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Volumn 25, Issue 1, 2014, Pages 1-16

A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1

Author keywords

[No Author keywords available]

Indexed keywords

SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 84891803634     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-05-0291     Document Type: Article
Times cited : (22)

References (78)
  • 1
    • 84870536561 scopus 로고    scopus 로고
    • The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase
    • Alonso A, D'Silva S, Rahman M, Meluh PB, Keeling J, Meednu N, Hoops HJ, Miller RK (2012). The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase. Mol Biol Cell 23, 4552-4566.
    • (2012) Mol Biol Cell , vol.23 , pp. 4552-4566
    • Alonso, A.1    D'silva, S.2    Rahman, M.3    Meluh, P.B.4    Keeling, J.5    Meednu, N.6    Hoops, H.J.7    Miller, R.K.8
  • 3
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann CB, Davies A, Cost GJ, Caputo E (1998). Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4
  • 4
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • Bylebyl GR, Belichenko I, Johnson ES (2003). The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J Biol Chem 278, 44113-44120.
    • (2003) J Biol Chem , vol.278 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 5
    • 70350499161 scopus 로고    scopus 로고
    • The evolution, complex structures and function of septin proteins
    • Cao L, Yu W, Wu Y, Yu L (2009). The evolution, complex structures and function of septin proteins. Cell Mol Life Sci 66, 3309-3323.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3309-3323
    • Cao, L.1    Yu, W.2    Wu, Y.3    Yu, L.4
  • 6
    • 33746604882 scopus 로고    scopus 로고
    • SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae
    • Cheng C-H, Lo Y-H, Liang S-S, Ti S-C, Lin F-M, Yeh C-H, Huang H-Y, Wang T-F (2006). SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae. Genes Dev 20, 2067-2081.
    • (2006) Genes Dev , vol.20 , pp. 2067-2081
    • Cheng, C.-H.1    Lo, Y.-H.2    Liang, S.-S.3    Ti, S.-C.4    Lin, F.-M.5    Yeh, C.-H.6    Huang, H.-Y.7    Wang, T.-F.8
  • 7
    • 65949105701 scopus 로고    scopus 로고
    • The SUMO-targeted ubiquitin ligase subunit Slx5 resides in nuclear foci and at sites of DNA breaks
    • Cook CE, Hochstrasser M, Kerscher O (2009). The SUMO-targeted ubiquitin ligase subunit Slx5 resides in nuclear foci and at sites of DNA breaks. Cell Cycle 8, 1080-1089.
    • (2009) Cell Cycle , vol.8 , pp. 1080-1089
    • Cook, C.E.1    Hochstrasser, M.2    Kerscher, O.3
  • 9
    • 0033523996 scopus 로고    scopus 로고
    • The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae
    • DeVit MJ, Johnston M (1999). The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae. Curr Biol 9, 1231-1241.
    • (1999) Curr Biol , vol.9 , pp. 1231-1241
    • Devit, M.J.1    Johnston, M.2
  • 13
    • 19044367766 scopus 로고    scopus 로고
    • Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5
    • Fagerlund R, Mélen K, Kinnunen L, Julkunen I (2002). Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5. J Biol Chem 277, 30072-30078.
    • (2002) J Biol Chem , vol.277 , pp. 30072-30078
    • Fagerlund, R.1    Mélen, K.2    Kinnunen, L.3    Julkunen, I.4
  • 14
    • 66149094306 scopus 로고    scopus 로고
    • Dimerization and a novel Tax speckled structure localization signal are required for Tax nuclear localization
    • Fryrear KA, Durkin SS, Gupta SK, Tiedebohl JB, Semmes OJ (2009). Dimerization and a novel Tax speckled structure localization signal are required for Tax nuclear localization. J Virol 83, 5339-5352.
    • (2009) J Virol , vol.83 , pp. 5339-5352
    • Fryrear, K.A.1    Durkin, S.S.2    Gupta, S.K.3    Tiedebohl, J.B.4    Semmes, O.J.5
  • 15
    • 84856621090 scopus 로고    scopus 로고
    • The Sumo-targeted ubiquitin ligase RNF4 regulates the localization and function of the HTLV-1 oncoprotein Tax
    • Fryrear KA, Guo X, Kerscher O, Semmes OJ (2012). The Sumo-targeted ubiquitin ligase RNF4 regulates the localization and function of the HTLV-1 oncoprotein Tax. Blood 119, 1173-1181.
    • (2012) Blood , vol.119 , pp. 1173-1181
    • Fryrear, K.A.1    Guo, X.2    Kerscher, O.3    Semmes, O.J.4
  • 16
    • 84870013890 scopus 로고    scopus 로고
    • STUbLs in chromatin and genome stability
    • Garza R, Pillus L (2013). STUbLs in chromatin and genome stability. Biopolymers 99, 146-154.
    • (2013) Biopolymers , vol.99 , pp. 146-154
    • Garza, R.1    Pillus, L.2
  • 17
    • 68049103216 scopus 로고    scopus 로고
    • An additional role for SUMO in ubiquitin-mediated proteolysis
    • Geoffroy M-C, Hay RT (2009). An additional role for SUMO in ubiquitin-mediated proteolysis. Nat Rev Mol Cell Biol 10, 564-568.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 564-568
    • Geoffroy, M.-C.1    Hay, R.T.2
  • 19
    • 84870760201 scopus 로고    scopus 로고
    • RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage
    • Guzzo CM, Berndsen CE, Zhu J, Gupta V, Datta A, Greenberg RA, Wolberger C, Matunis MJ (2012). RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage. Sci Signal 5, ra88.
    • (2012) Sci Signal , vol.5
    • Guzzo, C.M.1    Berndsen, C.E.2    Zhu, J.3    Gupta, V.4    Datta, A.5    Greenberg, R.A.6    Wolberger, C.7    Matunis, M.J.8
  • 20
    • 84875887144 scopus 로고    scopus 로고
    • Expanding SUMO and ubiquitin-mediated signaling through hybrid SUMO-ubiquitin chains and their receptors
    • Guzzo CM, Matunis MJ (2013). Expanding SUMO and ubiquitin-mediated signaling through hybrid SUMO-ubiquitin chains and their receptors. Cell Cycle 12, 1015-1017.
    • (2013) Cell Cycle , vol.12 , pp. 1015-1017
    • Guzzo, C.M.1    Matunis, M.J.2
  • 21
    • 65649091344 scopus 로고    scopus 로고
    • Reciprocal regulation of nuclear import of the yeast MutSalpha DNA mismatch repair proteins Msh2 and Msh6
    • Hayes AP, Sevi LA, Feldt MC, Rose MD, Gammie AE (2009). Reciprocal regulation of nuclear import of the yeast MutSalpha DNA mismatch repair proteins Msh2 and Msh6. DNA Repair (Amst) 8, 739-751.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 739-751
    • Hayes, A.P.1    Sevi, L.A.2    Feldt, M.C.3    Rose, M.D.4    Gammie, A.E.5
  • 22
    • 0029040945 scopus 로고
    • Arginine-rich regions succeeding the nuclear localization region of the herpes simplex virus type 1 regulatory protein ICP27 are required for efficient nuclear localization and late gene expression
    • Hibbard MK, Sandri-Goldin RM (1995). Arginine-rich regions succeeding the nuclear localization region of the herpes simplex virus type 1 regulatory protein ICP27 are required for efficient nuclear localization and late gene expression. J Virol 69, 4656-4667.
    • (1995) J Virol , vol.69 , pp. 4656-4667
    • Hibbard, M.K.1    Sandri-Goldin, R.M.2
  • 23
    • 79958753032 scopus 로고    scopus 로고
    • UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae
    • Ho C-W, Chen H-T, Hwang J (2011). UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae. J Biol Chem 286, 21826-21834.
    • (2011) J Biol Chem , vol.286 , pp. 21826-21834
    • Ho, C.-W.1    Chen, H.-T.2    Hwang, J.3
  • 24
    • 0026803107 scopus 로고
    • Expression of a ubiquitin derivative that conjugates to protein irreversibly produces phenotypes consistent with a ubiquitin deficiency
    • Hodgins RR, Ellison KS, Ellison MJ (1992). Expression of a ubiquitin derivative that conjugates to protein irreversibly produces phenotypes consistent with a ubiquitin deficiency. J Biol Chem 267, 8807-8812.
    • (1992) J Biol Chem , vol.267 , pp. 8807-8812
    • Hodgins, R.R.1    Ellison, K.S.2    Ellison, M.J.3
  • 25
    • 35348982302 scopus 로고    scopus 로고
    • Stimulation of in vitro sumoylation by Slx5-Slx8: Evidence for a functional interaction with the SUMO pathway
    • Ii T, Mullen JR, Slagle CE, Brill SJ (2007). Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway. DNA Repair (Amst) 6, 1679-1691.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 1679-1691
    • Ii, T.1    Mullen, J.R.2    Slagle, C.E.3    Brill, S.J.4
  • 26
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson ES, Blobel G (1999). Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J Cell Biol 147, 981-994.
    • (1999) J Cell Biol , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 27
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson ES, Gupta AA (2001). An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106, 735-744.
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 28
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O (2007). SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep 8, 550-555.
    • (2007) EMBO Rep , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 29
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M (2006). Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22, 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 30
    • 84891645382 scopus 로고    scopus 로고
    • Coordinate to guard: Crosstalk of phosphorylation, sumoylation, and ubiquitylation in DNA damage response
    • Kuo CY, Shieh C, Cai F, Ann DK (2012). Coordinate to guard: crosstalk of phosphorylation, sumoylation, and ubiquitylation in DNA damage response. Front Oncol 1, 61.
    • (2012) Front Oncol , vol.1 , pp. 61
    • Kuo, C.Y.1    Shieh, C.2    Cai, F.3    Ann, D.K.4
  • 31
    • 0036645506 scopus 로고    scopus 로고
    • Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast
    • Kusch J, Meyer A, Snyder MP, Barral Y (2002). Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Genes Dev 16, 1627-1639.
    • (2002) Genes Dev , vol.16 , pp. 1627-1639
    • Kusch, J.1    Meyer, A.2    Snyder, M.P.3    Barral, Y.4
  • 32
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S-J, Hochstrasser M (1999). A new protease required for cell-cycle progression in yeast. Nature 398, 246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 33
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • Li S-J, Hochstrasser M (2000). The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol Cell Biol 20, 2367-2377.
    • (2000) Mol Cell Biol , vol.20 , pp. 2367-2377
    • Li, S.-J.1    Hochstrasser, M.2
  • 34
    • 0037417333 scopus 로고    scopus 로고
    • The Ulp1 SUMO isopeptidase
    • Li S-J, Hochstrasser M (2003). The Ulp1 SUMO isopeptidase. J Cell Biol 160, 1069-1081.
    • (2003) J Cell Biol , vol.160 , pp. 1069-1081
    • Li, S.-J.1    Hochstrasser, M.2
  • 35
    • 77956638214 scopus 로고    scopus 로고
    • RING domain dimerization is essential for RNF4 function
    • Liew CW, Sun H, Hunter T, Day CL (2010). RING domain dimerization is essential for RNF4 function. Biochem J 431, 23-29.
    • (2010) Biochem J , vol.431 , pp. 23-29
    • Liew, C.W.1    Sun, H.2    Hunter, T.3    Day, C.L.4
  • 36
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Lin D-Y et al. (2006). Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol Cell 24, 341-354.
    • (2006) Mol Cell , vol.24 , pp. 341-354
    • Lin, D.-Y.1
  • 37
  • 39
    • 77949378117 scopus 로고    scopus 로고
    • The SUMO protease SENP6 is essential for inner kinetochore assembly
    • Mukhopadhyay D, Arnaoutov A, Dasso M (2010). The SUMO protease SENP6 is essential for inner kinetochore assembly. J Cell Biol 188, 681-692.
    • (2010) J Cell Biol , vol.188 , pp. 681-692
    • Mukhopadhyay, D.1    Arnaoutov, A.2    Dasso, M.3
  • 40
    • 50649104647 scopus 로고    scopus 로고
    • Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates
    • Mullen JR, Brill SJ (2008). Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates. J Biol Chem 283, 19912-19921.
    • (2008) J Biol Chem , vol.283 , pp. 19912-19921
    • Mullen, J.R.1    Brill, S.J.2
  • 41
    • 78951471597 scopus 로고    scopus 로고
    • Genetic evidence that polysumoylation bypasses the need for a SUMO-targeted Ub ligase
    • Mullen JR, Das M, Brill SJ (2011). Genetic evidence that polysumoylation bypasses the need for a SUMO-targeted Ub ligase. Genetics 187, 73-87.
    • (2011) Genetics , vol.187 , pp. 73-87
    • Mullen, J.R.1    Das, M.2    Brill, S.J.3
  • 42
    • 0035148955 scopus 로고    scopus 로고
    • Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae
    • Mullen JR, Kaliraman V, Ibrahim SS, Brill SJ (2001). Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae. Genetics 157, 103-118.
    • (2001) Genetics , vol.157 , pp. 103-118
    • Mullen, J.R.1    Kaliraman, V.2    Ibrahim, S.S.3    Brill, S.J.4
  • 44
    • 84865475874 scopus 로고    scopus 로고
    • Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions
    • Nie M, Aslanian A, Prudden J, Heideker J, Vashisht AA, Wohlschlegel JA, Yates JR, Boddy MN (2012). Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions. J Biol Chem 287, 29610-29619.
    • (2012) J Biol Chem , vol.287 , pp. 29610-29619
    • Nie, M.1    Aslanian, A.2    Prudden, J.3    Heideker, J.4    Vashisht, A.A.5    Wohlschlegel, J.A.6    Yates, J.R.7    Boddy, M.N.8
  • 46
    • 84871206469 scopus 로고    scopus 로고
    • A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA
    • Parker JL, Ulrich HD (2012). A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA. Nucleic Acids Res 40, 11380-11388.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11380-11388
    • Parker, J.L.1    Ulrich, H.D.2
  • 49
    • 33947539481 scopus 로고    scopus 로고
    • Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
    • Ravid T, Hochstrasser M (2007). Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue. Nat Cell Biol 9, 422-427.
    • (2007) Nat Cell Biol , vol.9 , pp. 422-427
    • Ravid, T.1    Hochstrasser, M.2
  • 51
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson DA, Wang M, Matunis MJ (2001). The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J Biol Chem 276, 21664-21669.
    • (2001) J Biol Chem , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 52
    • 0033571410 scopus 로고    scopus 로고
    • Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape
    • Sesaki H, Jensen RE (1999). Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape. J Cell Biol 147, 699-706.
    • (1999) J Cell Biol , vol.147 , pp. 699-706
    • Sesaki, H.1    Jensen, R.E.2
  • 54
    • 0034729194 scopus 로고    scopus 로고
    • Yeast nucleoporins involved in passive nuclear envelope permeability
    • Shulga N, Mosammaparast N, Wozniak R, Goldfarb DS (2000). Yeast nucleoporins involved in passive nuclear envelope permeability. J Cell Biol 149, 1027-1038.
    • (2000) J Cell Biol , vol.149 , pp. 1027-1038
    • Shulga, N.1    Mosammaparast, N.2    Wozniak, R.3    Goldfarb, D.S.4
  • 55
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling
    • Stehmeier P, Muller S (2009). Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol Cell 33, 400-409.
    • (2009) Mol Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 56
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • Sun H, Leverson JD, 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
  • 57
    • 84886814349 scopus 로고    scopus 로고
    • Budding yeast protein extraction and purification for the study of function, interactions, and post-translational modifications
    • Szymanski EP, Kerscher O (2013). Budding yeast protein extraction and purification for the study of function, interactions, and post-translational modifications. J Vis Exp 80, e50921.
    • (2013) J Vis Exp , vol.80
    • Szymanski, E.P.1    Kerscher, O.2
  • 58
  • 59
    • 0035966066 scopus 로고    scopus 로고
    • Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates
    • Takahashi Y, Kahyo T, Toh-E A, Yasuda H, Kikuchi Y (2001a). Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates. J Biol Chem 276, 48973-48977.
    • (2001) J Biol Chem , vol.276 , pp. 48973-48977
    • Takahashi, Y.1    Kahyo, T.2    Toh-E, A.3    Yasuda, H.4    Kikuchi, Y.5
  • 60
    • 27744503961 scopus 로고    scopus 로고
    • Yeast PIAS-type Ull1/Siz1 is composed of SUMO ligase and regulatory domains
    • Takahashi Y, Kikuchi Y (2005). Yeast PIAS-type Ull1/Siz1 is composed of SUMO ligase and regulatory domains. J Biol Chem 280, 35822-35828.
    • (2005) J Biol Chem , vol.280 , pp. 35822-35828
    • Takahashi, Y.1    Kikuchi, Y.2
  • 61
    • 0035913722 scopus 로고    scopus 로고
    • A novel factor required for the SUMO1/Smt3 conjugation of yeast septins
    • Takahashi Y, Toh-E A, Kikuchi Y (2001b). A novel factor required for the SUMO1/Smt3 conjugation of yeast septins. Gene 275, 223-231.
    • (2001) Gene , vol.275 , pp. 223-231
    • Takahashi, Y.1    Toh-E, A.2    Kikuchi, Y.3
  • 62
    • 33644761942 scopus 로고    scopus 로고
    • SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase II
    • Takahashi Y, Yong-Gonzalez V, Kikuchi Y, Strunnikov A (2006). SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase II. Genetics 172, 783-794.
    • (2006) Genetics , vol.172 , pp. 783-794
    • Takahashi, Y.1    Yong-Gonzalez, V.2    Kikuchi, Y.3    Strunnikov, A.4
  • 63
    • 84883213105 scopus 로고    scopus 로고
    • Physical and genetic interactions between Uls1 and the Slx5-Slx8 SUMO-targeted ubiquitin ligase
    • Tan W, Wang Z, Prelich G (2013). Physical and genetic interactions between Uls1 and the Slx5-Slx8 SUMO-targeted ubiquitin ligase. G3 (Bethesda) 3, 771-780.
    • (2013) G3 (Bethesda) , vol.3 , pp. 771-780
    • Tan, W.1    Wang, Z.2    Prelich, G.3
  • 65
    • 84865715286 scopus 로고    scopus 로고
    • Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress
    • Tkach JM et al. (2012). Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14, 966-976.
    • (2012) Nat Cell Biol , vol.14 , pp. 966-976
    • Tkach, J.M.1
  • 66
    • 55249096736 scopus 로고    scopus 로고
    • The fast-growing business of SUMO chains
    • Ulrich HD (2008). The fast-growing business of SUMO chains. Mol Cell 32, 301-305.
    • (2008) Mol Cell , vol.32 , pp. 301-305
    • Ulrich, H.D.1
  • 67
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich HD, Walden H (2010). Ubiquitin signalling in DNA replication and repair. Nat Rev Mol Cell Biol 11, 479-489.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 68
    • 36348977099 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolytic control of SUMO conjugates
    • Uzunova KK et al. (2007). Ubiquitin-dependent proteolytic control of SUMO conjugates. J Biol Chem 282, 34167-34175.
    • (2007) J Biol Chem , vol.282 , pp. 34167-34175
    • Uzunova, K.K.1
  • 69
    • 76449092386 scopus 로고    scopus 로고
    • SUMO chains: Polymeric signals
    • Vertegaal ACO (2010). SUMO chains: polymeric signals. Biochem Soc Trans 38, 46-49.
    • (2010) Biochem Soc Trans , vol.38 , pp. 46-49
    • Vertegaal, A.C.O.1
  • 70
    • 70849129868 scopus 로고    scopus 로고
    • SUMOylation and deSUMOylation at a glance
    • Wang Y, Dasso M (2009). SUMOylation and deSUMOylation at a glance. J Cell Sci 122, 4249-4252.
    • (2009) J Cell Sci , vol.122 , pp. 4249-4252
    • Wang, Y.1    Dasso, M.2
  • 71
    • 63049110916 scopus 로고    scopus 로고
    • Quality control of a transcriptional regulator by SUMO-targeted degradation
    • Wang Z, Prelich G (2009). Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol Cell Biol 29, 1694-1706.
    • (2009) Mol Cell Biol , vol.29 , pp. 1694-1706
    • Wang, Z.1    Prelich, G.2
  • 72
    • 33645222457 scopus 로고    scopus 로고
    • Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae
    • Wang Z, Jones GM, Prelich G (2006). Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae. Genetics 172, 1499-1509.
    • (2006) Genetics , vol.172 , pp. 1499-1509
    • Wang, Z.1    Jones, G.M.2    Prelich, G.3
  • 73
    • 65249173891 scopus 로고    scopus 로고
    • The multiple layers of ubiquitin-dependent cell cycle control
    • Wickliffe K, Williamson A, Jin L, Rape M (2009). The multiple layers of ubiquitin-dependent cell cycle control. Chem Rev 109, 1537-1548.
    • (2009) Chem Rev , vol.109 , pp. 1537-1548
    • Wickliffe, K.1    Williamson, A.2    Jin, L.3    Rape, M.4
  • 74
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie Y, Kerscher O, Kroetz MB, McConchie HF, Sung P, 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
    • 77951806546 scopus 로고    scopus 로고
    • SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor
    • Xie Y, Rubenstein EM, Matt T, Hochstrasser M (2010). SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor. Genes Dev 24, 893-903.
    • (2010) Genes Dev , vol.24 , pp. 893-903
    • Xie, Y.1    Rubenstein, E.M.2    Matt, T.3    Hochstrasser, M.4
  • 76
    • 84863870650 scopus 로고    scopus 로고
    • Regulation of gene expression by the ubiquitin-proteasome system
    • Yao T, Ndoja A (2012). Regulation of gene expression by the ubiquitin-proteasome system. Semin Cell Dev Biol 23, 523-529.
    • (2012) Semin Cell Dev Biol , vol.23 , pp. 523-529
    • Yao, T.1    Ndoja, A.2
  • 77
    • 32644477235 scopus 로고    scopus 로고
    • Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces cerevisiae
    • Zhang C, Roberts TM, Yang J, Desai R, Brown GW (2006). Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces cerevisiae. DNA Repair (Amst) 5, 336-346.
    • (2006) DNA Repair (Amst) , vol.5 , pp. 336-346
    • Zhang, C.1    Roberts, T.M.2    Yang, J.3    Desai, R.4    Brown, G.W.5
  • 78
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao X, Blobel G (2005). A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc Natl Acad Sci USA 102, 4777-4782.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2


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