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Volumn 53, Issue 12, 2004, Pages 3184-3192

Insulin stimulates and diabetes inhibits O-linked N-acetylglucosamine transferase and O-glycosylation of Sp1

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; GLUCAGON; INSULIN; N ACETYLGLUCOSAMINE; PHOSPHORUS 32; TRANSCRIPTION FACTOR SP1; TRANSFERASE;

EID: 9444252281     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.53.12.3184     Document Type: Article
Times cited : (50)

References (29)
  • 1
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White MF, Kahn CR: The insulin signaling system. J Biol Chem 269:1-4, 1994
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 2
    • 0042415031 scopus 로고    scopus 로고
    • Molecular mechanisms of insulin modulated signaling and regulation of gene transcription
    • Solomon SS, Raghow R: Molecular mechanisms of insulin modulated signaling and regulation of gene transcription. Recent Res Dev Endocrinol 3:79-99, 2002
    • (2002) Recent Res Dev Endocrinol , vol.3 , pp. 79-99
    • Solomon, S.S.1    Raghow, R.2
  • 3
  • 4
    • 0030775338 scopus 로고    scopus 로고
    • Transcription factor Sp1 is necessary for basal calmodulin gene transcription and for its selective stimulation by insulin
    • Solomon SS, Palazzolo MR, Takahashi T, Raghow R: Transcription factor Sp1 is necessary for basal calmodulin gene transcription and for its selective stimulation by insulin. Endocrinology 138:5052-5054, 1997
    • (1997) Endocrinology , vol.138 , pp. 5052-5054
    • Solomon, S.S.1    Palazzolo, M.R.2    Takahashi, T.3    Raghow, R.4
  • 5
    • 0035052395 scopus 로고    scopus 로고
    • Insulin deprivation leads to deficiency of Sp1 transcription factor in H-411E hepatoma cells and in streptozotocin-induced diabetic ketoacidosis in the rat
    • Pan X, Solomon SS, Borromeo DM, Martinez-Hernandez A, Raghow R: Insulin deprivation leads to deficiency of Sp1 transcription factor in H-411E hepatoma cells and in streptozotocin-induced diabetic ketoacidosis in the rat. Endocrinology 142:1635-1642, 2001
    • (2001) Endocrinology , vol.142 , pp. 1635-1642
    • Pan, X.1    Solomon, S.S.2    Borromeo, D.M.3    Martinez-Hernandez, A.4    Raghow, R.5
  • 7
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
    • Jackson SP, Tjian R: O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell 55:125-133, 1988
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 8
    • 0034703095 scopus 로고    scopus 로고
    • O-glycosylation of nuclear and cytosolic proteins: Dynamic interplay between O-GlcNAc and O-phosphate
    • Comer FI, Hart GW: O-Glycosylation of nuclear and cytosolic proteins: dynamic interplay between O-GlcNAc and O-phosphate. J Biol Chem 275:29179-29182, 2000
    • (2000) J Biol Chem , vol.275 , pp. 29179-29182
    • Comer, F.I.1    Hart, G.W.2
  • 9
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells L, Vosseller K, Hart GW: Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291:2376-2378, 2001
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 10
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart GW: Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu Rev Biochem 66:315-335, 1997
    • (1997) Annu Rev Biochem , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 11
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • Zachara NE, Hart GW: The emerging significance of O-GlcNAc in cellular regulation. Chem Rev 102:431-438, 2002
    • (2002) Chem Rev , vol.102 , pp. 431-438
    • Zachara, N.E.1    Hart, G.W.2
  • 13
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSinSA: Coupling protein O-GlcNAcylation to transcriptional repression
    • Yang X, Zhang F, Kudlow JE: Recruitment of O-GlcNAc transferase to promoters by corepressor mSinSA: coupling protein O-GlcNAcylation to transcriptional repression. Cell 110:69-80, 2002
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 14
    • 0016681097 scopus 로고
    • Effect of insulin and lipolyttc hormones on cyclic AMP phosphodieterase activity in normal and diabetic rat adipose tissue
    • Solomon SS: Effect of insulin and lipolyttc hormones on cyclic AMP phosphodieterase activity in normal and diabetic rat adipose tissue. Endocrinology 96:1366-1373, 1975
    • (1975) Endocrinology , vol.96 , pp. 1366-1373
    • Solomon, S.S.1
  • 16
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosamlnyltransferase
    • Haltiwanger RS, Holt GD, Hart GW: Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosamlnyltransferase. J Biol Chem 265:2563-2568, 1990
    • (1990) J Biol Chem , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 17
    • 0036834748 scopus 로고    scopus 로고
    • The role of O-linked protein glycosylation in beta-cell dysfunction
    • Konrad RJ, Kudlow JE: The role of O-linked protein glycosylation in beta-cell dysfunction. Int J Mol Med 10:535-539, 2002
    • (2002) Int J Mol Med , vol.10 , pp. 535-539
    • Konrad, R.J.1    Kudlow, J.E.2
  • 18
    • 0344642959 scopus 로고    scopus 로고
    • Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
    • Akimoto Y, Comer FI, Cole RN, Kudo A, Kawakami H, Hirano H, Hart GW: Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex. Brain Res 966:194-205, 2003
    • (2003) Brain Res , vol.966 , pp. 194-205
    • Akimoto, Y.1    Comer, F.I.2    Cole, R.N.3    Kudo, A.4    Kawakami, H.5    Hirano, H.6    Hart, G.W.7
  • 19
    • 0033080192 scopus 로고    scopus 로고
    • Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells
    • Hanover JA, Lai Z, Lee G, Lubas WA, Sato SM: Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells. Arch Biochem Biophys 362:38-45, 1999
    • (1999) Arch Biochem Biophys , vol.362 , pp. 38-45
    • Hanover, J.A.1    Lai, Z.2    Lee, G.3    Lubas, W.A.4    Sato, S.M.5
  • 20
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE: O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115:715-725, 2003
    • (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
  • 21
    • 0037199916 scopus 로고    scopus 로고
    • Lipopolysaccharide down-regulates Sp1 binding activity by promoting Sp1 protein dephosphorylation and degradation
    • Ye X, Liu SF: Lipopolysaccharide down-regulates Sp1 binding activity by promoting Sp1 protein dephosphorylation and degradation. J Biol Chem 277:31863-31870, 2002
    • (2002) J Biol Chem , vol.277 , pp. 31863-31870
    • Ye, X.1    Liu, S.F.2
  • 22
    • 0345277743 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: A new paradigm for metabolic control of signal transduction and transcription
    • Kamemura K, Hart GW: Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: a new paradigm for metabolic control of signal transduction and transcription. Prog Nucleic Acid Res Mol Biol 73:107-136, 2003
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.73 , pp. 107-136
    • Kamemura, K.1    Hart, G.W.2
  • 23
    • 0035971067 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor beta: Post-translational regulation of turnover and transactivation activity
    • Cheng X, Hart GW: Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor beta: post-translational regulation of turnover and transactivation activity. J Biol Chem 276:10570-10575, 2001
    • (2001) J Biol Chem , vol.276 , pp. 10570-10575
    • Cheng, X.1    Hart, G.W.2
  • 24
    • 0141884304 scopus 로고    scopus 로고
    • Dynamic interplay between O-GlcNAc and O-phosphate: The sweet side of protein regulation
    • Slawson C, Hart GW: Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation. Curr Opin Struct Biol 13:631-636, 2003
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 631-636
    • Slawson, C.1    Hart, G.W.2
  • 25
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I, Kudlow JE: Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol Cell Biol 17:2550-2558, 1997
    • (1997) Mol Cell Biol , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 26
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N- acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene) anuno-N-phenylcarbamate
    • Haltiwanger RS, Grove K, Philipsberg GA: Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy- D-glucopyranosylidene)anuno-N-phenylcarbamate. J Biol Chem 273:3611-3617, 1998
    • (1998) J Biol Chem , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 28
    • 0000012487 scopus 로고
    • Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins
    • Hart GW, Geis KD, Dong L-Y., Blomberg M.A., Chou T-Y: Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins. Pure Appl Chem 67:1637-1645, 1995
    • (1995) Pure Appl Chem , vol.67 , pp. 1637-1645
    • Hart, G.W.1    Geis, K.D.2    Dong, L.-Y.3    Blomberg, M.A.4    Chou, T.-Y.5
  • 29
    • 0035811072 scopus 로고    scopus 로고
    • O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
    • Yang X, Su K, Roos MD, Chang Q, Paterson AJ, Kudlow JE: O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc Natl Acad Sci USA 98:6611-6616, 2001
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6611-6616
    • Yang, X.1    Su, K.2    Roos, M.D.3    Chang, Q.4    Paterson, A.J.5    Kudlow, J.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.