablitzky, F.4
  • 15
    • 0029929792 scopus 로고    scopus 로고
    • Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins
    • A. Lasorella, A. Iavarone, and M.A. Israel 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
  • 16
    • 0028303223 scopus 로고
    • The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein
    • A. Iavarone, P. Garg, A. Lasorella, J. Hsu, and M.A. Israel The helix-loop-helix protein Id-2 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
  • 17
    • 0028582034 scopus 로고
    • Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related CDK6 inhibitor, correlates with wild-type pRb function
    • K.L. Guan, C.W. Jenkins, Y. Li, M.A. Nichols, X. Wu, C.L. O'Keefe, A.G. Matera, and Y. Xiong Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related CDK6 inhibitor, correlates with wild-type pRb function Genes Dev. 8 1994 2939 2952
    • (1994) Genes Dev. , vol.8 , pp. 2939-2952
    • Guan, K.L.1    Jenkins, C.W.2    Li, Y.3    Nichols, M.A.4    Wu, X.5    O'Keefe, C.L.6    Matera, A.G.7    Xiong, Y.8
  • 19
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • J. Kopp, and T. Schwede The SWISS-MODEL repository of annotated three-dimensional protein structure homology models Nucleic Acids Res. 32 2004 D230 D234 Database issue
    • (2004) Nucleic Acids Res. , vol.32
    • Kopp, J.1    Schwede, T.2
  • 20
    • 0033574614 scopus 로고    scopus 로고
    • Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors
    • N.P. Pavletich Mechanisms of cyclin-dependent kinase regulation: structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors J. Mol. Biol. 287 1999 821 828
    • (1999) J. Mol. Biol. , vol.287 , pp. 821-828
    • Pavletich, N.P.1
  • 21
    • 0029960519 scopus 로고    scopus 로고
    • Skeletal muscle cells lacking the retinoblastoma protein display defects in muscle gene expression and accumulate in S and G2 phases of the cell cycle
    • B.G. Novitch, G.J. Mulligan, T. Jacks, and A.B. Lassar Skeletal muscle cells lacking the retinoblastoma protein display defects in muscle gene expression and accumulate in S and G2 phases of the cell cycle J. Cell Biol. 135 1996 441 456
    • (1996) J. Cell Biol. , vol.135 , pp. 441-456
    • Novitch, B.G.1    Mulligan, G.J.2    Jacks, T.3    Lassar, A.B.4
  • 22
    • 0034964014 scopus 로고    scopus 로고
    • Retinoblastoma protein partners
    • E.J. Morris, and N.J. Dyson Retinoblastoma protein partners Adv. Cancer Res. 82 2001 1 54
    • (2001) Adv. Cancer Res. , vol.82 , pp. 1-54
    • Morris, E.J.1    Dyson, N.J.2
  • 24
    • 0034656331 scopus 로고    scopus 로고
    • Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases
    • T. Weber, R. Baumgartner, C. Renner, M.A. Marahiel, and T.A. Holak Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases Struct. Fold Des. 8 2000 407 418
    • (2000) Struct. Fold Des. , vol.8 , pp. 407-418
    • Weber, T.1    Baumgartner, R.2    Renner, C.3    Marahiel, M.A.4    Holak, T.A.5
  • 25
    • 0036899405 scopus 로고    scopus 로고
    • Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis
    • T. Rehm, R. Huber, and T.A. Holak Application of NMR in structural proteomics: screening for proteins amenable to structural analysis Structure (Camb.) 10 2002 1613 1618
    • (2002) Structure (Camb.) , vol.10 , pp. 1613-1618
    • Rehm, T.1    Huber, R.2    Holak, T.A.3
  • 27
    • 0028215362 scopus 로고
    • Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation
    • P.C. Ma, M.A. Rould, H. Weintraub, and C.O. Pabo Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation Cell 77 1994 451 459
    • (1994) Cell , vol.77 , pp. 451-459
    • Ma, P.C.1    Rould, M.A.2    Weintraub, H.3    Pabo, C.O.4
  • 28
    • 0025273737 scopus 로고
    • The regions of the retinoblastoma protein needed for binding to adenovirus E1A or SV40 large T antigen are common sites for mutations
    • Q.J. Hu, N. Dyson, and E. Harlow The regions of the retinoblastoma protein needed for binding to adenovirus E1A or SV40 large T antigen are common sites for mutations EMBO J. 9 1990 1147 1155
    • (1990) EMBO J. , vol.9 , pp. 1147-1155
    • Hu, Q.J.1    Dyson, N.2    Harlow, E.3
  • 29
    • 0025340056 scopus 로고
    • Two distinct and frequently mutated regions of retinoblastoma protein are required for binding to SV40 T antigen
    • S. Huang, N.P. Wang, B.Y. Tseng, W.H. Lee, and E.H. Lee Two distinct and frequently mutated regions of retinoblastoma protein are required for binding to SV40 T antigen EMBO J. 9 1990 1815 1822
    • (1990) EMBO J. , vol.9 , pp. 1815-1822
    • Huang, S.1    Wang, N.P.2    Tseng, B.Y.3    Lee, W.H.4    Lee, E.H.5
  • 30
    • 2642601106 scopus 로고    scopus 로고
    • Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7
    • J.O. Lee, A.A. Russo, and N.P. Pavletich Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7 Nature 391 1998 859 865
    • (1998) Nature , vol.391 , pp. 859-865
    • Lee, J.O.1    Russo, A.A.2    Pavletich, N.P.3
  • 31
    • 0029762617 scopus 로고    scopus 로고
    • Domains a and B in the Rb pocket interact to form a transcriptional repressor motif
    • K.N. Chow, and D.C. Dean Domains A and B in the Rb pocket interact to form a transcriptional repressor motif Mol. Cell. Biol. 16 1996 4862 4868
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4862-4868
    • Chow, K.N.1    Dean, D.C.2
  • 32
    • 0025287564 scopus 로고
    • Definition of the minimal simian virus 40 large T antigen- and adenovirus E1A-binding domain in the retinoblastoma gene product
    • W.G. Kaelin Jr., M.E. Ewen, and D.M. Livingston Definition of the minimal simian virus 40 large T antigen- and adenovirus E1A-binding domain in the retinoblastoma gene product Mol. Cell. Biol. 10 1990 3761 3769
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3761-3769
    • Kaelin Jr., W.G.1    Ewen, M.E.2    Livingston, D.M.3
  • 35
    • 0027429964 scopus 로고
    • A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle
    • P.J. Welch, and J.Y. Wang A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle Cell 75 1993 779 790
    • (1993) Cell , vol.75 , pp. 779-790
    • Welch, P.J.1    Wang, J.Y.2
  • 36
    • 0033553577 scopus 로고    scopus 로고
    • Intact functional domains of the retinoblastoma gene product (pRb) are required for downregulation of telomerase activity
    • D.C. Nguyen, and D.L. Crowe Intact functional domains of the retinoblastoma gene product (pRb) are required for downregulation of telomerase activity Biochim. Biophys. Acta 1445 1999 207 215
    • (1999) Biochim. Biophys. Acta , vol.1445 , pp. 207-215
    • Nguyen, D.C.1    Crowe, D.L.2
  • 37
    • 0030773139 scopus 로고    scopus 로고
    • Identification of proteins that interact with a protein of interest: Applications of the yeast two-hybrid system
    • R.D. Gietz, B. Triggs-Raine, A. Robbins, K.C. Graham, and R.A. Woods Identification of proteins that interact with a protein of interest: applications of the yeast two-hybrid system Mol. Cell. Biochem. 172 1997 67 79
    • (1997) Mol. Cell. Biochem. , vol.172 , pp. 67-79
    • Gietz, R.D.1    Triggs-Raine, B.2    Robbins, A.3    Graham, K.C.4    Woods, R.A.5
  • 38
    • 0034847625 scopus 로고    scopus 로고
    • Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions
    • G.G. Toby, and E.A. Golemis Using the yeast interaction trap and other two-hybrid-based approaches to study protein-protein interactions Methods 24 2001 201 217
    • (2001) Methods , vol.24 , pp. 201-217
    • Toby, G.G.1    Golemis, E.A.2
  • 40
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • B. Meyer, and T. Peters NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors Angew. Chem., Int. Ed. Engl. 42 2003 864 890
    • (2003) Angew. Chem., Int. Ed. Engl. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 48
    • 0032695604 scopus 로고    scopus 로고
    • P57(Kip2) stabilizes the MyoD protein by inhibiting cyclin E-Cdk2 kinase activity in growing myoblasts
    • E.G. Reynaud, K. Pelpel, M. Guillier, M.P. Leibovitch, and S.A. Leibovitch p57(Kip2) stabilizes the MyoD protein by inhibiting cyclin E-Cdk2 kinase activity in growing myoblasts Mol. Cell. Biol. 19 1999 7621 7629
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7621-7629
    • Reynaud, E.G.1    Pelpel, K.2    Guillier, M.3    Leibovitch, M.P.4    Leibovitch, S.A.5
  • 49
    • 0031594780 scopus 로고    scopus 로고
    • P27Kip1 is expressed transiently in developing myotomes and enhances myogenesis
    • S.D. Zabludoff, M. Csete, R. Wagner, X. Yu, and B.J. Wold p27Kip1 is expressed transiently in developing myotomes and enhances myogenesis Cell Growth Differ. 9 1998 1 11
    • (1998) Cell Growth Differ. , vol.9 , pp. 1-11
    • Zabludoff, S.D.1    Csete, M.2    Wagner, R.3    Yu, X.4    Wold, B.J.5
  • 50
    • 0034609818 scopus 로고    scopus 로고
    • Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins
    • A. Lasorella, M. Noseda, M. Beyna, Y. Yokota, and A. Iavarone Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins Nature 407 2000 592 598
    • (2000) Nature , vol.407 , pp. 592-598
    • Lasorella, A.1    Noseda, M.2    Beyna, M.3    Yokota, Y.4    Iavarone, A.5
  • 51
    • 0030879868 scopus 로고    scopus 로고
    • Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins
    • S. Prabhu, A. Ignatova, S.T. Park, and X.H. Sun Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins Mol. Cell. Biol. 17 1997 5888 5896
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5888-5896
    • Prabhu, S.1    Ignatova, A.2    Park, S.T.3    Sun, X.H.4
  • 52
    • 0026652346 scopus 로고
    • A cDNA encoding a pRB-binding protein with properties of the transcription factor E2F
    • K. Helin, J.A. Lees, M. Vidal, N. Dyson, E. Harlow, and A. Fattaey A cDNA encoding a pRB-binding protein with properties of the transcription factor E2F Cell 70 1992 337 350
    • (1992) Cell , vol.70 , pp. 337-350
    • Helin, K.1    Lees, J.A.2    Vidal, M.3    Dyson, N.4    Harlow, E.5    Fattaey, A.6
  • 53
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • D.O. Morgan Cyclin-dependent kinases: engines, clocks, and microprocessors Annu. Rev. Cell Dev. Biol. 13 1997 261 291
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 54
    • 0034719111 scopus 로고    scopus 로고
    • Oligomerization properties of the viral oncoproteins adenovirus E1A and human papillomavirus E7 and their complexes with the retinoblastoma protein
    • A. Clements, K. Johnston, J.M. Mazzarelli, R.P. Ricciardi, and R. Marmorstein Oligomerization properties of the viral oncoproteins adenovirus E1A and human papillomavirus E7 and their complexes with the retinoblastoma protein Biochemistry 39 2000 16033 16045
    • (2000) Biochemistry , vol.39 , pp. 16033-16045
    • Clements, A.1    Johnston, K.2    Mazzarelli, J.M.3    Ricciardi, R.P.4    Marmorstein, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.