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Volumn 12, Issue 2, 2013, Pages 449-463

Quantitative proteomics reveals factors regulating RNA biology as dynamic targets of stress-induced SUMOylation in arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; HISTONE; PROTEIN; RNA BINDING PROTEIN; SUMO PROTEIN; TRANSCRIPTOME;

EID: 84874050141     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.025056     Document Type: Article
Times cited : (115)

References (76)
  • 1
    • 33745944196 scopus 로고    scopus 로고
    • Transcriptional regula- tory networks in cellular responses and tolerance to dehydration and cold stresses
    • Yamaguchi-Shinozaki, K., and Shinozaki, K. (2006) Transcriptional regula- tory networks in cellular responses and tolerance to dehydration and cold stresses. Ann. Rev. Plant Biol. 57, 781-803
    • (2006) Ann. Rev. Plant Biol. , vol.57 , pp. 781-803
    • Yamaguchi-Shinozaki, K.1    Shinozaki, K.2
  • 2
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D. G., and Dangl, J. L. (2006) The plant immune system. Nature 444, 323-329
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 3
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter, K., Haslbeck, M., and Buchner, J. (2010) The heat shock response: life on the verge of death. Mol. Cell 40, 253-266
    • (2010) Mol. Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 4
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson, K. A., and Henley, J. M. (2010) Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 428, 133-145
    • (2010) Biochem. J. , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2
  • 6
    • 34848870906 scopus 로고    scopus 로고
    • SUMOylation, a post- translational regulatory process in plants
    • Miura, K., Jin, J. B., and Hasegawa, P. M. (2007) SUMOylation, a post- translational regulatory process in plants. Curr. Opin. Plant Biol. 10, 495-502
    • (2007) Curr. Opin. Plant Biol. , vol.10 , pp. 495-502
    • Miura, K.1    Jin, J.B.2    Hasegawa, P.M.3
  • 7
    • 0037470238 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) protein modification system in arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress
    • Kurepa, J., Walker, J. M., Smalle, J., Gosink, M. M., Davis, S. J., Durham, T. L., Sung, D. Y., and Vierstra, R. D. (2003) The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J. Biol. Chem. 278, 6862-6872
    • (2003) J. Biol. Chem. , vol.278 , pp. 6862-6872
    • Kurepa, J.1    Walker, J.M.2    Smalle, J.3    Gosink, M.M.4    Davis, S.J.5    Durham, T.L.6    Sung, D.Y.7    Vierstra, R.D.8
  • 8
    • 34548691835 scopus 로고    scopus 로고
    • Genetic analysis of SUMOylation in arabidopsis: Conjugation of SUMO1 and SUMO2 to nuclear proteins is essential
    • Saracco, S. A., Miller, M. J., Kurepa, J., and Vierstra, R. D. (2007) Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential. Plant Physiol. 145, 119-134
    • (2007) Plant Physiol. , vol.145 , pp. 119-134
    • Saracco, S.A.1    Miller, M.J.2    Kurepa, J.3    Vierstra, R.D.4
  • 11
    • 70949090880 scopus 로고    scopus 로고
    • The arabidopsis SUMO E3 ligase AtMMS21, a homologue of NSE2/MMS21, regulates cell proliferation in the root
    • Huang, L., Yang, S., Zhang, S., Liu, M., Lai, J., Qi, Y., Shi, S., Wang, J., Wang, Y., Xie, Q., and Yang, C. (2009) The Arabidopsis SUMO E3 ligase AtMMS21, a homologue of NSE2/MMS21, regulates cell proliferation in the root. Plant J. 60, 666-678
    • (2009) Plant J. , vol.60 , pp. 666-678
    • Huang, L.1    Yang, S.2    Zhang, S.3    Liu, M.4    Lai, J.5    Qi, Y.6    Shi, S.7    Wang, J.8    Wang, Y.9    Xie, Q.10    Yang, C.11
  • 12
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjuga- tion in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M. S., Dargemont, C., and Hay, R. T. (2001) SUMO-1 conjuga- tion in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276, 12654-12659
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 13
    • 77955999636 scopus 로고    scopus 로고
    • Sitespecific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic, I., Schimmel, J., Hendriks, I. A., van Santen, M. A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M., and Vertegaal, A. C. O. (2010) Sitespecific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell 39, 641-652
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    Van Santen, M.A.4    Van De Rijke, F.5    Van Dam, H.6    Gnad, F.7    Mann, M.8    Vertegaal, A.C.O.9
  • 15
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • Matic, I., van Hagen, M., Schimmel, J., Macek, B., Ogg, S. C., Tatham, M. H., Hay, R. T., Lamond, A. I., Mann, M., and Vertegaal, A. C. (2008) In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol. Cell. Proteomics 7, 132-144
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 132-144
    • Matic, I.1    Van Hagen, M.2    Schimmel, J.3    Macek, B.4    Ogg, S.C.5    Tatham, M.H.6    Hay, R.T.7    Lamond, A.I.8    Mann, M.9    Vertegaal, A.C.10
  • 16
    • 0142028822 scopus 로고    scopus 로고
    • A nuclear protease required for flowering-time regulation in arabidopsis reduces the abundance of small ubiquitin-related modifier conjugates
    • Murtas, G., Reeves, P. H., Fu, Y. F., Bancroft, I., Dean, C., and Coupland, G. (2003) A nuclear protease required for flowering-time regulation in Arabidopsis reduces the abundance of small ubiquitin-related modifier conjugates. Plant Cell 15, 2308-2319
    • (2003) Plant Cell , vol.15 , pp. 2308-2319
    • Murtas, G.1    Reeves, P.H.2    Fu, Y.F.3    Bancroft, I.4    Dean, C.5    Coupland, G.6
  • 17
    • 57749100154 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in arabidopsis
    • Conti, L., Price, G., O'Donnell, E., Schwessinger, B., Dominy, P., and Sadanandom, A. (2008) Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in Arabidopsis. Plant Cell 20, 2894-2908
    • (2008) Plant Cell , vol.20 , pp. 2894-2908
    • Conti, L.1    Price, G.2    O'Donnell, E.3    Schwessinger, B.4    Dominy, P.5    Sadanandom, A.6
  • 19
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiq- uitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh, H., and Hinchey, J. (2000) Functional heterogeneity of small ubiq- uitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275, 6252-6258
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 21
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka, K., Nishide, J., Okazaki, K., Kato, H., Niwa, O., Nakagawa, T., Matsuda, H., Kawamukai, M., and Murakami, Y. (1999) Characterization of a fission yeast SUMO-1 homologue, Pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19, 8660-8672
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1    Nishide, J.2    Okazaki, K.3    Kato, H.4    Niwa, O.5    Nakagawa, T.6    Matsuda, H.7    Kawamukai, M.8    Murakami, Y.9
  • 22
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein smt3p is activated for conjugation to other proteins by an aos1p/Uba2p heterodimer
    • Johnson, E. S., Schwienhorst, I., Dohmen, R. J., and Blobel, G. (1997) The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J. 16, 5509-5519
    • (1997) EMBO J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 23
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conju- gating enzyme in degradation of S- and M-phase cyclins
    • Seufert, W., Futcher, B., and Jentsch, S. (1995) Role of a ubiquitin-conju- gating enzyme in degradation of S- and M-phase cyclins. Nature 373, 78-81
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 24
    • 35748968208 scopus 로고    scopus 로고
    • The arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses
    • Catala, R., Ouyang, J., Abreu, I. A., Hu, Y., Seo, H., Zhang, X., and Chua, N. H. (2007) The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses. Plant Cell 19, 2952-2966
    • (2007) Plant Cell , vol.19 , pp. 2952-2966
    • Catala, R.1    Ouyang, J.2    Abreu, I.A.3    Hu, Y.4    Seo, H.5    Zhang, X.6    Chua, N.H.7
  • 26
    • 79960596484 scopus 로고    scopus 로고
    • Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1
    • Park, B. S., Song, J. T., and Seo, H. S. (2011) Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1. Nat. Commun. 2, 400
    • (2011) Nat. Commun. , vol.2 , pp. 400
    • Park, B.S.1    Song, J.T.2    Seo, H.S.3
  • 27
    • 77955717340 scopus 로고    scopus 로고
    • SUMOylation of arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance
    • Cohen-Peer, R., Schuster, S., Meiri, D., Breiman, A., and Avni, A. (2010) SUMOylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its activity during acquired thermotholerance. Plant Mol. Biol. 74, 33-45
    • (2010) Plant Mol. Biol. , vol.74 , pp. 33-45
    • Cohen-Peer, R.1    Schuster, S.2    Meiri, D.3    Breiman, A.4    Avni, A.5
  • 28
    • 33845630288 scopus 로고    scopus 로고
    • SIZ1, small ubiquitin-like modifier E3 ligase facilitates basal thermotolerance in arabidopsis independent of salicylic acid
    • Yoo, C. Y., Miura, K., Jin, J. B., Lee, J., Park, H. C., Salt, D. E., Yun, D. J., Bressan, R. A., and Hasegawa, P. M. (2006) SIZ1, small ubiquitin-like modifier E3 ligase facilitates basal thermotolerance in Arabidopsis independent of salicylic acid. Plant Physiol. 142, 1548-1558
    • (2006) Plant Physiol. , vol.142 , pp. 1548-1558
    • Yoo, C.Y.1    Miura, K.2    Jin, J.B.3    Lee, J.4    Park, H.C.5    Salt, D.E.6    Yun, D.J.7    Bressan, R.A.8    Hasegawa, P.M.9
  • 29
    • 77955898187 scopus 로고    scopus 로고
    • Arabidopsis small ubiquitin-like modifier paralogs have distinct functions in development and defense
    • van den Burg, H. A., Kini, R. K., Schuurink, R. C., and Takken, F. L. W. (2010) Arabidopsis small ubiquitin-like modifier paralogs have distinct functions in development and defense. Plant Cell 22, 1998-2016
    • (2010) Plant Cell , vol.22 , pp. 1998-2016
    • Van Den Burg, H.A.1    Kini, R.K.2    Schuurink, R.C.3    Takken, F.L.W.4
  • 31
    • 65249184459 scopus 로고    scopus 로고
    • SUMOylation of ABI5 by the arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling
    • Miura, K., Lee, J., Jin, J. B., Yoo, C. Y., Miura, T., and Hasegawa, P. M. (2009) SUMOylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling. Proc. Natl. Acad. Sci. U.S.A. 106, 5418-5423
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5418-5423
    • Miura, K.1    Lee, J.2    Jin, J.B.3    Yoo, C.Y.4    Miura, T.5    Hasegawa, P.M.6
  • 32
    • 74549151076 scopus 로고    scopus 로고
    • SIZ1 controls cell growth and plant development in arabidopsis through salicylic acid
    • Miura, K., Lee, J., Miura, T., and Hasegawa, P. M. (2010) SIZ1 controls cell growth and plant development in Arabidopsis through salicylic acid. Plant Cell Physiol. 51, 103-113
    • (2010) Plant Cell Physiol. , vol.51 , pp. 103-113
    • Miura, K.1    Lee, J.2    Miura, T.3    Hasegawa, P.M.4
  • 33
    • 0037781038 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier modulates abscisic acid signaling in arabidopsis
    • Lois, L. M., Lima, C. D., and Chua, N. H. (2003) Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis. Plant Cell 15, 1347-1359
    • (2003) Plant Cell , vol.15 , pp. 1347-1359
    • Lois, L.M.1    Lima, C.D.2    Chua, N.H.3
  • 35
    • 80053903500 scopus 로고    scopus 로고
    • Elevated global SUMOylation in ubc9 transgenic mice protects their brains against focal cerebral ischemic damage
    • Lee, Y. J., Mou, Y., Maric, D., Klimanis, D., Auh, S., and Hallenbeck, J. M. (2011) Elevated global SUMOylation in Ubc9 transgenic mice protects their brains against focal cerebral ischemic damage. PLoS One 6, e25852
    • (2011) PLoS One , vol.6
    • Lee, Y.J.1    Mou, Y.2    Maric, D.3    Klimanis, D.4    Auh, S.5    Hallenbeck, J.M.6
  • 37
    • 84856862707 scopus 로고    scopus 로고
    • Human pathogens and the host cell SUMOylation system
    • Wimmer, P., Schreiner, S., and Dobner, T. (2012) Human pathogens and the host cell SUMOylation system. J. Virol. 86, 642-654
    • (2012) J. Virol. , vol.86 , pp. 642-654
    • Wimmer, P.1    Schreiner, S.2    Dobner, T.3
  • 41
    • 78049235116 scopus 로고    scopus 로고
    • Pro-teomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in arabidopsis
    • Miller, M. J., Barrett-Wilt, G. A., Hua, Z., and Vierstra, R. D. (2010) Pro- teomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis. Proc. Natl. Acad. Sci. U.S.A. 107, 16512-16517
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16512-16517
    • Miller, M.J.1    Barrett-Wilt, G.A.2    Hua, Z.3    Vierstra, R.D.4
  • 42
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham, M. H., Matic, I., Mann, M., and Hay, R. T. (2011) Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci. Signal 4, rs4
    • (2011) Sci. Signal , vol.4
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 43
    • 2942525287 scopus 로고    scopus 로고
    • SUMOylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis
    • Li, T., Evdokimov, E., Shen, R. F., Chao, C. C., Tekle, E., Wang, T., Stadtman, E. R., Yang, D. C., and Chock, P. B. (2004) SUMOylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis. Proc. Natl. Acad. Sci. U.S.A. 101, 8551-8556
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8551-8556
    • Li, T.1    Evdokimov, E.2    Shen, R.F.3    Chao, C.C.4    Tekle, E.5    Wang, T.6    Stadtman, E.R.7    Yang, D.C.8    Chock, P.B.9
  • 44
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of SUMOylated proteins in saccharomyces cerevisiae. Induction of protein SUMOylation by cellular stresses
    • Zhou, W., Ryan, J. J., and Zhou, H. (2004) Global analyses of SUMOylated proteins in Saccharomyces cerevisiae. Induction of protein SUMOylation by cellular stresses. J. Biol. Chem. 279, 32262-32268
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 45
    • 78049234670 scopus 로고    scopus 로고
    • Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify arabidopsis proteins implicated in diverse biological processes
    • Elrouby, N., and Coupland, G. (2010) Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes. Proc. Natl. Acad. Sci. U.S.A. 107, 17415-17420
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17415-17420
    • Elrouby, N.1    Coupland, G.2
  • 46
    • 79959849574 scopus 로고    scopus 로고
    • Extending SILAC to proteomics of plant cell lines
    • Schutz, W., Hausmann, N., Krug, K., Hampp, R., and Macek, B. (2011) Extending SILAC to proteomics of plant cell lines. Plant Cell 23, 1701-1705
    • (2011) Plant Cell , vol.23 , pp. 1701-1705
    • Schutz, W.1    Hausmann, N.2    Krug, K.3    Hampp, R.4    Macek, B.5
  • 47
    • 77952538049 scopus 로고    scopus 로고
    • Quantitation in mass-spectrometry- based proteomics
    • Schulze, W. X., and Usadel, B. (2010) Quantitation in mass-spectrometry- based proteomics. Annu. Rev. Plant Biol. 61, 491-516
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 491-516
    • Schulze, W.X.1    Usadel, B.2
  • 49
    • 70349974261 scopus 로고    scopus 로고
    • High precision quantitative proteomics using iTRAQ on an LTQ orbitrap: A new mass spectrometric method combining the benefits of all
    • Kocher, T., Pichler, P., Schutzbier, M., Stingl, C., Kaul, A., Teucher, N., Hasenfuss, G., Penninger, J. M., and Mechtler, K. (2009) High precision quantitative proteomics using iTRAQ on an LTQ Orbitrap: a new mass spectrometric method combining the benefits of all. J. Proteome Res. 8, 4743-4752
    • (2009) J. Proteome Res. , vol.8 , pp. 4743-4752
    • Kocher, T.1    Pichler, P.2    Schutzbier, M.3    Stingl, C.4    Kaul, A.5    Teucher, N.6    Hasenfuss, G.7    Penninger, J.M.8    Mechtler, K.9
  • 50
    • 67649696034 scopus 로고    scopus 로고
    • Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in arabidopsis
    • Saracco, S. A., Hansson, M., Scalf, M., Walker, J. M., Smith, L. M., and Vierstra, R. D. (2009) Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant J. 59, 344-358
    • (2009) Plant J. , vol.59 , pp. 344-358
    • Saracco, S.A.1    Hansson, M.2    Scalf, M.3    Walker, J.M.4    Smith, L.M.5    Vierstra, R.D.6
  • 51
    • 34249342349 scopus 로고    scopus 로고
    • Verification of single-peptide protein identifications by the application of complementary database search algorithms
    • Rohrbough, J. G., Breci, L., Merchant, N., Miller, S., and Haynes, P. A. (2006) Verification of single-peptide protein identifications by the application of complementary database search algorithms. J. Biomol. Tech. 17, 327-332
    • (2006) J. Biomol. Tech. , vol.17 , pp. 327-332
    • Rohrbough, J.G.1    Breci, L.2    Merchant, N.3    Miller, S.4    Haynes, P.A.5
  • 52
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly,"
    • Ow, S. Y., Salim, M., Noirel, J., Evans, C., Rehman, I., and Wright, P. C. (2009) iTRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly." J. Proteome Res. 8, 5347-5355
    • (2009) J. Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 53
    • 67650720512 scopus 로고    scopus 로고
    • Systematic study of protein SUMOylation: Development of a site-specific predictor of SUMOsp 2.0
    • Ren, J., Gao, X., Jin, C., Zhu, M., Wang, X., Shaw, A., Wen, L., Yao, X., and Xue, Y. (2009) Systematic study of protein SUMOylation: development of a site-specific predictor of SUMOsp 2.0. Proteomics 9, 3409-3412
    • (2009) Proteomics , vol.9 , pp. 3409-3412
    • Ren, J.1    Gao, X.2    Jin, C.3    Zhu, M.4    Wang, X.5    Shaw, A.6    Wen, L.7    Yao, X.8    Xue, Y.9
  • 55
    • 33846345430 scopus 로고    scopus 로고
    • A heat-inducible transcription factor, HsfA2, is required for extension of acquired thermotolerance in arabidopsis
    • Charng, Y. Y., Liu, H. C., Liu, N. Y., Chi, W. T., Wang, C. N., Chang, S. H., and Wang, T. T. (2007) A heat-inducible transcription factor, HsfA2, is required for extension of acquired thermotolerance in Arabidopsis. Plant Physiol. 143, 251-262
    • (2007) Plant Physiol. , vol.143 , pp. 251-262
    • Charng, Y.Y.1    Liu, H.C.2    Liu, N.Y.3    Chi, W.T.4    Wang, C.N.5    Chang, S.H.6    Wang, T.T.7
  • 58
    • 4744360999 scopus 로고    scopus 로고
    • A proteome-wide approach identifies SUMOylated substrate proteins in yeast
    • Panse, V. G., Hardeland, U., Werner, T., Kuster, B., and Hurt, E. (2004) A proteome-wide approach identifies SUMOylated substrate proteins in yeast. J. Biol. Chem. 279, 41346-41351
    • (2004) J. Biol. Chem. , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.5
  • 59
    • 84863011119 scopus 로고    scopus 로고
    • Analysis of oxygen/glucosedeprivation-induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics
    • Yang, W., Thompson, J. W., Wang, Z., Wang, L., Sheng, H., Foster, M. W., Moseley, M. A., and Paschen, W. (2012) Analysis of oxygen/glucosedeprivation- induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics. J. Proteome Res. 11, 1108-1117
    • (2012) J. Proteome Res. , vol.11 , pp. 1108-1117
    • Yang, W.1    Thompson, J.W.2    Wang, Z.3    Wang, L.4    Sheng, H.5    Foster, M.W.6    Moseley, M.A.7    Paschen, W.8
  • 60
    • 0000423824 scopus 로고
    • Ubiquitin pool modula- tion and protein degradation in wheat roots during high temperature stress
    • Ferguson, D., Guikema, J., and Paulsen, G. (1989) Ubiquitin pool modula- tion and protein degradation in wheat roots during high temperature stress. Plant Physiol. 92, 740-746
    • (1989) Plant Physiol. , vol.92 , pp. 740-746
    • Ferguson, D.1    Guikema, J.2    Paulsen, G.3
  • 61
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes
    • Bossis, G., and Melchior, F. (2006) Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol. Cell 21, 349-357
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 65
    • 84860469639 scopus 로고    scopus 로고
    • MRNA export and SUMOylation - Lessons from plants
    • Meier, I. (2012) mRNA export and SUMOylation - lessons from plants. Biochim. Biophys. Acta 1819, 531-537
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 531-537
    • Meier, I.1
  • 66
    • 37749021009 scopus 로고    scopus 로고
    • A role for SUMO modification in transcriptional repression and activation
    • Lyst, M. J., and Stancheva, I. (2007) A role for SUMO modification in transcriptional repression and activation. Biochem. Soc. Trans. 35, 1389-1392
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1389-1392
    • Lyst, M.J.1    Stancheva, I.2
  • 67
    • 77953929082 scopus 로고    scopus 로고
    • SUMO functions in constitutive transcription and during activation of inducible genes in yeast
    • Rosonina, E., Duncan, S. M., and Manley, J. L. (2010) SUMO functions in constitutive transcription and during activation of inducible genes in yeast. Genes Dev. 24, 1242-1252
    • (2010) Genes Dev. , vol.24 , pp. 1242-1252
    • Rosonina, E.1    Duncan, S.M.2    Manley, J.L.3
  • 68
    • 71449098588 scopus 로고    scopus 로고
    • IDN1 and IDN2 are required for de novo DNA methylation in arabidopsis thaliana
    • Ausin, I., Mockler, T. C., Chory, J., and Jacobsen, S. E. (2009) IDN1 and IDN2 are required for de novo DNA methylation in Arabidopsis thaliana. Nat. Struct. Mol. Biol. 16, 1325-1327
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1325-1327
    • Ausin, I.1    Mockler, T.C.2    Chory, J.3    Jacobsen, S.E.4
  • 69
    • 78650732869 scopus 로고    scopus 로고
    • Genetic and environmental changes in SUMO homeostasis lead to nuclear mRNA retention in plants
    • Muthuswamy, S., and Meier, I. (2011) Genetic and environmental changes in SUMO homeostasis lead to nuclear mRNA retention in plants. Planta 233, 201-208
    • (2011) Planta , vol.233 , pp. 201-208
    • Muthuswamy, S.1    Meier, I.2
  • 70
    • 34347406950 scopus 로고    scopus 로고
    • NUCLEAR PORE ANCHOR, the arabidopsis homolog of tpr/Mlp1/Mlp2/megator, is involved in mRNA export and SUMO homeostasis and affects diverse aspects of plant development
    • Xu, X. M., Rose, A., Muthuswamy, S., Jeong, S. Y., Venkatakrishnan, S., Zhao, Q., and Meier, I. (2007) NUCLEAR PORE ANCHOR, the Arabidopsis homolog of Tpr/Mlp1/Mlp2/megator, is involved in mRNA export and SUMO homeostasis and affects diverse aspects of plant development. Plant Cell 19, 1537-1548
    • (2007) Plant Cell , vol.19 , pp. 1537-1548
    • Xu, X.M.1    Rose, A.2    Muthuswamy, S.3    Jeong, S.Y.4    Venkatakrishnan, S.5    Zhao, Q.6    Meier, I.7
  • 71
    • 0035947677 scopus 로고    scopus 로고
    • SUMO-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic Leukemia nuclear body associated transcription factor
    • Goodson, M. L., Hong, Y., Rogers, R., Matunis, M. J., Park-Sarge, O. K., and Sarge, K. D. (2001) SUMO-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor. J. Biol. Chem. 276, 18513-18518
    • (2001) J. Biol. Chem. , vol.276 , pp. 18513-18518
    • Goodson, M.L.1    Hong, Y.2    Rogers, R.3    Matunis, M.J.4    Park-Sarge, O.K.5    Sarge, K.D.6
  • 74
    • 36348964395 scopus 로고    scopus 로고
    • The yeast hex3/Slx8 heterodimer is a ubiquitin ligase stimulated by substrate SUMOylation
    • Xie, Y., Kerscher, O., Kroetz, M. B., McConchie, H. F., Sung, P., and Hochstrasser, M. (2007) The yeast Hex3/Slx8 heterodimer is a ubiquitin ligase stimulated by substrate SUMOylation. J. Biol. Chem. 282, 34176-34184
    • (2007) J. Biol. Chem. , vol.282 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 75
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in Eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • Sun, H., Leverson, J. D., and Hunter, T. (2007) Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 26, 4102-4112
    • (2007) EMBO J. , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 76
    • 79955642715 scopus 로고    scopus 로고
    • The cullin-RING ubiquitin-protein ligases
    • Hua, Z., and Vierstra, R. D. (2011) The cullin-RING ubiquitin-protein ligases. Ann. Rev. Plant Biol. 62, 299-334
    • (2011) Ann. Rev. Plant Biol. , vol.62 , pp. 299-334
    • Hua, Z.1    Vierstra, R.D.2


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