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Volumn 382, Issue 3, 2009, Pages 593-597

O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y

Author keywords

NF Y; O GlcNAc; Sp1; Transcription with NF Y

Indexed keywords

N ACETYLGLUCOSAMINE; NF Y TRANSCRIPTION FACTOR; SERINE; THREONINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SP1; UNCLASSIFIED DRUG;

EID: 64049092248     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.075     Document Type: Article
Times cited : (22)

References (25)
  • 1
    • 44749090905 scopus 로고    scopus 로고
    • Sp1: Emerging roles-beyond constitutive activation of TATA-less housekeeping genes
    • Wierstra I. Sp1: Emerging roles-beyond constitutive activation of TATA-less housekeeping genes. Biochem. Biophys. Res. Commun. 372 (2008) 1-13
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 1-13
    • Wierstra, I.1
  • 2
    • 0024290265 scopus 로고
    • Distinct regions of Sp1 modulate DNA binding and transcriptional activation
    • Kadonaga J.T., Courey A.J., Ladika J., and Tjian R. Distinct regions of Sp1 modulate DNA binding and transcriptional activation. Science 242 (1988) 1566-1570
    • (1988) Science , vol.242 , pp. 1566-1570
    • Kadonaga, J.T.1    Courey, A.J.2    Ladika, J.3    Tjian, R.4
  • 3
    • 15744393419 scopus 로고    scopus 로고
    • Sp1: regulation of gene expression by phosphorylation
    • Chu S., and Ferro T.J. Sp1: regulation of gene expression by phosphorylation. Gene 348 (2005) 1-11
    • (2005) Gene , vol.348 , pp. 1-11
    • Chu, S.1    Ferro, T.J.2
  • 4
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation
    • Jackson S.P., and Tjian R. O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell 55 (1988) 125-133
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 5
    • 0030772457 scopus 로고    scopus 로고
    • O-glycosylation of a Sp1-derived peptide blocks known Sp1 protein interactions
    • Roos M.D., Su K., Baker J.R., and Kudlow J.E. O-glycosylation of a Sp1-derived peptide blocks known Sp1 protein interactions. Mol. Cell. Biol. 17 (1997) 6472-6480
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6472-6480
    • Roos, M.D.1    Su, K.2    Baker, J.R.3    Kudlow, J.E.4
  • 6
    • 0035811072 scopus 로고    scopus 로고
    • O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
    • Yang X., Su K., Roos M.D., Chang Q., and Kudlow J.E. O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc. Natl. Acad. Sci. USA 98 (2001) 6611-6616
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6611-6616
    • Yang, X.1    Su, K.2    Roos, M.D.3    Chang, Q.4    Kudlow, J.E.5
  • 7
    • 33746904776 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1
    • Lim K., and Chang H.I. O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1. FEBS Lett. 580 (2006) 4645-4652
    • (2006) FEBS Lett. , vol.580 , pp. 4645-4652
    • Lim, K.1    Chang, H.I.2
  • 8
    • 58649098191 scopus 로고    scopus 로고
    • O-GlcNAc modification of Sp1 inhibits the functional interaction between Sp1 and Oct1
    • Lim K., and Chang H.I. O-GlcNAc modification of Sp1 inhibits the functional interaction between Sp1 and Oct1. FEBS Lett. 583 (2009) 512-520
    • (2009) FEBS Lett. , vol.583 , pp. 512-520
    • Lim, K.1    Chang, H.I.2
  • 9
    • 60549087667 scopus 로고    scopus 로고
    • O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription factors
    • Lim K., and Chang H.I. O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription factors. Biochem. Biophys. Res. Commun. 380 (2009) 569-574
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 569-574
    • Lim, K.1    Chang, H.I.2
  • 11
    • 0032851812 scopus 로고    scopus 로고
    • The molecular biology of the CCAAT-binding factor NF-Y
    • Mantovani R. The molecular biology of the CCAAT-binding factor NF-Y. Gene 239 (1999) 15-27
    • (1999) Gene , vol.239 , pp. 15-27
    • Mantovani, R.1
  • 13
    • 0034674552 scopus 로고    scopus 로고
    • Sp family members and nuclear factor-Y cooperatively stimulate transcription from the rat pyruvate kinase M gene distal promoter region via their direct interactions
    • Yamada K., Tanaka T., Miyamoto K., and Noguchi T. Sp family members and nuclear factor-Y cooperatively stimulate transcription from the rat pyruvate kinase M gene distal promoter region via their direct interactions. J. Biol. Chem. 275 (2000) 18129-18137
    • (2000) J. Biol. Chem. , vol.275 , pp. 18129-18137
    • Yamada, K.1    Tanaka, T.2    Miyamoto, K.3    Noguchi, T.4
  • 15
    • 41949114259 scopus 로고    scopus 로고
    • Positive regulation of promoter activity of human 3-phosphoglycerate dehydrogenase (PHGDH) gene is mediated by transcription factors Sp1 and NF-Y
    • Jun D.Y., Park H.S., Lee J.Y., Baek J.Y., Park H.K., Fukui K., and Kim Y.H. Positive regulation of promoter activity of human 3-phosphoglycerate dehydrogenase (PHGDH) gene is mediated by transcription factors Sp1 and NF-Y. Gene 414 (2008) 106-114
    • (2008) Gene , vol.414 , pp. 106-114
    • Jun, D.Y.1    Park, H.S.2    Lee, J.Y.3    Baek, J.Y.4    Park, H.K.5    Fukui, K.6    Kim, Y.H.7
  • 16
    • 0035396768 scopus 로고    scopus 로고
    • Transcription regulation of human cystathionine β-synthase-1b basal promoter: synergistic transcription by transcription factors NF-Y and Sp1/Sp3
    • Yubin G.E., Konrad M.A., Matherly L.H., and Taub J.W. Transcription regulation of human cystathionine β-synthase-1b basal promoter: synergistic transcription by transcription factors NF-Y and Sp1/Sp3. Biochem. J. 357 (2001) 97-105
    • (2001) Biochem. J. , vol.357 , pp. 97-105
    • Yubin, G.E.1    Konrad, M.A.2    Matherly, L.H.3    Taub, J.W.4
  • 17
    • 0034674679 scopus 로고    scopus 로고
    • NF-Y and Sp1 cooperate for the transcriptional activation and cAMP response of human inhibitor of metalloproteinases-2
    • Zhong Z.D., Hammani K., Bae W.S., and DeClerck Y.A. NF-Y and Sp1 cooperate for the transcriptional activation and cAMP response of human inhibitor of metalloproteinases-2. J. Biol. Chem. 275 (2000) 18602-18610
    • (2000) J. Biol. Chem. , vol.275 , pp. 18602-18610
    • Zhong, Z.D.1    Hammani, K.2    Bae, W.S.3    DeClerck, Y.A.4
  • 18
    • 0036183134 scopus 로고    scopus 로고
    • Characterization of human cathepsin L promoter and identification of binding sites for NF-Y, Sp1 and Sp3 that are essential for its activity
    • Jean D., Guillaume N., Frade R., and promoter C.o.h.c.L. Characterization of human cathepsin L promoter and identification of binding sites for NF-Y, Sp1 and Sp3 that are essential for its activity. Biochem. J. 361 (2002) 173-184
    • (2002) Biochem. J. , vol.361 , pp. 173-184
    • Jean, D.1    Guillaume, N.2    Frade, R.3    promoter, C.o.h.c.L.4
  • 19
    • 0032966918 scopus 로고    scopus 로고
    • Interaction between the two ubiquitously expressed transcription factors NF-Y and Sp1
    • Roder K., Wolf S.S., Larkin K.J., and Schweizer M. Interaction between the two ubiquitously expressed transcription factors NF-Y and Sp1. Gene 234 (1999) 61-69
    • (1999) Gene , vol.234 , pp. 61-69
    • Roder, K.1    Wolf, S.S.2    Larkin, K.J.3    Schweizer, M.4
  • 20
    • 29644436424 scopus 로고    scopus 로고
    • Streptozotocin inhibits O-GlcNAcase via the production of a transition state analog
    • Toleman C., Paterson A.J., Shin R., and Kudlow J.E. Streptozotocin inhibits O-GlcNAcase via the production of a transition state analog. Biochem. Biophys. Res. Commun. 340 (2006) 526-534
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 526-534
    • Toleman, C.1    Paterson, A.J.2    Shin, R.3    Kudlow, J.E.4
  • 21
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang W.H., Kim J.E., Nam H.W., Ju J.W., Kim H.S., Kim Y.S., and Cho J.W. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat. Cell Biol. 8 (2006) 1074-1083
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6    Cho, J.W.7
  • 22
    • 33645646866 scopus 로고    scopus 로고
    • Insulin dynamically regulates calmodulin gene expression by sequential O-glycosylation and phosphorylation of Sp1 and its subcellular compartmentalization in liver cells
    • Majumdar G., Harrington A., Hungerford J., Martinez-Hernandez A., Gerling I.C., Raghow R., and Solomon S. Insulin dynamically regulates calmodulin gene expression by sequential O-glycosylation and phosphorylation of Sp1 and its subcellular compartmentalization in liver cells. J. Biol. Chem. 281 (2006) 3642-3650
    • (2006) J. Biol. Chem. , vol.281 , pp. 3642-3650
    • Majumdar, G.1    Harrington, A.2    Hungerford, J.3    Martinez-Hernandez, A.4    Gerling, I.C.5    Raghow, R.6    Solomon, S.7
  • 23
    • 50349093142 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity
    • Copeland R.J., Bullen J.W., and Hart G.W. Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity. Am. J. Physiol. Endocrinol. Metab. 295 (2008) E17-28
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.295
    • Copeland, R.J.1    Bullen, J.W.2    Hart, G.W.3
  • 24
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F., Su K., Yang X., Bowe D.B., Paterson A.J., and Kudlow J.E. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115 (2003) 715-725
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.