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Volumn 504, Issue 2, 2012, Pages 213-219

Interplay between two myogenesis-related proteins: TBP-interacting protein 120B and MyoD

Author keywords

CAND2; MyoD; Myogenesis; TIP120B; Transcriptional regulation

Indexed keywords

DEXAMETHASONE; MYOD PROTEIN; MYOGENIN; PROTEASOME; PROTEIN; TATA BINDING PROTEIN INTERACTING PROTEIN 120B; UNCLASSIFIED DRUG;

EID: 84862768812     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.05.022     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0033546750 scopus 로고    scopus 로고
    • TIP120B: a novel TIP120-family protein that is expressed specifically in muscle tissues
    • Aoki T., et al. TIP120B: a novel TIP120-family protein that is expressed specifically in muscle tissues. Biochem. Biophys. Res. Commun. 1999, 261:911-916.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 911-916
    • Aoki, T.1
  • 2
    • 0036387131 scopus 로고    scopus 로고
    • TBP-interacting protein 120B, which is induced in relation to myogenesis, binds to NOT3
    • Aoki T., Okada N., Wakamatsu T., Tamura T.A. TBP-interacting protein 120B, which is induced in relation to myogenesis, binds to NOT3. Biochem. Biophys. Res. Commun. 2002, 296:1097-1103.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1097-1103
    • Aoki, T.1    Okada, N.2    Wakamatsu, T.3    Tamura, T.A.4
  • 3
    • 24344491888 scopus 로고    scopus 로고
    • MyoD and the transcriptional control of myogenesis
    • Berkes C.A., Tapscott S.J. MyoD and the transcriptional control of myogenesis. Semin. Cell Dev. Biol. 2005, 16:585-595.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 585-595
    • Berkes, C.A.1    Tapscott, S.J.2
  • 4
    • 0023663888 scopus 로고
    • Expression of a single transfected cDNA converts fibroblasts to myoblasts
    • Davis R.L., Weintraub H., Lassar A.B. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 1987, 51:987-1000.
    • (1987) Cell , vol.51 , pp. 987-1000
    • Davis, R.L.1    Weintraub, H.2    Lassar, A.B.3
  • 5
    • 22844434368 scopus 로고    scopus 로고
    • Homodimeric MyoD preferentially binds tetraplex structures of regulatory sequences of muscle-specific genes
    • Etzioni S., et al. Homodimeric MyoD preferentially binds tetraplex structures of regulatory sequences of muscle-specific genes. J. Biol. Chem. 2005, 280:26805-26812.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26805-26812
    • Etzioni, S.1
  • 6
    • 0029907306 scopus 로고    scopus 로고
    • Growth hormone and the insulin-like growth factor system in myogenesis
    • Florini J.R., Ewton D.Z., Coolican S.A. Growth hormone and the insulin-like growth factor system in myogenesis. Endocr. Rev. 1996, 17:481-517.
    • (1996) Endocr. Rev. , vol.17 , pp. 481-517
    • Florini, J.R.1    Ewton, D.Z.2    Coolican, S.A.3
  • 8
    • 0028941483 scopus 로고
    • Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD
    • Halevy O., et al. Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD. Science 1995, 267:1018-1021.
    • (1995) Science , vol.267 , pp. 1018-1021
    • Halevy, O.1
  • 9
    • 69249222488 scopus 로고    scopus 로고
    • Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase
    • Jogo M., Shiraishi S., Tamura T.A. Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase. FEBS Lett. 2009, 583:2715-2719.
    • (2009) FEBS Lett. , vol.583 , pp. 2715-2719
    • Jogo, M.1    Shiraishi, S.2    Tamura, T.A.3
  • 10
    • 0035074694 scopus 로고    scopus 로고
    • TBP-interacting protein TIP120A is a new global transcription activator with bipartite functional domains
    • Kayukawa K., Kitajima Y., Tamura T. TBP-interacting protein TIP120A is a new global transcription activator with bipartite functional domains. Genes Cells 2001, 6:165-174.
    • (2001) Genes Cells , vol.6 , pp. 165-174
    • Kayukawa, K.1    Kitajima, Y.2    Tamura, T.3
  • 11
    • 84655176710 scopus 로고    scopus 로고
    • Mouse Wee1 gene is repressed by Krüppel-like factor 3 (KLF3) via interaction with multiple upstream elements
    • Kitamura T., Suzuki H., Tamura T. Mouse Wee1 gene is repressed by Krüppel-like factor 3 (KLF3) via interaction with multiple upstream elements. Gene 2012, 25:361-367.
    • (2012) Gene , vol.25 , pp. 361-367
    • Kitamura, T.1    Suzuki, H.2    Tamura, T.3
  • 12
    • 0033025071 scopus 로고    scopus 로고
    • Transcriptional regulation of mouse type 1 inositol 1,4,5-trisphosphate receptor gene by NeuroD-related factor
    • Konishi Y., et al. Transcriptional regulation of mouse type 1 inositol 1,4,5-trisphosphate receptor gene by NeuroD-related factor. J. Neurochem. 1999, 72:1717-1724.
    • (1999) J. Neurochem. , vol.72 , pp. 1717-1724
    • Konishi, Y.1
  • 13
    • 39149134903 scopus 로고    scopus 로고
    • Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis
    • Koyama S., et al. Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis. J. Mol. Biol. 2008, 376:1224-1236.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1224-1236
    • Koyama, S.1
  • 14
    • 0024448304 scopus 로고
    • MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer
    • Lassar A.B., et al. MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer. Cell 1989, 58:823-831.
    • (1989) Cell , vol.58 , pp. 823-831
    • Lassar, A.B.1
  • 15
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker S.H., Solomon V., Mitch W.E., Goldberg A.L. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. 1999, 129:227S-237S.
    • (1999) J. Nutr. , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 16
    • 27144513736 scopus 로고    scopus 로고
    • E12 and E47 modulate cellular localization and proteasome-mediated degradation of MyoD and Id1
    • Lingbeck J.M., Trausch-Azar J.S., Ciechanover A., Schwartz A.L. E12 and E47 modulate cellular localization and proteasome-mediated degradation of MyoD and Id1. Oncogene 2005, 24:6376-6384.
    • (2005) Oncogene , vol.24 , pp. 6376-6384
    • Lingbeck, J.M.1    Trausch-Azar, J.S.2    Ciechanover, A.3    Schwartz, A.L.4
  • 17
    • 22744432989 scopus 로고    scopus 로고
    • CAND1 enhances deneddylation of CUL1 by COP9 signalosome
    • Min K.W., et al. CAND1 enhances deneddylation of CUL1 by COP9 signalosome. Biochem. Biophys. Res. Commun. 2005, 334:867-874.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 867-874
    • Min, K.W.1
  • 18
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway
    • Mitch W.E., Goldberg A.L. Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 1996, 335:1897-1905.
    • (1996) N. Engl. J. Med. , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 19
    • 0027297310 scopus 로고
    • Myogenin gene disruption results in perinatal lethality because of severe muscle defect
    • Nabeshima Y., et al. Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 1993, 364:532-535.
    • (1993) Nature , vol.364 , pp. 532-535
    • Nabeshima, Y.1
  • 20
    • 0033804899 scopus 로고    scopus 로고
    • Regulation of muscle regulatory factors by DNA-binding, interacting proteins, and post-transcriptional modifications
    • Puri P.L., Sartorelli V. Regulation of muscle regulatory factors by DNA-binding, interacting proteins, and post-transcriptional modifications. J. Cell. Physiol. 2000, 185:155-173.
    • (2000) J. Cell. Physiol. , vol.185 , pp. 155-173
    • Puri, P.L.1    Sartorelli, V.2
  • 21
    • 4544293878 scopus 로고    scopus 로고
    • IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
    • Sacheck J.M., Ohtsuka A., McLary S.C., Goldberg A.L. IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. Am. J. Physiol. Endocrinol. Metab. 2004, 287:591-601.
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.287 , pp. 591-601
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 23
    • 34247860685 scopus 로고    scopus 로고
    • TBP-interacting protein 120B (TIP120B)/cullin-associated and neddylation-dissociated 2 (CAND2) inhibits SCF-dependent ubiquitination of myogenin and accelerates myogenic differentiation
    • Shiraishi S., et al. TBP-interacting protein 120B (TIP120B)/cullin-associated and neddylation-dissociated 2 (CAND2) inhibits SCF-dependent ubiquitination of myogenin and accelerates myogenic differentiation. J. Biol. Chem. 2007, 282:9017-9028.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9017-9028
    • Shiraishi, S.1
  • 24
    • 0034464217 scopus 로고    scopus 로고
    • Dexamethasone inhibits insulin-like growth factor signaling and potentiates myoblast apoptosis
    • Singleton J.R., Baker B.L., Thorburn A. Dexamethasone inhibits insulin-like growth factor signaling and potentiates myoblast apoptosis. Endocrinology 2000, 141:2945-2950.
    • (2000) Endocrinology , vol.141 , pp. 2945-2950
    • Singleton, J.R.1    Baker, B.L.2    Thorburn, A.3
  • 25
    • 33751433640 scopus 로고    scopus 로고
    • Transcriptional repression of the mouse wee1 gene by TBP-related factor 2
    • Tanaka Y., et al. Transcriptional repression of the mouse wee1 gene by TBP-related factor 2. Biochem. Biophys. Res. Commun. 2006, 352:21-28.
    • (2006) Biochem. Biophys. Res. Commun. , vol.352 , pp. 21-28
    • Tanaka, Y.1
  • 26
    • 21644434750 scopus 로고    scopus 로고
    • The circuitry of a master switch: Myod and the regulation of skeletal muscle gene transcription
    • Tapscott S.J. The circuitry of a master switch: Myod and the regulation of skeletal muscle gene transcription. Development 2005, 132:2685-2695.
    • (2005) Development , vol.132 , pp. 2685-2695
    • Tapscott, S.J.1
  • 27
    • 0024406874 scopus 로고
    • Positive autoregulation of the myogenic determination gene MyoD1
    • Thayer M.J., et al. Positive autoregulation of the myogenic determination gene MyoD1. Cell 1989, 58:241-248.
    • (1989) Cell , vol.58 , pp. 241-248
    • Thayer, M.J.1
  • 28
    • 13244264946 scopus 로고    scopus 로고
    • Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase
    • Tintignac L.A., et al. Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase. J. Biol. Chem. 2005, 280:2847-2856.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2847-2856
    • Tintignac, L.A.1
  • 29
    • 0024381667 scopus 로고
    • Activation of muscle-specific genes in pigment, nerve, fat, liver, and fibroblast cell lines by forced expression of MyoD
    • Weintraub H., et al. Activation of muscle-specific genes in pigment, nerve, fat, liver, and fibroblast cell lines by forced expression of MyoD. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:5434-5438.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5434-5438
    • Weintraub, H.1
  • 30
    • 0025994343 scopus 로고
    • Muscle-specific transcriptional activation by MyoD
    • Weintraub H., et al. Muscle-specific transcriptional activation by MyoD. Genes Dev. 1991, 5:1377-1386.
    • (1991) Genes Dev. , vol.5 , pp. 1377-1386
    • Weintraub, H.1
  • 31
    • 0030582691 scopus 로고    scopus 로고
    • Molecular cloning of a novel 120-kDa TBP-interacting protein
    • Yogosawa S., et al. Molecular cloning of a novel 120-kDa TBP-interacting protein. Biochem. Biophys. Res. Commun. 1996, 229:612-617.
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 612-617
    • Yogosawa, S.1
  • 32
    • 0025339555 scopus 로고
    • Differential trans activation associated with the muscle regulatory factors MyoD1, myogenin, and MRF4
    • Yutzey K.E., Rhodes S.J., Konieczny S.F. Differential trans activation associated with the muscle regulatory factors MyoD1, myogenin, and MRF4. Mol. Cell. Biol. 1990, 10:3934-3944.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3934-3944
    • Yutzey, K.E.1    Rhodes, S.J.2    Konieczny, S.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.