메뉴 건너뛰기




Volumn 10, Issue 6, 2009, Pages 385-397

The ubiquitin-26S proteasome system at the nexus of plant biology

Author keywords

[No Author keywords available]

Indexed keywords

DNA 26S; ETHYLENE; F BOX PROTEIN; GIBBERELLIN DERIVATIVE; JASMONIC ACID; PHYTOHORMONE; PROTEASOME; UBIQUITIN;

EID: 67349254570     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2688     Document Type: Review
Times cited : (1036)

References (139)
  • 1
    • 67349139572 scopus 로고    scopus 로고
    • [No authors listed.] Webster's Collegiate Dictionary (N. E. Merriam-Webster Publishers, springfield, Massachusetts, 1987).
    • [No authors listed.] Webster's Collegiate Dictionary (N. E. Merriam-Webster Publishers, springfield, Massachusetts, 1987).
  • 2
    • 0019174693 scopus 로고
    • ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes
    • Wilkinson, K. D., urban, M. K. & Haas, A. L. ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. J. Biol. Chem. 255, 7529-7532 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 7529-7532
    • Wilkinson, K.D.1    urban, M.K.2    Haas, A.L.3
  • 3
    • 18044364830 scopus 로고    scopus 로고
    • Post-translational regulation in plants employing a diverse set of polypeptide tags
    • Downes, B. & Vierstra, R. D. Post-translational regulation in plants employing a diverse set of polypeptide tags. Biochem. Soc. Trans. 33, 393-399 (2005).
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 393-399
    • Downes, B.1    Vierstra, R.D.2
  • 4
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher, O., Felberbaum, R. & Hochstrasser, M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell. Dev. Biol. 22, 1 59-180 (2006).
    • (2006) Annu. Rev. Cell. Dev. Biol , vol.22 , Issue.1 , pp. 59-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 5
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26s proteasome proteolytic pathway
    • smalle, J. & Vierstra, R. D. The ubiquitin 26s proteasome proteolytic pathway. Annu. Rev. Plant Biol. 55, 555-590 (2004).
    • (2004) Annu. Rev. Plant Biol , vol.55 , pp. 555-590
    • smalle, J.1    Vierstra, R.D.2
  • 6
    • 33646064427 scopus 로고    scopus 로고
    • Harper, J. W. & schulman, B. A. structural complexity in ubiquitin recognition. Cell 124, 1133-1136 (2006).
    • Harper, J. W. & schulman, B. A. structural complexity in ubiquitin recognition. Cell 124, 1133-1136 (2006).
  • 7
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay, D. & Riezman, H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315, 201-205(2007).
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 8
    • 34250897234 scopus 로고    scopus 로고
    • ubiquitin, hormones and biotic stress in plants
    • Dreher, K. & Callis, J. ubiquitin, hormones and biotic stress in plants. Ann. Bot. 99, 787-822 (2007).
    • (2007) Ann. Bot , vol.99 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 9
    • 36249022073 scopus 로고    scopus 로고
    • ubiquitin receptors and ERAD: A network of pathways to the proteasome
    • Raasi, s. & Wolf, D. H. ubiquitin receptors and ERAD: a network of pathways to the proteasome. Semin. Cell. Dev. Biol. 18, 780-791 (2007).
    • (2007) Semin. Cell. Dev. Biol , vol.18 , pp. 780-791
    • Raasi, S.1    Wolf, D.H.2
  • 10
    • 35148872652 scopus 로고    scopus 로고
    • The E3 ligase AtCHIP ubiquitylates FtsH 1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts
    • Shen, G., Adam, Z. & Zhang, H. The E3 ligase AtCHIP ubiquitylates FtsH 1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts. Plant J. 52, 309-321 (2007).
    • (2007) Plant J , vol.52 , pp. 309-321
    • Shen, G.1    Adam, Z.2    Zhang, H.3
  • 11
    • 0034512691 scopus 로고    scopus 로고
    • Yan, N., Doelling,J. H., Falbel, T. G., Durski, A. M. & Vierstra, R. D. The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine. Plant Physiol. 124, 1828-1843(2000).
    • Yan, N., Doelling,J. H., Falbel, T. G., Durski, A. M. & Vierstra, R. D. The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine. Plant Physiol. 124, 1828-1843(2000).
  • 13
    • 21444450086 scopus 로고    scopus 로고
    • Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis
    • Gingerich, D. J. et al. Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis. J. Biol. Chem. 280, 18810-18821 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 18810-18821
    • Gingerich, D.J.1
  • 14
    • 0141567486 scopus 로고    scopus 로고
    • The HECT ubiquitin-protein ligase (uPL) family in Arabidopsis: UPL3 has a specific role in trichome development
    • Downes, B. P.,stupar, R. M., Gingerich, D. J. & Vierstra, R. D. The HECT ubiquitin-protein ligase (uPL) family in Arabidopsis: uPL3 has a specific role in trichome development. Plant J. 35, 729-742 (2003).
    • (2003) Plant J , vol.35 , pp. 729-742
    • Downes, B.P.1    stupar, R.M.2    Gingerich, D.J.3    Vierstra, R.D.4
  • 15
    • 0037700017 scopus 로고    scopus 로고
    • First glance at the plant APC/C, a highly conserved ubiquitin-protein ligase
    • Capron, A., Okresz, L. & Genschik, P. First glance at the plant APC/C, a highly conserved ubiquitin-protein ligase. Trends Plant Sci. 8, 83-89 (2003).
    • (2003) Trends Plant Sci , vol.8 , pp. 83-89
    • Capron, A.1    Okresz, L.2    Genschik, P.3
  • 16
    • 33644993733 scopus 로고    scopus 로고
    • Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis
    • Kraft, E. et al. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol. 139, 1597-1611 (2005).
    • (2005) Plant Physiol , vol.139 , pp. 1597-1611
    • Kraft, E.1
  • 17
    • 18044394093 scopus 로고    scopus 로고
    • stone, s. L. et al. Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis. Plant Physiol. 137, 13-30(2005).
    • stone, s. L. et al. Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis. Plant Physiol. 137, 13-30(2005).
  • 18
    • 43549110569 scopus 로고    scopus 로고
    • Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CuL4-RING E3 ubiquitin ligases
    • Lee, J. H. et al.Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CuL4-RING E3 ubiquitin ligases. Plant Cell 20, 152-167(2008).
    • (2008) Plant Cell , vol.20 , pp. 152-167
    • Lee, J.H.1
  • 19
    • 0037143725 scopus 로고    scopus 로고
    • Gagne, J. M., Downes, B. P.,shiu, s.-H., Durski, A. M. & Vierstra, R. D. The F-box subunit of the sCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis. Proc. Natl Acad. Sci. USA 99, 11519-11524(2002).
    • Gagne, J. M., Downes, B. P.,shiu, s.-H., Durski, A. M. & Vierstra, R. D. The F-box subunit of the sCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis. Proc. Natl Acad. Sci. USA 99, 11519-11524(2002).
  • 20
    • 0842264053 scopus 로고    scopus 로고
    • Mudgil, Y, Shiu, s. H., stone, s. L., salt, J. N. & Goring, D. R. A large complement of the predicted Arabidopsis ARM repeat proteins are members of the u-box E3 ubiquitin ligase family. Plant Physiol. 134, 59-66 (2004).
    • Mudgil, Y, Shiu, s. H., stone, s. L., salt, J. N. & Goring, D. R. A large complement of the predicted Arabidopsis ARM repeat proteins are members of the u-box E3 ubiquitin ligase family. Plant Physiol. 134, 59-66 (2004).
  • 21
    • 48249156236 scopus 로고    scopus 로고
    • Biochemical function of typical and variant Arabidopsis thaliana U-box E3 ubiquitin-protein ligases
    • Wiborg, J., O'shea, C. & skriver, K. Biochemical function of typical and variant Arabidopsis thaliana U-box E3 ubiquitin-protein ligases. Biochem. J. 413, 447-457 (2008).
    • (2008) Biochem. J , vol.413 , pp. 447-457
    • Wiborg, J.1    O'shea, C.2    skriver, K.3
  • 22
    • 35348861423 scopus 로고    scopus 로고
    • Gingerich, D. J., Hanada, K., shiu, s. H. & Vierstra, R. D. Large-scale, lineage-specific expansion of a bric-a-brac/tramtrack/broad complex ubiquitin-ligase gene family in rice. Plant Cell 19, 2329-2348 (2007).
    • Gingerich, D. J., Hanada, K., shiu, s. H. & Vierstra, R. D. Large-scale, lineage-specific expansion of a bric-a-brac/tramtrack/broad complex ubiquitin-ligase gene family in rice. Plant Cell 19, 2329-2348 (2007).
  • 23
    • 34249819663 scopus 로고    scopus 로고
    • F-box proteins in rice. Genome-wide analysis, classification, temporal and spatial gene expression during panicle and seed development, and regulation by light and abiotic stress
    • Jain, M. et al. F-box proteins in rice. Genome-wide analysis, classification, temporal and spatial gene expression during panicle and seed development, and regulation by light and abiotic stress. Plant Physiol. 143, 1467-1483(2007).
    • (2007) Plant Physiol , vol.143 , pp. 1467-1483
    • Jain, M.1
  • 24
    • 57749114494 scopus 로고    scopus 로고
    • The F-box gene family is expanded in herbaceous annual plants relative to woody perennial plants
    • Yang, X. et al. The F-box gene family is expanded in herbaceous annual plants relative to woody perennial plants. Plant Physiol. 148, 1189-1200 (2008).
    • (2008) Plant Physiol , vol.148 , pp. 1189-1200
    • Yang, X.1
  • 25
    • 33947500177 scopus 로고    scopus 로고
    • Stone, s. L., Williams, L. A., Farmer, L. M., Vierstra, R. D. & Callis, J. KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and development, is involved in abscisic acid signaling. Plant Cell 18, 3415-3428(2006).
    • Stone, s. L., Williams, L. A., Farmer, L. M., Vierstra, R. D. & Callis, J. KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and development, is involved in abscisic acid signaling. Plant Cell 18, 3415-3428(2006).
  • 26
    • 44949242505 scopus 로고    scopus 로고
    • Regulation of cullin RING ligases
    • Hotton,s. K. & Callis, J. Regulation of cullin RING ligases. Annu. Rev. Plant Biol. 59, 467-489 (2008).
    • (2008) Annu. Rev. Plant Biol , vol.59 , pp. 467-489
    • Hotton, S.K.1    Callis, J.2
  • 29
    • 1342346597 scopus 로고    scopus 로고
    • Purification of the Arabidopsis 26s proteasome: Biochemical and molecular analyses revealed the presence of multiple isoforms
    • Yang, P. et al. Purification of the Arabidopsis 26s proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms. J. Biol. Chem. 279, 6401-6413 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 6401-6413
    • Yang, P.1
  • 30
    • 64749095658 scopus 로고    scopus 로고
    • The RPN5 subunit of the 26s proteasome is essential for gametogenesis, sporophyte development, and complex assembly in Arabidopsis
    • Book, A. J. et al. The RPN5 subunit of the 26s proteasome is essential for gametogenesis, sporophyte development, and complex assembly in Arabidopsis. Plant Cell 21, 460-478 (2009).
    • (2009) Plant Cell , vol.21 , pp. 460-478
    • Book, A.J.1
  • 31
    • 0032867676 scopus 로고    scopus 로고
    • The 26s proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P. & Baumeister, W. The 26s proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068(1999).
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 32
    • 44349116590 scopus 로고    scopus 로고
    • Proteasome subunit Rpn13 isa novel ubiquitin receptor
    • Husnjak, K. et al. Proteasome subunit Rpn13 isa novel ubiquitin receptor. Nature 453, 481 -488 (2008).
    • (2008) Nature , vol.453 , pp. 481-488
    • Husnjak, K.1
  • 33
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NEDD-CuL1 conjugate cleavage by COP9 signalosome
    • Lyapina, s. et al. Promotion of NEDD-CuL1 conjugate cleavage by COP9 signalosome. Science 292, 1382-1385(2001).
    • (2001) Science , vol.292 , pp. 1382-1385
    • Lyapina, S.1
  • 34
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 s proteasome subunit Mcb 1
    • Fu,H. et al. Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 s proteasome subunit Mcb 1. J. Biol. Chem. 273, 1970-1981 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 1970-1981
    • Fu, H.1
  • 35
    • 0037390990 scopus 로고    scopus 로고
    • The pleiotropic role of the 26s proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling
    • Smalle, J. et al. The pleiotropic role of the 26s proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling. Plant Cell 15, 965-980 (2003).
    • (2003) Plant Cell , vol.15 , pp. 965-980
    • Smalle, J.1
  • 36
    • 0036007963 scopus 로고    scopus 로고
    • Cytokinin growth responses in Arabidopsis involve the 26s proteasome subunit RPN 12
    • smalle, J. et al. Cytokinin growth responses in Arabidopsis involve the 26s proteasome subunit RPN 12. Plant Cell 14, 17-32 (2002).
    • (2002) Plant Cell , vol.14 , pp. 17-32
    • smalle, J.1
  • 37
    • 33644878524 scopus 로고    scopus 로고
    • Brukhin, V., Gheyselinck, J., Gagliardini, V., Genschik, P. & Grossniklaus, u. The RPN 1 subunit of the 26s proteasome in Arabidopsisis essential for embryogenesis. Plant Cell 17, 2723-2737 (2005).
    • Brukhin, V., Gheyselinck, J., Gagliardini, V., Genschik, P. & Grossniklaus, u. The RPN 1 subunit of the 26s proteasome in Arabidopsisis essential for embryogenesis. Plant Cell 17, 2723-2737 (2005).
  • 38
    • 2542602913 scopus 로고    scopus 로고
    • The HALTED ROOT gene encoding the 26s proteasome subunit RPT2a is essential for the maintenance of Arabidopsismeristems
    • Ueda, M. et al. The HALTED ROOT gene encoding the 26s proteasome subunit RPT2a is essential for the maintenance of Arabidopsismeristems. Development 131, 2101-2111 (2004).
    • (2004) Development , vol.131 , pp. 2101-2111
    • Ueda, M.1
  • 39
    • 0346965700 scopus 로고    scopus 로고
    • O-GIcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang, F. X. et al. O-GIcNAc modification is an endogenous inhibitor of the proteasome. Cell 115, 715-725(2003).
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.X.1
  • 40
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • Schmidt, M., Hanna, J., Elsasser, s. & Finley, D. Proteasome-associated proteins: regulation of a proteolytic machine. Biol. Chem. 386, 725-737 (2005).
    • (2005) Biol. Chem , vol.386 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 41
    • 37249080675 scopus 로고    scopus 로고
    • 26s proteasome regulatory particle mutants have increased oxidative stress tolerance
    • Kurepa, J., Toh, E. A. & smalle, J. A. 26s proteasome regulatory particle mutants have increased oxidative stress tolerance. Plant J. 53, 102-114 (2008).
    • (2008) Plant J , vol.53 , pp. 102-114
    • Kurepa, J.1    Toh, E.A.2    smalle, J.A.3
  • 42
    • 0036646488 scopus 로고    scopus 로고
    • Ustrell, V., Hoffman, L., Pratt, G. & Rechsteiner, M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21, 3516-3525 (2002).
    • Ustrell, V., Hoffman, L., Pratt, G. & Rechsteiner, M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21, 3516-3525 (2002).
  • 43
    • 0034795089 scopus 로고    scopus 로고
    • The ubiquitin-specific protease uBP14 is essential for early embryo development in Arabidopsis thaliana
    • Doelling,J. H., Yan, N., Kurepa, J., Walker, J. & Vierstra, R. D. The ubiquitin-specific protease uBP14 is essential for early embryo development in Arabidopsis thaliana. Plant J. 27, 393-405 (2001).
    • (2001) Plant J , vol.27 , pp. 393-405
    • Doelling, J.H.1    Yan, N.2    Kurepa, J.3    Walker, J.4    Vierstra, R.D.5
  • 44
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating enzyme ubp6 functions noncatalytically to delay proteasomal degradation
    • Hanna, J. et al.Deubiquitinating enzyme ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99-111 (2006).
    • (2006) Cell , vol.127 , pp. 99-111
    • Hanna, J.1
  • 45
    • 36249000098 scopus 로고    scopus 로고
    • The ubiquitin-specific protease subfamily uBP3/uBP4 is essential for pollen development and transmission in Arabidopsis
    • Doelling, J. H. et al. The ubiquitin-specific protease subfamily uBP3/uBP4 is essential for pollen development and transmission in Arabidopsis. Plant Physiol. 145, 801-813 (2007).
    • (2007) Plant Physiol , vol.145 , pp. 801-813
    • Doelling, J.H.1
  • 46
    • 34547135169 scopus 로고    scopus 로고
    • ubiquitin C-terminal hydrolases 1 and 2 affect shoot architecture in Arabidopsis
    • Yang, P. et al. ubiquitin C-terminal hydrolases 1 and 2 affect shoot architecture in Arabidopsis. Plant J. 51, 441-457(2007).
    • (2007) Plant J , vol.51 , pp. 441-457
    • Yang, P.1
  • 47
    • 34250025664 scopus 로고    scopus 로고
    • Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination
    • Sridhar, V. V. et al.Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination. Nature 447, 735-738 (2007).
    • (2007) Nature , vol.447 , pp. 735-738
    • Sridhar, V.V.1
  • 48
    • 56049101398 scopus 로고    scopus 로고
    • uBIQuITIN-sPECIFIC PROTEAsE 26 is required for seed development and the repression of PHERES1 in Arabidopsis
    • Luo, M. et al. uBIQuITIN-sPECIFIC PROTEAsE 26 is required for seed development and the repression of PHERES1 in Arabidopsis. Genetics 180, 229-236 (2008).
    • (2008) Genetics , vol.180 , pp. 229-236
    • Luo, M.1
  • 49
    • 0031080458 scopus 로고    scopus 로고
    • The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana
    • Hatfield, P. M., Gosink, M. M., Carpenter, T. B. & Vierstra, R. D. The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana. Plant J. 11, 213-226(1997).
    • (1997) Plant J , vol.11 , pp. 213-226
    • Hatfield, P.M.1    Gosink, M.M.2    Carpenter, T.B.3    Vierstra, R.D.4
  • 50
    • 7544234937 scopus 로고    scopus 로고
    • systematic analysis and nomenclature of mammalian F-box proteins
    • Jin, J. et al. systematic analysis and nomenclature of mammalian F-box proteins. Genes Dev. 18, 2573-2580(2004).
    • (2004) Genes Dev , vol.18 , pp. 2573-2580
    • Jin, J.1
  • 51
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26s proteasome pathway, the complex last chapter in the life of many plant proteins
    • Vierstra, R. D. The ubiquitin/26s proteasome pathway, the complex last chapter in the life of many plant proteins. Trends Plant Sci. 8, 135-142 (2003).
    • (2003) Trends Plant Sci , vol.8 , pp. 135-142
    • Vierstra, R.D.1
  • 52
    • 0034643336 scopus 로고    scopus 로고
    • schubert, u. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
    • schubert, u. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
  • 53
    • 0037468758 scopus 로고    scopus 로고
    • unravelling angiosperm genome evolution by phylogenetic analysis of chromosomal duplication events
    • Bowers, J. E., Chapman, B. A., Rong, J. & Paterson, A. H. unravelling angiosperm genome evolution by phylogenetic analysis of chromosomal duplication events. Nature 422, 433-438 (2003).
    • (2003) Nature , vol.422 , pp. 433-438
    • Bowers, J.E.1    Chapman, B.A.2    Rong, J.3    Paterson, A.H.4
  • 55
    • 34547108086 scopus 로고    scopus 로고
    • Common sequence polymorphisms shaping genetic diversity in Arabidopsis thaliana
    • Clark, R. M. et al.Common sequence polymorphisms shaping genetic diversity in Arabidopsis thaliana. Science 317, 338-342 (2007).
    • (2007) Science , vol.317 , pp. 338-342
    • Clark, R.M.1
  • 56
    • 40449131628 scopus 로고    scopus 로고
    • TOPLEss mediates auxin-dependent transcriptional repression during Arabidopsis embryogenesis
    • Szemenyei, H., Hannon, M. & Long, J. A. TOPLEss mediates auxin-dependent transcriptional repression during Arabidopsis embryogenesis. Science 319, 1384-1386(2008).
    • (2008) Science , vol.319 , pp. 1384-1386
    • Szemenyei, H.1    Hannon, M.2    Long, J.A.3
  • 57
    • 19544386804 scopus 로고    scopus 로고
    • The ArabidopsisF-box protein TIR1 is an auxin receptor
    • Kepinski, s. & Leyser, O. The ArabidopsisF-box protein TIR1 is an auxin receptor. Nature 435, 446-451 (2005).
    • (2005) Nature , vol.435 , pp. 446-451
    • Kepinski, S.1    Leyser, O.2
  • 58
    • 21344458139 scopus 로고    scopus 로고
    • Plant development is regulated by a family of auxin receptor F box proteins
    • Dharmasiri, N. et al.Plant development is regulated by a family of auxin receptor F box proteins. Dev. Cell 9, 109-119(2005).
    • (2005) Dev. Cell , vol.9 , pp. 109-119
    • Dharmasiri, N.1
  • 59
    • 19544379019 scopus 로고    scopus 로고
    • The F-box protein TIR1 is an auxin receptor
    • Dharmasiri, N., Dharmasiri, s. & Estelle, M. The F-box protein TIR1 is an auxin receptor. Nature 435, 441-445(2005).
    • (2005) Nature , vol.435 , pp. 441-445
    • Dharmasiri, N.1    Dharmasiri, S.2    Estelle, M.3
  • 60
    • 34247219263 scopus 로고    scopus 로고
    • Mechanism of auxin perception by the TIR1 ubiquitin ligase
    • Tan,X. et al. Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature 446, 640-645 (2007).
    • (2007) Nature , vol.446 , pp. 640-645
    • Tan, X.1
  • 61
    • 44449108005 scopus 로고    scopus 로고
    • small-molecule agonists and antagonists of F-box protein-substrate interactions in auxin perception and signaling
    • Hayashi, K. et al.small-molecule agonists and antagonists of F-box protein-substrate interactions in auxin perception and signaling. Proc. Natl Acad. Sci. USA 105, 5632-5637 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 5632-5637
    • Hayashi, K.1
  • 62
    • 0032524404 scopus 로고    scopus 로고
    • COI1: An Arabidopsis gene required for jasmonate-regulated defense and fertility
    • Xie, D. X., Feys, B. F., James, s., Nieto-Rostro, M. & Turner, J. G. COI1: an Arabidopsis gene required for jasmonate-regulated defense and fertility. Science 280, 1091-1094(1998).
    • (1998) Science , vol.280 , pp. 1091-1094
    • Xie, D.X.1    Feys, B.F.2    James, S.3    Nieto-Rostro, M.4    Turner, J.G.5
  • 63
    • 34547727206 scopus 로고    scopus 로고
    • col11 complex during jasmonate signalling
    • col11 complex during jasmonate signalling. Nature 448, 661-665 (2007).
    • (2007) Nature , vol.448 , pp. 661-665
    • Thines, B.1
  • 64
    • 34547743829 scopus 로고    scopus 로고
    • The JAZ family of repressors is the missing link in jasmonate signalling
    • Chini, A. et al. The JAZ family of repressors is the missing link in jasmonate signalling. Nature 448, 666-671 (2007).
    • (2007) Nature , vol.448 , pp. 666-671
    • Chini, A.1
  • 65
    • 44349195100 scopus 로고    scopus 로고
    • Katsir, L, Schilmiller, A. L., staswick, P. E., He, s. Y. & Howe, G. A. COI1 is a critical component of a receptor for jasmonate and the bacterial virulence factor coronatine. Proc. Natl Acad. Sci. USA 105, 7100-7105(2008).
    • Katsir, L, Schilmiller, A. L., staswick, P. E., He, s. Y. & Howe, G. A. COI1 is a critical component of a receptor for jasmonate and the bacterial virulence factor coronatine. Proc. Natl Acad. Sci. USA 105, 7100-7105(2008).
  • 66
    • 34250660460 scopus 로고    scopus 로고
    • The DELLA domain of GA INsENsITIVE mediates the interaction with the GA INsENsITIVE DWARF1A gibberellin receptor of Arabidopsis
    • Willige, B. C. et al.The DELLA domain of GA INsENsITIVE mediates the interaction with the GA INsENsITIVE DWARF1A gibberellin receptor of Arabidopsis. Plant Cell 19, 1209-1220 (2007).
    • (2007) Plant Cell , vol.19 , pp. 1209-1220
    • Willige, B.C.1
  • 67
    • 34548295852 scopus 로고    scopus 로고
    • Molecular interactions of a soluble gibberellin receptor, GID1, with a rice DELLA protein, sLR1, and gibberellin
    • Ueguchi-Tanaka, M. et al. Molecular interactions of a soluble gibberellin receptor, GID1, with a rice DELLA protein, sLR1, and gibberellin. Plant Cell 19, 2140-2155(2007).
    • (2007) Plant Cell , vol.19 , pp. 2140-2155
    • Ueguchi-Tanaka, M.1
  • 68
    • 57049177946 scopus 로고    scopus 로고
    • structural basis for gibberellin recognition by its receptor GID1
    • Shimada, A. et al.structural basis for gibberellin recognition by its receptor GID1. Nature 456, 520-523 (2008).
    • (2008) Nature , vol.456 , pp. 520-523
    • Shimada, A.1
  • 69
    • 57049155555 scopus 로고    scopus 로고
    • Gibberellin-induced DELLA recognition by the gibberellin receptor GID1
    • Murase, K., Hirano, Y., sun, T. P. & Hakoshima, T. Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. Nature 456, 459-463 (2008).
    • (2008) Nature , vol.456 , pp. 459-463
    • Murase, K.1    Hirano, Y.2    sun, T.P.3    Hakoshima, T.4
  • 70
    • 40949092722 scopus 로고    scopus 로고
    • MAPK phosphorylation-induced stabilization of ACs6 protein is mediated by the non-catalytic C-terminal domain, which also contains the cis-determinant for rapid degradation by the 26s proteasome pathway
    • Joo, s., Liu, Y., Lueth, A. & Zhang, s. MAPK phosphorylation-induced stabilization of ACs6 protein is mediated by the non-catalytic C-terminal domain, which also contains the cis-determinant for rapid degradation by the 26s proteasome pathway. Plant J. 54, 129-140 (2008).
    • (2008) Plant J , vol.54 , pp. 129-140
    • Joo, S.1    Liu, Y.2    Lueth, A.3    Zhang, S.4
  • 71
    • 33749013242 scopus 로고    scopus 로고
    • The ACCsynthase TOE sequence is required for interaction with ETO1 family proteins and destabilization of target proteins
    • Yoshida, H. et al. The ACCsynthase TOE sequence is required for interaction with ETO1 family proteins and destabilization of target proteins. Plant Mol. Biol. 62, 427-437 (2006).
    • (2006) Plant Mol. Biol , vol.62 , pp. 427-437
    • Yoshida, H.1
  • 72
    • 0037329952 scopus 로고    scopus 로고
    • The eto 1, eto2, and eto3 mutations and cytokinin treatment increase ethylene biosynthesis in Arabidopsisby increasing the stability of ACs protein
    • Chae, H. s., Faure, F. & Kieber, J. J. The eto 1, eto2, and eto3 mutations and cytokinin treatment increase ethylene biosynthesis in Arabidopsisby increasing the stability of ACs protein. Plant Cell 15, 545-559 (2003).
    • (2003) Plant Cell , vol.15 , pp. 545-559
    • Chae, H.S.1    Faure, F.2    Kieber, J.J.3
  • 73
    • 2342482400 scopus 로고    scopus 로고
    • Regulation of ethylene gas biosynthesis by the ArabidopsisETO1 protein
    • Wang, K. L., Yoshida, H., Lurin, C. & Ecker, J. R. Regulation of ethylene gas biosynthesis by the ArabidopsisETO1 protein. Nature 428, 945-950 (2004).
    • (2004) Nature , vol.428 , pp. 945-950
    • Wang, K.L.1    Yoshida, H.2    Lurin, C.3    Ecker, J.R.4
  • 74
    • 58349085565 scopus 로고    scopus 로고
    • The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate ethylene biosynthesis in Arabidosis by controlling type-2 ACC synthase levels
    • Christians, M. J. et al. The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate ethylene biosynthesis in Arabidosis by controlling type-2 ACC synthase levels. Plant J. 57, 332-345 (2009).
    • (2009) Plant J , vol.57 , pp. 332-345
    • Christians, M.J.1
  • 75
    • 34548324654 scopus 로고    scopus 로고
    • Ligand-induced degradation of the ethylene receptor ETR2 through a proteasome-dependent pathway in Arabidopsis
    • Chen, Y. F. et al. Ligand-induced degradation of the ethylene receptor ETR2 through a proteasome-dependent pathway in Arabidopsis. J. Biol. Chem. 282, 24752-24758 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 24752-24758
    • Chen, Y.F.1
  • 76
    • 61449191658 scopus 로고    scopus 로고
    • Interplay between ethylene, ETP1/ETP2 F-Box proteins, and degradation of EIN2 triggers ethylene responses in Arabidopsis
    • Qiao, H., Chang, K. N.,Yazaki, J. & Ecker, J. R. Interplay between ethylene, ETP1/ETP2 F-Box proteins, and degradation of EIN2 triggers ethylene responses in Arabidopsis. Genes Dev. 23, 512-521 (2009).
    • (2009) Genes Dev , vol.23 , pp. 512-521
    • Qiao, H.1    Chang, K.N.2    Yazaki, J.3    Ecker, J.R.4
  • 77
    • 34250675590 scopus 로고    scopus 로고
    • The Arabidopsis EIN3 binding F-Box proteins EBF1 and EBF2 have distinct but overlapping roles in ethylene signaling
    • Binder, B. M. et al. The Arabidopsis EIN3 binding F-Box proteins EBF1 and EBF2 have distinct but overlapping roles in ethylene signaling. Plant Cell 19, 509-523 (2007).
    • (2007) Plant Cell , vol.19 , pp. 509-523
    • Binder, B.M.1
  • 78
    • 2342452005 scopus 로고    scopus 로고
    • Arabidopsis EIN3-binding F-BOX 1 and 2 form ubiquitin-protein ligases that repress ethylene action and promote growth by directing EIN3 degradation
    • Gagne, J. M. et al. Arabidopsis EIN3-binding F-BOX 1 and 2 form ubiquitin-protein ligases that repress ethylene action and promote growth by directing EIN3 degradation. Proc. Natl Acad. Sci. USA 101,6803-6808(2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6803-6808
    • Gagne, J.M.1
  • 79
    • 0347911970 scopus 로고    scopus 로고
    • EBF1-EBF-2-dependent proteolysis of EIN3 transcription factor
    • EBF1-EBF-2-dependent proteolysis of EIN3 transcription factor. Cell 115, 667-677 (2003).
    • (2003) Cell , vol.115 , pp. 667-677
    • Guo, H.W.1    Ecker, J.R.2
  • 80
    • 0347281690 scopus 로고    scopus 로고
    • EIN3-dependent regulation of plant ethylene hormone signaling by two ArabidopsisF box proteins: EBF1 and EBF2
    • Potuschak, T. et al. EIN3-dependent regulation of plant ethylene hormone signaling by two ArabidopsisF box proteins: EBF1 and EBF2. Cell 115, 679-689 (2003).
    • (2003) Cell , vol.115 , pp. 679-689
    • Potuschak, T.1
  • 81
    • 0141963860 scopus 로고    scopus 로고
    • Yanagisawa, s., Yoo, s. D. & sheen, J. Differential regulation of EIN3 stability by glucose and ethylene signalling in plants. Nature 425, 521-525 (2003).
    • Yanagisawa, s., Yoo, s. D. & sheen, J. Differential regulation of EIN3 stability by glucose and ethylene signalling in plants. Nature 425, 521-525 (2003).
  • 82
    • 39149095565 scopus 로고    scopus 로고
    • 4 signalling. Nature 451, 789-795 (2008).
    • 4 signalling. Nature 451, 789-795 (2008).
  • 83
    • 33845742490 scopus 로고    scopus 로고
    • The exonuclease XRN4 is a component of the ethylene response pathway in Arabidopsis
    • Potushak, T. et al.The exonuclease XRN4 is a component of the ethylene response pathway in Arabidopsis. Plant Cell 18, 3047-3057 (2006).
    • (2006) Plant Cell , vol.18 , pp. 3047-3057
    • Potushak, T.1
  • 84
    • 49849101171 scopus 로고    scopus 로고
    • Ethylene signaling in Arabidopsisinvolves feedback regulation via the elaborate control of EBF2 expression by EIN3
    • Konishi, M. & Yanagisawa, s. Ethylene signaling in Arabidopsisinvolves feedback regulation via the elaborate control of EBF2 expression by EIN3. Plant J. 55,821-831 (2008).
    • (2008) Plant J , vol.55 , pp. 821-831
    • Konishi, M.1    Yanagisawa, S.2
  • 85
    • 33748600413 scopus 로고    scopus 로고
    • ETHYLENE-INSENSITIVE5 encodes a 5'→3' exoribonuclease required for regulation of the EIN3-targeting F-box proteins EBF1/2
    • Olmedo, G. et al. ETHYLENE-INSENSITIVE5 encodes a 5'→3' exoribonuclease required for regulation of the EIN3-targeting F-box proteins EBF1/2. Proc. Natl Acad. Sci. USA 103, 13286-13293 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 13286-13293
    • Olmedo, G.1
  • 86
    • 33947682757 scopus 로고    scopus 로고
    • MAX2 participates in an sCF complex which acts locally at the node to suppress shoot branching
    • Stirnberg, P., Furner, I. J. & Ottoline Leyser, H. M. MAX2 participates in an sCF complex which acts locally at the node to suppress shoot branching. Plant J. 50, 80-94 (2007).
    • (2007) Plant J , vol.50 , pp. 80-94
    • Stirnberg, P.1    Furner, I.J.2    Ottoline Leyser, H.M.3
  • 87
    • 51649096075 scopus 로고    scopus 로고
    • strigolactone inhibition of shoot branching
    • Gomez-Roldan, V. et al.strigolactone inhibition of shoot branching. Nature455, 189-194 (2008).
    • (2008) Nature , vol.455 , pp. 189-194
    • Gomez-Roldan, V.1
  • 88
    • 51649112342 scopus 로고    scopus 로고
    • Inhibition of shoot branching by new terpenoid plant hormones
    • umehara, M. et al.Inhibition of shoot branching by new terpenoid plant hormones. Nature 455, 195-200(2008).
    • (2008) Nature , vol.455 , pp. 195-200
    • umehara, M.1
  • 89
    • 22344447315 scopus 로고    scopus 로고
    • The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradation
    • Zhang, X., Garreton, V. & Chua, N. H. The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradation. Genes Dev. 19,1532-1543(2005).
    • (2005) Genes Dev , vol.19 , pp. 1532-1543
    • Zhang, X.1    Garreton, V.2    Chua, N.H.3
  • 90
    • 57749089790 scopus 로고    scopus 로고
    • Arabidopsis DREB2A-interacting proteins function as RING E3 ligases and negatively regulate plant drought stress-responsive gene expression
    • Qin, F. et al. Arabidopsis DREB2A-interacting proteins function as RING E3 ligases and negatively regulate plant drought stress-responsive gene expression. Plant Cell 20, 1693-1707 (2008).
    • (2008) Plant Cell , vol.20 , pp. 1693-1707
    • Qin, F.1
  • 91
    • 31944433230 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase BIG BROTHER controls Arabidopsisorgan size in a dosage-dependent manner
    • Disch, s. et al. The E3 ubiquitin ligase BIG BROTHER controls Arabidopsisorgan size in a dosage-dependent manner. Curr. Biol. 16, 272-279 (2006).
    • (2006) Curr. Biol , vol.16 , pp. 272-279
    • Disch, S.1
  • 92
    • 44149085427 scopus 로고    scopus 로고
    • Control of final seed and organ size by the DA1 gene family in Arabidopsis thaliana
    • Li, Y., Zheng, L., Corke, F., smith, C. & Bevan, M. W. Control of final seed and organ size by the DA1 gene family in Arabidopsis thaliana. Genes Dev. 22, 1331-1336(2008).
    • (2008) Genes Dev , vol.22 , pp. 1331-1336
    • Li, Y.1    Zheng, L.2    Corke, F.3    smith, C.4    Bevan, M.W.5
  • 93
    • 54549123590 scopus 로고    scopus 로고
    • FBL17 degradation of cell cycle inhibitors
    • FBL17 degradation of cell cycle inhibitors. Nature 455, 1134-1137(2008).
    • (2008) Nature , vol.455 , pp. 1134-1137
    • Kim, H.J.1
  • 94
    • 44449158107 scopus 로고    scopus 로고
    • The BLADE-ON-PETIOLE genes are essential for abscission zone formation in Arabidopsis
    • McKim, s.M. et al. The BLADE-ON-PETIOLE genes are essential for abscission zone formation in Arabidopsis. Development 135, 1537-1546 (2008).
    • (2008) Development , vol.135 , pp. 1537-1546
    • McKim, S.M.1
  • 95
    • 33744965905 scopus 로고    scopus 로고
    • uFO in the Arabidopsisinflorescence apex is required for floral-meristem identity and bract suppression
    • Hepworth, S. R., Klenz, J. E. & Haughn, G. W. uFO in the Arabidopsisinflorescence apex is required for floral-meristem identity and bract suppression. Planta 223, 769-778 (2006).
    • (2006) Planta , vol.223 , pp. 769-778
    • Hepworth, S.R.1    Klenz, J.E.2    Haughn, G.W.3
  • 96
    • 0036336159 scopus 로고    scopus 로고
    • MAX1 and MAX2 control shoot lateral branching in Arabidopsis
    • Stirnberg, P., van De sande, K. & Leyser, H. M. MAX1 and MAX2 control shoot lateral branching in Arabidopsis. Development 129, 1131-1141 (2002).
    • (2002) Development , vol.129 , pp. 1131-1141
    • Stirnberg, P.1    van De sande, K.2    Leyser, H.M.3
  • 97
    • 34250675605 scopus 로고    scopus 로고
    • Characterization of the VIER F-BOX PROTEINE genes from Arabidopsisreveals their importance for plant growth and development
    • Schwager, K. M. et al. Characterization of the VIER F-BOX PROTEINE genes from Arabidopsisreveals their importance for plant growth and development. Plant Cell 19, 1163-1178 (2007).
    • (2007) Plant Cell , vol.19 , pp. 1163-1178
    • Schwager, K.M.1
  • 99
    • 23944503311 scopus 로고    scopus 로고
    • Regulated proteolysis in light signaling
    • Hoecker, u. Regulated proteolysis in light signaling. Curr. Opin. Plant Biol. 8, 469-476 (2005).
    • (2005) Curr. Opin. Plant Biol , vol.8 , pp. 469-476
    • Hoecker, U.1
  • 100
    • 0033041152 scopus 로고    scopus 로고
    • sequences within both the N- and C-terminal domains of phytochrome A are required for PFR ubiquitination and degradation
    • Clough, R. C. et al. sequences within both the N- and C-terminal domains of phytochrome A are required for PFR ubiquitination and degradation. Plant J. 17, 155-167 (1999).
    • (1999) Plant J , vol.17 , pp. 155-167
    • Clough, R.C.1
  • 101
    • 37249059866 scopus 로고    scopus 로고
    • Arabidopsiscryptochrome 2 completes its posttranslational life cycle in the nucleus
    • Yu, X. et al. Arabidopsiscryptochrome 2 completes its posttranslational life cycle in the nucleus. Plant Cell 19, 3146-3156(2007).
    • (2007) Plant Cell , vol.19 , pp. 3146-3156
    • Yu, X.1
  • 102
    • 33746428382 scopus 로고    scopus 로고
    • Photoactivated phytochrome induces rapid PIF3 phosphorylation prior to proteasome-mediated degradation
    • Al-sady, B., Ni, W., Kircher, s., schafer, E. & Quail, P. H. Photoactivated phytochrome induces rapid PIF3 phosphorylation prior to proteasome-mediated degradation. Mol. Cell 23, 439-446 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 439-446
    • Al-sady, B.1    Ni, W.2    Kircher, S.3    schafer, E.4    Quail, P.H.5
  • 103
    • 0034713297 scopus 로고    scopus 로고
    • Targeted destabilization of HY5 during light-regulated development of Arabidopsis
    • Osterlund, M. T., Hardtke, C. s., Wei, N. & Deng, X. W. Targeted destabilization of HY5 during light-regulated development of Arabidopsis. Nature 405, 462-466 (2000).
    • (2000) Nature , vol.405 , pp. 462-466
    • Osterlund, M.T.1    Hardtke, C.S.2    Wei, N.3    Deng, X.W.4
  • 104
    • 42449119813 scopus 로고    scopus 로고
    • ArabidopsisCOP1 shapes the temporal pattern of CO accumulation conferring a photoperiodic flowering response
    • Jang, s. et al. ArabidopsisCOP1 shapes the temporal pattern of CO accumulation conferring a photoperiodic flowering response. EMBOJ. 27, 1277-1288(2008).
    • (2008) EMBOJ , vol.27 , pp. 1277-1288
    • Jang, S.1
  • 105
    • 0348134861 scopus 로고    scopus 로고
    • Mas, P., Kim, W. Y., somers, D. E. & Kay, s. A. Targeted degradation of TOC1 by ZTL modulates circadian function in Arabidopsis thaliana. Nature 426, 567-570 (2003).
    • Mas, P., Kim, W. Y., somers, D. E. & Kay, s. A. Targeted degradation of TOC1 by ZTL modulates circadian function in Arabidopsis thaliana. Nature 426, 567-570 (2003).
  • 106
    • 35348910170 scopus 로고    scopus 로고
    • sawa, M., Nusinow, D. A., Kay, s. A. & Imaizumi, T. FKF1 and GIGANTEA complex formation is required for day-length measurement in Arabidopsis. Science 318,261-265(2007).
    • sawa, M., Nusinow, D. A., Kay, s. A. & Imaizumi, T. FKF1 and GIGANTEA complex formation is required for day-length measurement in Arabidopsis. Science 318,261-265(2007).
  • 107
    • 22044444886 scopus 로고    scopus 로고
    • Imaizumi, T, Schultz, T. F., Harmon, F. G., Ho, L. A. & Kay, s. A. FKF1 F-box protein mediates cyclic degradation of a repressor of CONSTANS in Arabidopsis. Science 309, 293-297 (2005).
    • Imaizumi, T, Schultz, T. F., Harmon, F. G., Ho, L. A. & Kay, s. A. FKF1 F-box protein mediates cyclic degradation of a repressor of CONSTANS in Arabidopsis. Science 309, 293-297 (2005).
  • 108
    • 34548813657 scopus 로고    scopus 로고
    • ZEITLuPE is a circadian photoreceptor stabilized by GIGANTEA in blue light
    • Kim, W. Y. et al.ZEITLuPE is a circadian photoreceptor stabilized by GIGANTEA in blue light. Nature 449, 356-360 (2007).
    • (2007) Nature , vol.449 , pp. 356-360
    • Kim, W.Y.1
  • 109
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D. & Dangl, J. L. The plant immune system. Nature 444, 323-329 (2006).
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 110
    • 0037086007 scopus 로고    scopus 로고
    • The RAR1 interactorsGT1,an essential component of R gene-triggered disease resistance
    • Azevedo, C. et al.The RAR1 interactorsGT1,an essential component of R gene-triggered disease resistance. Science 295, 2073-2076 (2002).
    • (2002) Science , vol.295 , pp. 2073-2076
    • Azevedo, C.1
  • 111
    • 0037086347 scopus 로고    scopus 로고
    • Regulatory role of SGT1 in early R gene-mediated plant defenses
    • Austin, M.J. et al. Regulatory role of SGT1 in early R gene-mediated plant defenses. Science 295, 2077-2080 (2002).
    • (2002) Science , vol.295 , pp. 2077-2080
    • Austin, M.J.1
  • 112
    • 33745479207 scopus 로고    scopus 로고
    • The u-box protein CMPG1 is required for efficient activation of defense mechanisms triggered by multiple resistance genes in tobacco and tomato
    • Gonzalez-Lamothe, R. et al. The u-box protein CMPG1 is required for efficient activation of defense mechanisms triggered by multiple resistance genes in tobacco and tomato. Plant Cell 18, 1067-1083 (2006).
    • (2006) Plant Cell , vol.18 , pp. 1067-1083
    • Gonzalez-Lamothe, R.1
  • 113
    • 52049119002 scopus 로고    scopus 로고
    • Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in Arabidopsis
    • Trujillo, M., Ichimura, K., Casais, C. & shirasu, K. Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in Arabidopsis. Curr. Biol. 18, 1396-1401 (2008).
    • (2008) Curr. Biol , vol.18 , pp. 1396-1401
    • Trujillo, M.1    Ichimura, K.2    Casais, C.3    shirasu, K.4
  • 114
    • 49649112131 scopus 로고    scopus 로고
    • Plant immunity requires conformational charges of NPR1 via s-nitrosylation and thioredoxins
    • Tada, Y. et al. Plant immunity requires conformational charges of NPR1 via s-nitrosylation and thioredoxins. Science 321, 952-956 (2008).
    • (2008) Science , vol.321 , pp. 952-956
    • Tada, Y.1
  • 115
    • 30844458212 scopus 로고    scopus 로고
    • A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase
    • Janjusevic, R., Abramovitch, R. B., Martin, G. B. & stebbins, C. E. A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 311, 222-226 (2006).
    • (2006) Science , vol.311 , pp. 222-226
    • Janjusevic, R.1    Abramovitch, R.B.2    Martin, G.B.3    stebbins, C.E.4
  • 116
    • 34447542796 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity
    • Rosebrock, T. R. et al. A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity. Nature 448, 370-374 (2007).
    • (2007) Nature , vol.448 , pp. 370-374
    • Rosebrock, T.R.1
  • 118
    • 34548474870 scopus 로고    scopus 로고
    • The polerovirus silencing suppressor P0 targets ARGONAuTE proteins for degradation
    • Baumberger, N., Tsai, C. H., Lie, M., Havecker, E. & Baulcombe, D. C. The polerovirus silencing suppressor P0 targets ARGONAuTE proteins for degradation. Curr. Biol. 17, 1609-1614 (2007).
    • (2007) Curr. Biol , vol.17 , pp. 1609-1614
    • Baumberger, N.1    Tsai, C.H.2    Lie, M.3    Havecker, E.4    Baulcombe, D.C.5
  • 119
    • 33749257294 scopus 로고    scopus 로고
    • Ralstonia solanacearum requires F-box-like domain-containing type III effectors to promote disease on several host plants
    • Angot, A. et al. Ralstonia solanacearum requires F-box-like domain-containing type III effectors to promote disease on several host plants. Proc. Natl Acad. Sci. USA 103, 14620-14625 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14620-14625
    • Angot, A.1
  • 120
    • 4544272781 scopus 로고    scopus 로고
    • Involvement of targeted proteolysis in plant genetic transformation by Agrobacterium
    • Tzfira, T., Vaidya, M. & Citovsky, V. Involvement of targeted proteolysis in plant genetic transformation by Agrobacterium. Nature 431, 87-92 (2004).
    • (2004) Nature , vol.431 , pp. 87-92
    • Tzfira, T.1    Vaidya, M.2    Citovsky, V.3
  • 121
    • 0242416566 scopus 로고    scopus 로고
    • ARC1 is an E3 ubiquitin ligase and promotes the ubiquitination of proteins during the rejection of self-incompatible Brassica pollen
    • Stone, S. L., Anderson, E. M., Mullen, R. T. & Goring, D. R. ARC1 is an E3 ubiquitin ligase and promotes the ubiquitination of proteins during the rejection of self-incompatible Brassica pollen. Plant Cell 15, 885-898 (2003).
    • (2003) Plant Cell , vol.15 , pp. 885-898
    • Stone, S.L.1    Anderson, E.M.2    Mullen, R.T.3    Goring, D.R.4
  • 122
    • 53749090930 scopus 로고    scopus 로고
    • Interactions between the s-domain receptor kinases and AtPuB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis
    • Samuel, M. A. et al. Interactions between the s-domain receptor kinases and AtPuB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis. Plant Physiol. 147, 2084-2095 (2008).
    • (2008) Plant Physiol , vol.147 , pp. 2084-2095
    • Samuel, M.A.1
  • 123
    • 2442692997 scopus 로고    scopus 로고
    • Identification of the pollen determinant of s-RNase-mediated self-incompatibility
    • Sijacic, P. et al. Identification of the pollen determinant of s-RNase-mediated self-incompatibility. Nature 429, 302-305 (2004).
    • (2004) Nature , vol.429 , pp. 302-305
    • Sijacic, P.1
  • 124
    • 33646865011 scopus 로고    scopus 로고
    • AhssK1, a novel sKP1 -like protein that interacts with the s-locus F-Box protein sLF
    • Huang, J., Zhao, L., Yang, Q. & Xue, Y. AhssK1, a novel sKP1 -like protein that interacts with the s-locus F-Box protein sLF. Plant J. 46, 780-793 (2006).
    • (2006) Plant J , vol.46 , pp. 780-793
    • Huang, J.1    Zhao, L.2    Yang, Q.3    Xue, Y.4
  • 125
    • 33750999066 scopus 로고    scopus 로고
    • Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in s-RNase-based self-incompatibility
    • Hua, Z. & Kao, T. H. Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in s-RNase-based self-incompatibility. Plant Cell 18, 2531-2553(2006).
    • (2006) Plant Cell , vol.18 , pp. 2531-2553
    • Hua, Z.1    Kao, T.H.2
  • 126
    • 37849007169 scopus 로고    scopus 로고
    • Comparison of Petunia inflata S-locus F-box protein (Pi sLF) with Pi sLF like proteins reveals its unique function in s-RNase based self-incompatibility
    • Hua, Z., Meng, X. & Kao, T. H. Comparison of Petunia inflata S-locus F-box protein (Pi sLF) with Pi sLF like proteins reveals its unique function in s-RNase based self-incompatibility. Plant Cell 19, 3593-3609 (2007).
    • (2007) Plant Cell , vol.19 , pp. 3593-3609
    • Hua, Z.1    Meng, X.2    Kao, T.H.3
  • 127
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake, V. M. & Workman, J. L. Histone ubiquitination: triggering gene activity. Mol. Cell 29, 653-663 (2008).
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 128
    • 34250650034 scopus 로고    scopus 로고
    • The Arabidopsis thaliana homolog of yeast BRE1 has a function in cell cycle regulation during early leaf and root growth
    • Fleury, D. et al. The Arabidopsis thaliana homolog of yeast BRE1 has a function in cell cycle regulation during early leaf and root growth. Plant Cell 19, 417-432(2007).
    • (2007) Plant Cell , vol.19 , pp. 417-432
    • Fleury, D.1
  • 129
    • 34250620427 scopus 로고    scopus 로고
    • The absence of histone H2B monoubiquitination in the Arabidopsis hub 1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy
    • Liu, Y., Koornneef, M. & soppe, W. J. The absence of histone H2B monoubiquitination in the Arabidopsis hub 1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy. Plant Cell 19, 433-444 (2007).
    • (2007) Plant Cell , vol.19 , pp. 433-444
    • Liu, Y.1    Koornneef, M.2    soppe, W.J.3
  • 130
    • 57649106346 scopus 로고    scopus 로고
    • Kraft, E., Bostick, M., Jacobsen, s. E. & Callis, J. ORTH/VIM proteins that regulate DNA methylation are functional ubiquitin E3 ligases. Plant J. 56, 704-715(2008).
    • Kraft, E., Bostick, M., Jacobsen, s. E. & Callis, J. ORTH/VIM proteins that regulate DNA methylation are functional ubiquitin E3 ligases. Plant J. 56, 704-715(2008).
  • 131
    • 0041706156 scopus 로고    scopus 로고
    • A proteomics approach to understanding protein ubiquitination
    • Peng, J. et al. A proteomics approach to understanding protein ubiquitination. Nature Biotech. 21, 921-926 (2003).
    • (2003) Nature Biotech , vol.21 , pp. 921-926
    • Peng, J.1
  • 132
    • 20044373693 scopus 로고    scopus 로고
    • Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin
    • Kirkpatrick, D. s., Weldon, s. F., Tsaprailis, G., Liebler, D. C. & Gandolfi, A. J. Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin. Proteomics 5, 2104-2111 (2005).
    • (2005) Proteomics , vol.5 , pp. 2104-2111
    • Kirkpatrick, D.S.1    Weldon, S.F.2    Tsaprailis, G.3    Liebler, D.C.4    Gandolfi, A.J.5
  • 133
    • 27744500428 scopus 로고    scopus 로고
    • Large-scale analysis of the human ubiquitin-related proteome
    • Matsumoto, M. et al. Large-scale analysis of the human ubiquitin-related proteome. Proteomics 5, 4145-4151 (2005).
    • (2005) Proteomics , vol.5 , pp. 4145-4151
    • Matsumoto, M.1
  • 134
    • 36749080327 scopus 로고    scopus 로고
    • Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn 10 receptor pathway
    • Mayor, T., Graumann, J., Bryan, J., MacCoss, M.J. & Deshaies, R. J. Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn 10 receptor pathway. Mol. Cell. Proteomics 6,1885-1895 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1885-1895
    • Mayor, T.1    Graumann, J.2    Bryan, J.3    MacCoss, M.J.4    Deshaies, R.J.5
  • 135
    • 0242300110 scopus 로고    scopus 로고
    • Hitchcock, A. L., Auld, K., Gygi, s. P. & silver, P. A. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl Acad. Sci. USA 100, 12735-12740 (2003).
    • Hitchcock, A. L., Auld, K., Gygi, s. P. & silver, P. A. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl Acad. Sci. USA 100, 12735-12740 (2003).
  • 136
    • 34247342702 scopus 로고    scopus 로고
    • Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants
    • Maor, R. et al. Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants. Mol. Cell Proteomics 6, 601 -610 (2007).
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 601-610
    • Maor, R.1
  • 137
    • 67649696034 scopus 로고    scopus 로고
    • saracco, s. A. et al. Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant J. 9 Mar 2009 (doi: 10.1111 /j. 1365-313×.2009.03862.×).
    • saracco, s. A. et al. Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant J. 9 Mar 2009 (doi: 10.1111 /j. 1365-313×.2009.03862.×).
  • 138
    • 63549150374 scopus 로고    scopus 로고
    • A rice kinase-protein interaction map
    • Ding, X. et al. A rice kinase-protein interaction map. Plant Physiol. 149, 1478-1492 (2009).
    • (2009) Plant Physiol , vol.149 , pp. 1478-1492
    • Ding, X.1
  • 139
    • 0023234618 scopus 로고
    • Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin
    • Vijay-Kumar, s. et al.Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin. J. Biol. Chem. 262, 6396-6399 (1987).
    • (1987) J. Biol. Chem , vol.262 , pp. 6396-6399
    • Vijay-Kumar, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.