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Volumn 33, Issue 8, 2013, Pages 1487-1502

A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; PROTEINASE; SIRTUIN 1; TRANSCRIPTION FACTOR SAGA; UBIQUITIN SPECIFIC PROTEASE 22; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 84876339680     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00971-12     Document Type: Article
Times cited : (52)

References (93)
  • 1
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 3
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny JC, Dowd GJ, Huang J, Hilz H, Moazed D. 1999. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99:735-745.
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 4
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye RA. 1999. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260:273-279.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 5
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • Guarente L. 2000. Sir2 links chromatin silencing, metabolism, and aging. Genes Dev. 14:1021-1026.
    • (2000) Genes Dev. , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 6
    • 4944245398 scopus 로고    scopus 로고
    • Human Sir T1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D. 2004. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16:93-105.
    • (2004) Mol. Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 10
    • 34548289502 scopus 로고    scopus 로고
    • Dynamic FoxO transcription factors
    • Huang H, Tindall DJ. 2007. Dynamic FoxO transcription factors. J. Cell Sci. 120:2479-2487.
    • (2007) J. Cell Sci. , vol.120 , pp. 2479-2487
    • Huang, H.1    Tindall, D.J.2
  • 13
    • 0242322010 scopus 로고    scopus 로고
    • Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)- interacting protein 2-mediated transcriptional repression
    • Senawong T, Peterson VJ, Avram D, Shepherd DM, Frye RA, Minucci S, Leid M. 2003. Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)- interacting protein 2-mediated transcriptional repression. J. Biol. Chem. 278:43041-43050.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43041-43050
    • Senawong, T.1    Peterson, V.J.2    Avram, D.3    Shepherd, D.M.4    Frye, R.A.5    Minucci, S.6    Leid, M.7
  • 14
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR
    • Li X, Zhang S, Blander G, Tse JG, Krieger M, Guarente L. 2007. SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell 28:91-106.
    • (2007) Mol. Cell , vol.28 , pp. 91-106
    • Li, X.1    Zhang, S.2    Blander, G.3    Tse, J.G.4    Krieger, M.5    Guarente, L.6
  • 17
    • 65349096174 scopus 로고    scopus 로고
    • A c-Myc-SIRT1 feedback loop regulates cell growth and transformation
    • Yuan J, Minter-Dykhouse K, Lou Z. 2009. A c-Myc-SIRT1 feedback loop regulates cell growth and transformation. J. Cell Biol. 185:203-211.
    • (2009) J. Cell Biol. , vol.185 , pp. 203-211
    • Yuan, J.1    Minter-Dykhouse, K.2    Lou, Z.3
  • 18
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, Frye RA, Mayo MW. 2004. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23:2369-2380.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 19
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, Puigserver P. 2005. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434:113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 20
    • 77953257025 scopus 로고    scopus 로고
    • Aging and disease: connections to sirtuins
    • Donmez G, Guarente L. 2010. Aging and disease: connections to sirtuins. Aging Cell 9:285-290.
    • (2010) Aging Cell , vol.9 , pp. 285-290
    • Donmez, G.1    Guarente, L.2
  • 21
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • Haigis MC, Sinclair DA. 2010. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5:253-295.
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 22
    • 79957557182 scopus 로고    scopus 로고
    • Dissecting systemic control of metabolism and aging in the NAD world: the importance of SIRT1 and NAMPT-mediated NAD biosynthesis
    • Imai S. 2011. Dissecting systemic control of metabolism and aging in the NAD world: the importance of SIRT1 and NAMPT-mediated NAD biosynthesis. FEBS Lett. 585:1657-1662.
    • (2011) FEBS Lett. , vol.585 , pp. 1657-1662
    • Imai, S.1
  • 23
    • 77952876986 scopus 로고    scopus 로고
    • Protein deacetylation by SIRT1: an emerging key post-translational modification in metabolic regulation
    • Yu J, Auwerx J. 2010. Protein deacetylation by SIRT1: an emerging key post-translational modification in metabolic regulation. Pharm. Res. 62: 35-41.
    • (2010) Pharm. Res. , vol.62 , pp. 35-41
    • Yu, J.1    Auwerx, J.2
  • 25
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC- 1{alpha}
    • Nemoto S, Fergusson MM, Finkel T. 2005. SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC- 1{alpha}. J. Biol. Chem. 280:16456-16460.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 31
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • Chen WY, Wang DH, Yen RC, Luo J, Gu W, Baylin SB. 2005. Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 123:437-448.
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1    Wang, D.H.2    Yen, R.C.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 33
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • Nemoto S, Fergusson MM, Finkel T. 2004. Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science 306:2105-2108.
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 37
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Yang Y, Fu W, Chen J, Olashaw N, Zhang X, Nicosia SV, Bhalla K, Bai W. 2007. SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat. Cell Biol. 9:1253-1262.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3    Olashaw, N.4    Zhang, X.5    Nicosia, S.V.6    Bhalla, K.7    Bai, W.8
  • 38
    • 79959355078 scopus 로고    scopus 로고
    • Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity
    • Gao Z, Zhang J, Kheterpal I, Kennedy N, Davis RJ, Ye J. 2011. Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity. J. Biol. Chem. 286:22227-22234.
    • (2011) J. Biol. Chem. , vol.286 , pp. 22227-22234
    • Gao, Z.1    Zhang, J.2    Kheterpal, I.3    Kennedy, N.4    Davis, R.J.5    Ye, J.6
  • 41
    • 30144435945 scopus 로고    scopus 로고
    • SIRT1 top 40 hits: use of one-bead, onecompound acetyl-peptide libraries and quantum dots to probe deacetylase specificity
    • Garske AL, Denu JM. 2006. SIRT1 top 40 hits: use of one-bead, onecompound acetyl-peptide libraries and quantum dots to probe deacetylase specificity. Biochemistry 45:94-101.
    • (2006) Biochemistry , vol.45 , pp. 94-101
    • Garske, A.L.1    Denu, J.M.2
  • 44
    • 38749108891 scopus 로고    scopus 로고
    • Dubbing SAGA unveils new epigenetic crosstalk
    • Pijnappel WW, Timmers HT. 2008. Dubbing SAGA unveils new epigenetic crosstalk. Mol. Cell 29:152-154.
    • (2008) Mol. Cell , vol.29 , pp. 152-154
    • Pijnappel, W.W.1    Timmers, H.T.2
  • 45
    • 45849133054 scopus 로고    scopus 로고
    • USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb- catalyzed ubiquitylation of histone H2A
    • Zhang XY, Pfeiffer HK, Thorne AW, McMahon SB. 2008. USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb- catalyzed ubiquitylation of histone H2A. Cell Cycle 7:1522-1524.
    • (2008) Cell Cycle , vol.7 , pp. 1522-1524
    • Zhang, X.Y.1    Pfeiffer, H.K.2    Thorne, A.W.3    McMahon, S.B.4
  • 46
    • 38149078715 scopus 로고    scopus 로고
    • The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression
    • Zhang XY, Varthi M, Sykes SM, Phillips C, Warzecha C, Zhu W, Wyce A, Thorne AW, Berger SL, McMahon SB. 2008. The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol. Cell 29:102-111.
    • (2008) Mol. Cell , vol.29 , pp. 102-111
    • Zhang, X.Y.1    Varthi, M.2    Sykes, S.M.3    Phillips, C.4    Warzecha, C.5    Zhu, W.6    Wyce, A.7    Thorne, A.W.8    Berger, S.L.9    McMahon, S.10
  • 48
    • 33744906046 scopus 로고    scopus 로고
    • Genomic models of metastatic cancer: functional analysis of death-from-cancer signature genes reveals aneuploid, anoikisresistant, metastasis-enabling phenotype with altered cell cycle control and activated polycomb group (PcG) protein chromatin silencing pathway
    • Glinsky GV. 2006. Genomic models of metastatic cancer: functional analysis of death-from-cancer signature genes reveals aneuploid, anoikisresistant, metastasis-enabling phenotype with altered cell cycle control and activated polycomb group (PcG) protein chromatin silencing pathway. Cell Cycle 5:1208-1216.
    • (2006) Cell Cycle , vol.5 , pp. 1208-1216
    • Glinsky, G.V.1
  • 49
    • 20444457518 scopus 로고    scopus 로고
    • Microarray analysis identifies a death-from-cancer signature predicting therapy failure in patients with multiple types of cancer
    • Glinsky GV, Berezovska O, Glinskii AB. 2005. Microarray analysis identifies a death-from-cancer signature predicting therapy failure in patients with multiple types of cancer. J. Clin. Invest. 115:1503-1521.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1503-1521
    • Glinsky, G.V.1    Berezovska, O.2    Glinskii, A.B.3
  • 50
    • 79952030196 scopus 로고    scopus 로고
    • Aberrant expression of USP22 is associated with liver metastasis and poor prognosis of colorectal cancer
    • Liu YL, Yang YM, Xu H, Dong XS. 2011. Aberrant expression of USP22 is associated with liver metastasis and poor prognosis of colorectal cancer. J. Surg. Oncol. 103:283-289.
    • (2011) J. Surg. Oncol. , vol.103 , pp. 283-289
    • Liu, Y.L.1    Yang, Y.M.2    Xu, H.3    Dong, X.S.4
  • 51
    • 79961170767 scopus 로고    scopus 로고
    • Elevated expression of USP22 in correlation with poor prognosis in patients with invasive breast cancer
    • Zhang Y, Yao L, Zhang X, Ji H, Wang L, Sun S, Pang D. 2011. Elevated expression of USP22 in correlation with poor prognosis in patients with invasive breast cancer. J. Cancer Res. Clin. Oncol. 137:1245-1253.
    • (2011) J. Cancer Res. Clin. Oncol. , vol.137 , pp. 1245-1253
    • Zhang, Y.1    Yao, L.2    Zhang, X.3    Ji, H.4    Wang, L.5    Sun, S.6    Pang, D.7
  • 53
    • 80052281618 scopus 로고    scopus 로고
    • USP22 regulates cell proliferation by deubiquitinating the transcriptional regulator FBP1
    • Atanassov BS, Dent SY. 2011. USP22 regulates cell proliferation by deubiquitinating the transcriptional regulator FBP1.EMBORep. 12:924-930.
    • (2011) EMBORep. , vol.12 , pp. 924-930
    • Atanassov, B.S.1    Dent, S.Y.2
  • 54
    • 84856551094 scopus 로고    scopus 로고
    • The ubiquitin hydrolase USP22 contributes to 3″-end processing of JAK-STAT-inducible genes
    • Chipumuro E, Henriksen MA. 2012. The ubiquitin hydrolase USP22 contributes to 3″-end processing of JAK-STAT-inducible genes. FASEB J. 26:842-854.
    • (2012) FASEB J. , vol.26 , pp. 842-854
    • Chipumuro, E.1    Henriksen, M.A.2
  • 55
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW. 2009. Defining the human deubiquitinating enzyme interaction landscape. Cell 138:389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 56
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber J, Mann M, Ishihama Y. 2007. Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2:1896-1906.
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 57
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias JE, Gygi SP. 2007. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4:207-214.
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 58
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW. 2010. Network organization of the human autophagy system. Nature 466:68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 59
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber J, Ishihama Y, Mann M. 2003. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75:663-670.
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 60
    • 34250771721 scopus 로고    scopus 로고
    • High-performance liquid chromatography/electrospray ionization ion-trap mass spectrometry for analysis of oligosaccharides derivatized by reductive amination and N,N-dimethylation
    • Broberg A. 2007. High-performance liquid chromatography/electrospray ionization ion-trap mass spectrometry for analysis of oligosaccharides derivatized by reductive amination and N,N-dimethylation. Carbohydr. Res. 342:1462-1469.
    • (2007) Carbohydr. Res. , vol.342 , pp. 1462-1469
    • Broberg, A.1
  • 63
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR. 1994. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 65
    • 53449090280 scopus 로고    scopus 로고
    • Inhibition of transcriptional activity of c-JUN by SIRT1
    • Gao Z, Ye J. 2008. Inhibition of transcriptional activity of c-JUN by SIRT1. Biochem. Biophys. Res. Commun. 376:793-796.
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 793-796
    • Gao, Z.1    Ye, J.2
  • 67
    • 82955169641 scopus 로고    scopus 로고
    • Proatherogenic abnormalities of lipid metabolism in SirT1 transgenic mice are mediated through Creb deacetylation
    • Qiang L, Lin HV, Kim-Muller JY, Welch CL, Gu W, Accili D. 2011. Proatherogenic abnormalities of lipid metabolism in SirT1 transgenic mice are mediated through Creb deacetylation. Cell Metab. 14:758-767.
    • (2011) Cell Metab. , vol.14 , pp. 758-767
    • Qiang, L.1    Lin, H.V.2    Kim-Muller, J.Y.3    Welch, C.L.4    Gu, W.5    Accili, D.6
  • 68
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ, Kho JH, Kang MR, Um SJ. 2007. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol. Cell 28:277-290.
    • (2007) Mol. Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 69
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • Kim JE, Chen J, Lou Z. 2008. DBC1 is a negative regulator of SIRT1. Nature 451:583-586.
    • (2008) Nature , vol.451 , pp. 583-586
    • Kim, J.E.1    Chen, J.2    Lou, Z.3
  • 70
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • Zhao W, Kruse JP, Tang Y, Jung SY, Qin J, Gu W. 2008. Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451:587-590.
    • (2008) Nature , vol.451 , pp. 587-590
    • Zhao, W.1    Kruse, J.P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 73
    • 84861461517 scopus 로고    scopus 로고
    • USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development
    • Lin Z, Yang H, Kong Q, Li J, Lee SM, Gao B, Dong H, Wei J, Song J, Zhang DD, Fang D. 2012. USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development. Mol. Cell 46:484-494.
    • (2012) Mol. Cell , vol.46 , pp. 484-494
    • Lin, Z.1    Yang, H.2    Kong, Q.3    Li, J.4    Lee, S.M.5    Gao, B.6    Dong, H.7    Wei, J.8    Song, J.9    Zhang, D.D.10    Fang, D.11
  • 74
    • 44649179312 scopus 로고    scopus 로고
    • Yeastataxin-7 links histone deubiquitination with gene gating and mRNA export
    • Kohler A, Schneider M, Cabal GG, Nehrbass U, Hurt E. 2008. Yeastataxin-7 links histone deubiquitination with gene gating and mRNA export. Nat. Cell Biol. 10:707-715.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 707-715
    • Kohler, A.1    Schneider, M.2    Cabal, G.G.3    Nehrbass, U.4    Hurt, E.5
  • 75
    • 77952519938 scopus 로고    scopus 로고
    • Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module
    • Kohler A, Zimmerman E, Schneider M, Hurt E, Zheng N. 2010. Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 141:606-617.
    • (2010) Cell , vol.141 , pp. 606-617
    • Kohler, A.1    Zimmerman, E.2    Schneider, M.3    Hurt, E.4    Zheng, N.5
  • 77
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA. 2002. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 277:45099-45107.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 78
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, Beppu T. 1990. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 265:17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 79
    • 80052597874 scopus 로고    scopus 로고
    • The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements
    • Lang G, Bonnet J, Umlauf D, Karmodiya K, Koffler J, Stierle M, Devys D, Tora L. 2011. The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements. Mol. Cell. Biol. 31:3734-3744.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3734-3744
    • Lang, G.1    Bonnet, J.2    Umlauf, D.3    Karmodiya, K.4    Koffler, J.5    Stierle, M.6    Devys, D.7    Tora, L.8
  • 80
    • 79955960768 scopus 로고    scopus 로고
    • Acetyl-CoA induces cell growth and proliferation by promoting the acetylation of histones at growth genes
    • Cai L, Sutter BM, Li B, Tu BP. 2011. Acetyl-CoA induces cell growth and proliferation by promoting the acetylation of histones at growth genes. Mol. Cell 42:426-437.
    • (2011) Mol. Cell , vol.42 , pp. 426-437
    • Cai, L.1    Sutter, B.M.2    Li, B.3    Tu, B.P.4
  • 82
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. 2000. The language of covalent histone modifications. Nature 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 83
    • 33749669082 scopus 로고    scopus 로고
    • Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10
    • Ahn SH, Diaz RL, Grunstein M, Allis CD. 2006. Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10. Mol. Cell 24:211-220.
    • (2006) Mol. Cell , vol.24 , pp. 211-220
    • Ahn, S.H.1    Diaz, R.L.2    Grunstein, M.3    Allis, C.D.4
  • 84
    • 67651161889 scopus 로고    scopus 로고
    • BubR1 acetylation at prometaphase is required for modulating APC/C activity and timing of mitosis
    • Choi E, Choe H, Min J, Choi JY, Kim J, Lee H. 2009. BubR1 acetylation at prometaphase is required for modulating APC/C activity and timing of mitosis. EMBO J. 28:2077-2089.
    • (2009) EMBO J. , vol.28 , pp. 2077-2089
    • Choi, E.1    Choe, H.2    Min, J.3    Choi, J.Y.4    Kim, J.5    Lee, H.6
  • 85
    • 84861452914 scopus 로고    scopus 로고
    • A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress
    • de la Vega L, Grishina I, Moreno R, Kruger M, Braun T, Schmitz ML. 2012. A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress. Mol. Cell 46:472-483.
    • (2012) Mol. Cell , vol.46 , pp. 472-483
    • de la Vega, L.1    Grishina, I.2    Moreno, R.3    Kruger, M.4    Braun, T.5    Schmitz, M.L.6
  • 87
    • 34147208064 scopus 로고    scopus 로고
    • An acetylation/deacetylationSUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity
    • Stankovic-Valentin N, Deltour S, Seeler J, Pinte S, Vergoten G, Guerardel C, Dejean A, Leprince D. 2007. An acetylation/deacetylation- SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity. Mol. Cell. Biol. 27:2661-2675.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2661-2675
    • Stankovic-Valentin, N.1    Deltour, S.2    Seeler, J.3    Pinte, S.4    Vergoten, G.5    Guerardel, C.6    Dejean, A.7    Leprince, D.8
  • 88
    • 84863003858 scopus 로고    scopus 로고
    • An acetylation switch regulates SUMO-dependent protein interaction networks
    • Ullmann R, Chien CD, Avantaggiati ML, Muller S. 2012. An acetylation switch regulates SUMO-dependent protein interaction networks. Mol. Cell 46:759-770.
    • (2012) Mol. Cell , vol.46 , pp. 759-770
    • Ullmann, R.1    Chien, C.D.2    Avantaggiati, M.L.3    Muller, S.4
  • 89
    • 80555156095 scopus 로고    scopus 로고
    • SAGA and ATAC histone acetyl transferase complexes regulate distinct sets of genes and ATAC defines a class of p300-independent enhancer
    • Krebs AR, Karmodiya K, Lindahl-Allen M, Struhl K, Tora L. 2011. SAGA and ATAC histone acetyl transferase complexes regulate distinct sets of genes and ATAC defines a class of p300-independent enhancers. Mol. Cell 44:410-423.
    • (2011) Mol. Cell , vol.44 , pp. 410-423
    • Krebs, A.R.1    Karmodiya, K.2    Lindahl-Allen, M.3    Struhl, K.4    Tora, L.5
  • 92
    • 43149122898 scopus 로고    scopus 로고
    • Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells
    • Minsky N, Shema E, Field Y, Schuster M, Segal E, Oren M. 2008. Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells. Nat. Cell Biol. 10:483-488.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 483-488
    • Minsky, N.1    Shema, E.2    Field, Y.3    Schuster, M.4    Segal, E.5    Oren, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.