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Volumn 30, Issue 8, 2016, Pages 960-972

Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes

Author keywords

O GlcNAcylation; Post translation modifications; Proteolysis

Indexed keywords

2 LINKED N ACETYLGLUCOSAMINE TRANSFERASE; GLYCOSYLTRANSFERASE; HOST CELL FACTOR C1; SERINE; THREONINE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; HCFC1 PROTEIN, HUMAN; N ACETYLGLUCOSAMINYLTRANSFERASE; O-GLCNAC TRANSFERASE; UDP-N-ACETYLGLUCOSAMINE-PEPTIDE BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE;

EID: 84963852308     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.275925.115     Document Type: Article
Times cited : (17)

References (36)
  • 3
    • 35148901465 scopus 로고    scopus 로고
    • Species selectivity of mixedlineage leukemia/trithorax and HCF proteolytic maturation pathways
    • Capotosti F, Hsieh JJ, HerrW. 2007. Species selectivity of mixedlineage leukemia/trithorax and HCF proteolytic maturation pathways. Mol Cell Biol 27: 7063-7072.
    • (2007) Mol Cell Biol , vol.27 , pp. 7063-7072
    • Capotosti, F.1    Hsieh, J.J.2    Herr, W.3
  • 6
    • 84907698574 scopus 로고    scopus 로고
    • O-GlcNAcylation, an epigenetic mark. Focus on the histone code, TET family proteins, and Polycomb group proteins
    • Dehennaut V, Leprince D, Lefebvre T. 2014. O-GlcNAcylation, an epigenetic mark. Focus on the histone code, TET family proteins, and Polycomb group proteins. Front Endocrinol (Lausanne) 5: 155.
    • (2014) Front Endocrinol (Lausanne) , vol.5 , pp. 155
    • Dehennaut, V.1    Leprince, D.2    Lefebvre, T.3
  • 7
    • 77953292595 scopus 로고    scopus 로고
    • Post-translational modifications in signal integration
    • Deribe YL, Pawson T, Dikic I. 2010. Post-translational modifications in signal integration. Nat Struct Mol Biol 17: 666-672.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 666-672
    • Deribe, Y.L.1    Pawson, T.2    Dikic, I.3
  • 8
    • 84949108534 scopus 로고    scopus 로고
    • A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin
    • Gambetta M, Müller J. 2015. A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin. Chromosoma 124: 429-442.
    • (2015) Chromosoma , vol.124 , pp. 429-442
    • Gambetta, M.1    Müller, J.2
  • 9
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • Gambetta MC, Oktaba K, Muller J. 2009. Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325: 93-96.
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Muller, J.3
  • 11
    • 23844481789 scopus 로고    scopus 로고
    • A Caenorhabditis elegans model of insulin resistance: Altered macronutrient storage and dauer formation in an OGT-1 knockout
    • Hanover JA, Forsythe ME, Hennessey PT, Brodigan TM, Love DC, Ashwell G, Krause M. 2005. A Caenorhabditis elegans model of insulin resistance: altered macronutrient storage and dauer formation in an OGT-1 knockout. Proc Natl Acad Sci 102: 11266-11271.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 11266-11271
    • Hanover, J.A.1    Forsythe, M.E.2    Hennessey, P.T.3    Brodigan, T.M.4    Love, D.C.5    Ashwell, G.6    Krause, M.7
  • 12
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: Linking metabolism to epigenetics throughO-GlcNAcylation
    • Hanover JA, Krause MW, Love DC. 2012. Bittersweet memories: linking metabolism to epigenetics throughO-GlcNAcylation. Nat Rev Mol Cell Biol 13: 312-321.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 312-321
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 13
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O. 2011. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem 80: 825-858.
    • (2011) Annu Rev Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 14
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
    • Iyer SP, Hart GW. 2003. Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J Biol Chem 278: 24608-24616.
    • (2003) J Biol Chem , vol.278 , pp. 24608-24616
    • Iyer, S.P.1    Hart, G.W.2
  • 15
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
    • Jinek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, Conti E. 2004. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α. Nat Struct Mol Biol 11: 1001-1007.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1001-1007
    • Jinek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 16
    • 84952937323 scopus 로고    scopus 로고
    • Proteolytic cleavage driven by glycosylation
    • KötzlerMP,Withers SG. 2016. Proteolytic cleavage driven by glycosylation. J Biol Chem 291: 429-434.
    • (2016) J Biol Chem , vol.291 , pp. 429-434
    • Kötzler, M.P.1    Withers, S.G.2
  • 17
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel LK, HartGW. 1999. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 274: 32015-32022.
    • (1999) J Biol Chem , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 18
    • 0028904801 scopus 로고
    • The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides
    • Kristie TM, Pomerantz JL, Twomey TC, Parent SA, Sharp PA. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J Biol Chem 270: 4387-4394.
    • (1995) J Biol Chem , vol.270 , pp. 4387-4394
    • Kristie, T.M.1    Pomerantz, J.L.2    Twomey, T.C.3    Parent, S.A.4    Sharp, P.A.5
  • 19
    • 27444447560 scopus 로고    scopus 로고
    • Mutational analysis of the catalytic domain ofO-linked N-acetylglucosaminyl transferase
    • Lazarus BD, Roos MD, Hanover JA. 2005. Mutational analysis of the catalytic domain ofO-linked N-acetylglucosaminyl transferase. J Biol Chem 280: 35537-35544.
    • (2005) J Biol Chem , vol.280 , pp. 35537-35544
    • Lazarus, B.D.1    Roos, M.D.2    Hanover, J.A.3
  • 20
    • 33646159532 scopus 로고    scopus 로고
    • Recombinant OGlcNAc transferase isoforms: Identification ofO-GlcNAcase, yes tyrosine kinase, and τ as isoform-specific substrates
    • Lazarus BD, Love DC, Hanover JA. 2006. Recombinant OGlcNAc transferase isoforms: identification ofO-GlcNAcase, yes tyrosine kinase, and τ as isoform-specific substrates. Glycobiology 16: 415-421.
    • (2006) Glycobiology , vol.16 , pp. 415-421
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 21
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S. 2011. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469: 564-567.
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 23
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
    • Lubas WA, Hanover JA. 2000. Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J Biol Chem 275: 10983-10988.
    • (2000) J Biol Chem , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 25
    • 84867905135 scopus 로고    scopus 로고
    • HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation
    • Park J, Lammers F, Herr W, Song JJ. 2012. HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation. Proc Natl Acad Sci 109: 17430-17435.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 17430-17435
    • Park, J.1    Lammers, F.2    Herr, W.3    Song, J.J.4
  • 32
    • 84908151229 scopus 로고    scopus 로고
    • Histone core modifications regulating nucleosome structure and dynamics
    • Tessarz P, Kouzarides T. 2014. Histone core modifications regulating nucleosome structure and dynamics. Nat Rev Mol Cell Biol 15: 703-708.
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 703-708
    • Tessarz, P.1    Kouzarides, T.2
  • 33
    • 0027328280 scopus 로고
    • The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein
    • Wilson AC, LaMarco K, Peterson MG, Herr W. 1993. The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein. Cell 74: 115-125.
    • (1993) Cell , vol.74 , pp. 115-125
    • Wilson, A.C.1    LaMarco, K.2    Peterson, M.G.3    Herr, W.4
  • 34
    • 0028860944 scopus 로고
    • The HCF repeat is an unusual proteolytic cleavage signal
    • Wilson AC, Peterson MG, Herr W. 1995. The HCF repeat is an unusual proteolytic cleavage signal. Genes Dev 9: 2445-2458.
    • (1995) Genes Dev , vol.9 , pp. 2445-2458
    • Wilson, A.C.1    Peterson, M.G.2    Herr, W.3
  • 35
    • 0037382574 scopus 로고    scopus 로고
    • Human Sin3 deacetylase and trithorax-related Set1/ Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1
    • Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W. 2003. Human Sin3 deacetylase and trithorax-related Set1/ Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev 17: 896-911.
    • (2003) Genes Dev , vol.17 , pp. 896-911
    • Wysocka, J.1    Myers, M.P.2    Laherty, C.D.3    Eisenman, R.N.4    Herr, W.5
  • 36
    • 84864088377 scopus 로고    scopus 로고
    • Role of host cell factor-1 in cell cycle regulation
    • Zargar Z, Tyagi S. 2012. Role of host cell factor-1 in cell cycle regulation. Transcription 3: 187-192.
    • (2012) Transcription , vol.3 , pp. 187-192
    • Zargar, Z.1    Tyagi, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.