메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Targeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; LYSINE; SUMO PROTEIN; SUMO TARGETED UBIQUITIN LIGASE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; CARRIER PROTEIN; CDC48 PROTEIN; CELL CYCLE PROTEIN; MANNOSYLTRANSFERASE; NPL4 PROTEIN, S CEREVISIAE; NPL4 PROTEIN, S POMBE; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN; PMT3 PROTEIN, S POMBE; PROTEIN O-MANNOSYLTRANSFERASE; REPRESSOR PROTEIN; RFP1 PROTEIN, S POMBE; RFP2 PROTEIN, S POMBE; SACCHAROMYCES CEREVISIAE PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; SLX5 PROTEIN, S CEREVISIAE; SLX8 PROTEIN, S CEREVISIAE; SLX8 PROTEIN, S POMBE; SUMO 1 PROTEIN; TRANSCRIPTION FACTOR; UFD1 PROTEIN, S CEREVISIAE; UFD1 PROTEIN, S POMBE; VESICULAR TRANSPORT PROTEIN;

EID: 84946592741     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9827     Document Type: Article
Times cited : (28)

References (70)
  • 1
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho, A. & Melchior, F. Sumoylation: a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385 (2013).
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 2
    • 69849114721 scopus 로고    scopus 로고
    • SUMO chain formation is required for response to replication arrest in S pombe
    • Skilton, A., Ho, J. C., Mercer, B., Outwin, E. & Watts, F. Z. SUMO chain formation is required for response to replication arrest in S. pombe. PLoS ONE 4, e6750 (2009).
    • (2009) PLoS ONE , vol.4 , pp. e6750
    • Skilton, A.1    Ho, J.C.2    Mercer, B.3    Outwin, E.4    Watts, F.Z.5
  • 3
    • 37749023742 scopus 로고    scopus 로고
    • The role of Schizosaccharomyces pombe SUMO ligases in genome stability
    • Watts, F. Z. et al. The role of Schizosaccharomyces pombe SUMO ligases in genome stability. Biochem. Soc. Trans. 35, 1379-1384 (2007).
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1379-1384
    • Watts, F.Z.1
  • 4
    • 36348977099 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolytic control of SUMO conjugates
    • Uzunova, K. et al. Ubiquitin-dependent proteolytic control of SUMO conjugates. J. Biol. Chem. 282, 34167-34175 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 34167-34175
    • Uzunova, K.1
  • 5
    • 34648840192 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin ligases in genome stability
    • Prudden, J. et al. SUMO-targeted ubiquitin ligases in genome stability. EMBO J. 26, 4089-4101 (2007).
    • (2007) EMBO J. , vol.26 , pp. 4089-4101
    • Prudden, J.1
  • 6
    • 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. & Hunter, T. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 26, 4102-4112 (2007).
    • (2007) EMBO J. , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 7
    • 34547136728 scopus 로고    scopus 로고
    • Fission yeast Rnf4 homologs are required for DNA repair
    • Kosoy, A., Calonge, T. M., Outwin, E. A. & O'Connell, M. J. Fission yeast Rnf4 homologs are required for DNA repair. J. Biol. Chem. 282, 20388-20394 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 20388-20394
    • Kosoy, A.1    Calonge, T.M.2    Outwin, E.A.3    O'Connell, M.J.4
  • 8
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham, M. H. et al. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell Biol. 10, 538-546 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 538-546
    • Tatham, M.H.1
  • 9
    • 84896375470 scopus 로고    scopus 로고
    • SUMO chain-induced dimerization activates RNF4
    • Rojas-Fernandez, A. et al. SUMO chain-induced dimerization activates RNF4. Mol. Cell 53, 880-892 (2014).
    • (2014) Mol. Cell , vol.53 , pp. 880-892
    • Rojas-Fernandez, A.1
  • 10
    • 84861784690 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage
    • Yin, Y. et al. SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage. Genes Dev. 26, 1196-1208 (2012).
    • (2012) Genes Dev. , vol.26 , pp. 1196-1208
    • Yin, Y.1
  • 11
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • Lallemand-Breitenbach, V. et al. Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat. Cell Biol. 10, 547-555 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 547-555
    • Lallemand-Breitenbach, V.1
  • 12
    • 63049110916 scopus 로고    scopus 로고
    • Quality control of a transcriptional regulator by SUMO-targeted degradation
    • Wang, Z. & Prelich, G. Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol. Cell Biol. 29, 1694-1706 (2009).
    • (2009) Mol. Cell Biol. , vol.29 , pp. 1694-1706
    • Wang, Z.1    Prelich, G.2
  • 13
    • 77949378117 scopus 로고    scopus 로고
    • The SUMO protease SENP6 is essential for inner kinetochore assembly
    • Mukhopadhyay, D., Arnaoutov, A. & Dasso, M. The SUMO protease SENP6 is essential for inner kinetochore assembly. J. Cell Biol. 188, 681-692 (2010).
    • (2010) J. Cell Biol. , vol.188 , pp. 681-692
    • Mukhopadhyay, D.1    Arnaoutov, A.2    Dasso, M.3
  • 14
    • 84861765707 scopus 로고    scopus 로고
    • RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair
    • Galanty, Y., Belotserkovskaya, R., Coates, J. & Jackson, S. P. RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair. Genes Dev. 26, 1179-1195 (2012).
    • (2012) Genes Dev. , vol.26 , pp. 1179-1195
    • Galanty, Y.1    Belotserkovskaya, R.2    Coates, J.3    Jackson, S.P.4
  • 15
    • 84894292654 scopus 로고    scopus 로고
    • Pds5 prevents the PolySUMO-dependent separation of sister chromatids
    • D'Ambrosio, L. M. & Lavoie, B. D. Pds5 prevents the PolySUMO-dependent separation of sister chromatids. Curr. Biol. 24, 361-371 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 361-371
    • D'Ambrosio, L.M.1    Lavoie, B.D.2
  • 16
    • 84891803634 scopus 로고    scopus 로고
    • A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1
    • Westerbeck, J. W. et al. A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1. Mol. Biol. Cell 25, 1-16 (2014).
    • (2014) Mol. Biol. Cell , vol.25 , pp. 1-16
    • Westerbeck, J.W.1
  • 17
    • 84878985126 scopus 로고    scopus 로고
    • Centromere binding and a conserved role in chromosome stability for SUMO-dependent ubiquitin ligases
    • van de Pasch, L. A. et al. Centromere binding and a conserved role in chromosome stability for SUMO-dependent ubiquitin ligases. PLoS ONE 8, e65628 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e65628
    • Van De-Pasch, L.A.1
  • 18
    • 84870013890 scopus 로고    scopus 로고
    • STUbLs in chromatin and genome stability
    • Garza, R. & Pillus, L. STUbLs in chromatin and genome stability. Biopolymers 99, 146-154 (2013).
    • (2013) Biopolymers , vol.99 , pp. 146-154
    • Garza, R.1    Pillus, L.2
  • 19
    • 84892959701 scopus 로고    scopus 로고
    • Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response
    • Kohler, J. B., Jorgensen, M. L., Beinoraite, G., Thorsen, M. & Thon, G. Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response. PLoS ONE 8, e80442 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e80442
    • Kohler, J.B.1    Jorgensen, M.L.2    Beinoraite, G.3    Thorsen, M.4    Thon, G.5
  • 20
    • 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. et al. 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).
    • (2012) J. Biol. Chem. , vol.287 , pp. 29610-29619
    • Nie, M.1
  • 21
    • 84877585813 scopus 로고    scopus 로고
    • Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction
    • Bergink, S. et al. Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction. Nat. Cell Biol. 15, 526-532 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 526-532
    • Bergink, S.1
  • 22
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M. & Bremer, S. Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117-123 (2012).
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 23
    • 84899636473 scopus 로고    scopus 로고
    • Cdc48: A swiss army knife of cell biology
    • Baek, G. H. et al. Cdc48: a swiss army knife of cell biology. J. Amino Acids 2013, 183421 (2013).
    • (2013) J. Amino Acids , vol.2013 , pp. 183421
    • Baek, G.H.1
  • 24
    • 8544273758 scopus 로고    scopus 로고
    • Global analysis of protein sumoylation in Saccharomyces cerevisiae
    • Wohlschlegel, J. A., Johnson, E. S., Reed, S. I. & Yates, 3rd J. R. Global analysis of protein sumoylation in Saccharomyces cerevisiae. J. Biol. Chem. 279, 45662-45668 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 45662-45668
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates, J.R.4
  • 25
    • 14244260623 scopus 로고    scopus 로고
    • Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae
    • Hannich, J. T. et al. Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J. Biol. Chem. 280, 4102-4110 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 4102-4110
    • Hannich, J.T.1
  • 26
    • 67649173012 scopus 로고    scopus 로고
    • System-wide changes to SUMO modifications in response to heat shock
    • Golebiowski, F. et al. System-wide changes to SUMO modifications in response to heat shock. Sci. Signal. 2, ra24 (2009).
    • (2009) Sci. Signal. , vol.2 , pp. ra24
    • Golebiowski, F.1
  • 27
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic, I. et al. Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell 39, 641-652 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1
  • 28
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham, M. H., Matic, I., Mann, M. & Hay, R. T. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci. Signal. 4, rs4 (2011).
    • (2011) Sci. Signal. , vol.4 , pp. rs4
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 29
    • 84899759007 scopus 로고    scopus 로고
    • Proteome-wide identification of SUMO2 modification sites
    • Tammsalu, T. et al. Proteome-wide identification of SUMO2 modification sites. Sci. Signal. 7, rs2 (2014).
    • (2014) Sci. Signal. , vol.7 , pp. rs2
    • Tammsalu, T.1
  • 30
    • 84925775745 scopus 로고    scopus 로고
    • Uncovering global SUMOylation signaling networks in a site-specific manner
    • Hendriks, I. A. et al. Uncovering global SUMOylation signaling networks in a site-specific manner. Nat. Struct. Mol. Biol. 21, 927-936 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 927-936
    • Hendriks, I.A.1
  • 31
    • 84906695084 scopus 로고    scopus 로고
    • Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli
    • Impens, F., Radoshevich, L., Cossart, P. & Ribet, D. Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. Proc. Natl Acad. Sci. USA 111, 12432-12437 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 12432-12437
    • Impens, F.1    Radoshevich, L.2    Cossart, P.3    Ribet, D.4
  • 32
    • 33645783699 scopus 로고    scopus 로고
    • Improved identification of SUMO attachment sites using C-terminal SUMO mutants and tailored protease digestion strategies
    • Wohlschlegel, J. A., Johnson, E. S., Reed, S. I. & Yates, 3rd J. R. Improved identification of SUMO attachment sites using C-terminal SUMO mutants and tailored protease digestion strategies. J. Proteome Res. 5, 761-770 (2006).
    • (2006) J. Proteome Res. , vol.5 , pp. 761-770
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates, J.R.4
  • 33
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 7, 952-958 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 34
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G., Paige, J. S. & Jaffrey, S. R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 28, 868-873 (2010).
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 35
    • 84868028972 scopus 로고    scopus 로고
    • Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells
    • Marguerat, S. et al. Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells. Cell 151, 671-683 (2012).
    • (2012) Cell , vol.151 , pp. 671-683
    • Marguerat, S.1
  • 36
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 37
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M. S., Dargemont, C. & Hay, R. T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276, 12654-12659 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 38
    • 74249093169 scopus 로고    scopus 로고
    • Phosphorylation of H2A by Bub1 prevents chromosomal instability through localizing shugoshin
    • Kawashima, S. A., Yamagishi, Y., Honda, T., Ishiguro, K. & Watanabe, Y. Phosphorylation of H2A by Bub1 prevents chromosomal instability through localizing shugoshin. Science 327, 172-177 (2010).
    • (2010) Science , vol.327 , pp. 172-177
    • Kawashima, S.A.1    Yamagishi, Y.2    Honda, T.3    Ishiguro, K.4    Watanabe, Y.5
  • 39
    • 84869094439 scopus 로고    scopus 로고
    • Structure of a topoisomerase IIDNA-nucleotide complex reveals a new control mechanism for ATPase activity
    • Schmidt, B. H., Osheroff, N. & Berger, J. M. Structure of a topoisomerase IIDNA-nucleotide complex reveals a new control mechanism for ATPase activity. Nat. Struct. Mol. Biol. 19, 1147-1154 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1147-1154
    • Schmidt, B.H.1    Osheroff, N.2    Berger, J.M.3
  • 40
    • 0036291014 scopus 로고    scopus 로고
    • The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II
    • Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N. & Elledge, S. J. The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell 9, 1169-1182 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 41
    • 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. et al. 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).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1
  • 42
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye, I. & Jentsch, S. Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 151, 807-820 (2012).
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 43
    • 84858305675 scopus 로고    scopus 로고
    • PomBase: A comprehensive online resource for fission yeast
    • Wood, V. et al. PomBase: a comprehensive online resource for fission yeast. Nucleic Acids Res. 40, D695-D699 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. D695-D699
    • Wood, V.1
  • 44
    • 15944414509 scopus 로고    scopus 로고
    • A proteomic strategy for gaining insights into protein sumoylation in yeast
    • Denison, C. et al. A proteomic strategy for gaining insights into protein sumoylation in yeast. Mol. Cell Proteomics 4, 246-254 (2005).
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 246-254
    • Denison, C.1
  • 45
    • 84884638785 scopus 로고    scopus 로고
    • Distinct SUMO ligases cooperate with Esc2 and Slx5 to suppress duplication-mediated genome rearrangements
    • Albuquerque, C. P. et al. Distinct SUMO ligases cooperate with Esc2 and Slx5 to suppress duplication-mediated genome rearrangements. PLoS Genet. 9, e1003670 (2013).
    • (2013) PLoS Genet. , vol.9 , pp. e1003670
    • Albuquerque, C.P.1
  • 46
    • 4744360999 scopus 로고    scopus 로고
    • A proteome-wide approach identifies sumoylated substrate proteins in yeast
    • Panse, V. G., Hardeland, U., Werner, T., Kuster, B. & Hurt, E. A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem. 279, 41346-41351 (2004).
    • (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
  • 47
    • 84862262073 scopus 로고    scopus 로고
    • YeastMine-an integrated data warehouse for Saccharomyces cerevisiae data as a multipurpose tool-kit
    • Balakrishnan, R. et al. YeastMine-an integrated data warehouse for Saccharomyces cerevisiae data as a multipurpose tool-kit. Database (Oxford) 2012, bar062 (2012).
    • (2012) Database (Oxford) , vol.2012 , pp. bar062
    • Balakrishnan, R.1
  • 48
    • 79952840074 scopus 로고    scopus 로고
    • Mis17 is a regulatory module of the Mis6-Mal2-Sim4 centromere complex that is required for the recruitment of CenH3/CENP-A in fission yeast
    • Shiroiwa, Y. et al. Mis17 is a regulatory module of the Mis6-Mal2-Sim4 centromere complex that is required for the recruitment of CenH3/CENP-A in fission yeast. PLoS ONE 6, e17761 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e17761
    • Shiroiwa, Y.1
  • 49
    • 27844498429 scopus 로고    scopus 로고
    • Molecular analysis of kinetochore architecture in fission yeast
    • Liu, X., McLeod, I., Anderson, S., Yates, 3rd J. R. & He, X. Molecular analysis of kinetochore architecture in fission yeast. EMBO J. 24, 2919-2930 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2919-2930
    • Liu, X.1    McLeod, I.2    Anderson, S.3    Yates, J.R.4    He, X.5
  • 50
    • 27844557066 scopus 로고    scopus 로고
    • The DASH complex and Klp5/Klp6 kinesin coordinate bipolar chromosome attachment in fission yeast
    • Sanchez-Perez, I. et al. The DASH complex and Klp5/Klp6 kinesin coordinate bipolar chromosome attachment in fission yeast. EMBO J. 24, 2931-2943 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2931-2943
    • Sanchez-Perez, I.1
  • 51
    • 84875472600 scopus 로고    scopus 로고
    • End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1
    • Lescasse, R., Pobiega, S., Callebaut, I. & Marcand, S. End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1. EMBO J. 32, 805-815 (2013).
    • (2013) EMBO J. , vol.32 , pp. 805-815
    • Lescasse, R.1    Pobiega, S.2    Callebaut, I.3    Marcand, S.4
  • 52
    • 70449850077 scopus 로고    scopus 로고
    • Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to ensure chromosomal bouquet formation
    • Chikashige, Y. et al. Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to ensure chromosomal bouquet formation. J. Cell Biol. 187, 413-427 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 413-427
    • Chikashige, Y.1
  • 53
    • 84867890079 scopus 로고    scopus 로고
    • Telomere-nuclear envelope dissociation promoted by Rap1 phosphorylation ensures faithful chromosome segregation
    • Fujita, I. et al. Telomere-nuclear envelope dissociation promoted by Rap1 phosphorylation ensures faithful chromosome segregation. Curr. Biol. 22, 1932-1937 (2012).
    • (2012) Curr. Biol. , vol.22 , pp. 1932-1937
    • Fujita, I.1
  • 54
    • 84860162529 scopus 로고    scopus 로고
    • Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina
    • Gonzalez, Y., Saito, A. & Sazer, S. Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina. Nucleus 3, 60-76 (2012).
    • (2012) Nucleus , vol.3 , pp. 60-76
    • Gonzalez, Y.1    Saito, A.2    Sazer, S.3
  • 55
    • 84866109279 scopus 로고    scopus 로고
    • Structure and function in the budding yeast nucleus
    • Taddei, A. & Gasser, S. M. Structure and function in the budding yeast nucleus. Genetics 192, 107-129 (2012).
    • (2012) Genetics , vol.192 , pp. 107-129
    • Taddei, A.1    Gasser, S.M.2
  • 56
    • 84890837804 scopus 로고    scopus 로고
    • The shelterin protein POT-1 anchors Caenorhabditis elegans telomeres through SUN-1 at the nuclear periphery
    • Ferreira, H. C., Towbin, B. D., Jegou, T. & Gasser, S. M. The shelterin protein POT-1 anchors Caenorhabditis elegans telomeres through SUN-1 at the nuclear periphery. J. Cell Biol. 203, 727-735 (2013).
    • (2013) J. Cell Biol. , vol.203 , pp. 727-735
    • Ferreira, H.C.1    Towbin, B.D.2    Jegou, T.3    Gasser, S.M.4
  • 57
    • 84878636197 scopus 로고    scopus 로고
    • A global S cerevisiae small ubiquitinrelated modifier (SUMO) system interactome
    • Srikumar, T., Lewicki, M. C. & Raught, B. A global S. cerevisiae small ubiquitinrelated modifier (SUMO) system interactome. Mol. Syst. Biol. 9, 668 (2013).
    • (2013) Mol. Syst. Biol. , vol.9 , pp. 668
    • Srikumar, T.1    Lewicki, M.C.2    Raught, B.3
  • 58
    • 84876313595 scopus 로고    scopus 로고
    • Global analysis of SUMO chain function reveals multiple roles in chromatin regulation
    • Srikumar, T. et al. Global analysis of SUMO chain function reveals multiple roles in chromatin regulation. J. Cell Biol. 201, 145-163 (2013).
    • (2013) J. Cell Biol. , vol.201 , pp. 145-163
    • Srikumar, T.1
  • 59
    • 38949174194 scopus 로고    scopus 로고
    • Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2
    • Darst, R. P., Garcia, S. N., Koch, M. R. & Pillus, L. Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2. Mol. Cell Biol. 28, 1361-1372 (2008).
    • (2008) Mol. Cell Biol. , vol.28 , pp. 1361-1372
    • Darst, R.P.1    Garcia, S.N.2    Koch, M.R.3    Pillus, L.4
  • 60
    • 84866148011 scopus 로고    scopus 로고
    • SUMOylation of the alpha-kleisin subunit of cohesin is required for DNA damage-induced cohesion
    • McAleenan, A. et al. SUMOylation of the alpha-kleisin subunit of cohesin is required for DNA damage-induced cohesion. Curr. Biol. 22, 1564-1575 (2012).
    • (2012) Curr. Biol. , vol.22 , pp. 1564-1575
    • McAleenan, A.1
  • 61
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R. T. SUMO: a history of modification. Mol. Cell 18, 1-12 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 62
    • 84899052640 scopus 로고    scopus 로고
    • SUMOylation regulates telomere length by targeting the shelterin subunit Tpz1(Tpp1) to modulate shelterin-Stn1 interaction in fission yeast
    • Miyagawa, K. et al. SUMOylation regulates telomere length by targeting the shelterin subunit Tpz1(Tpp1) to modulate shelterin-Stn1 interaction in fission yeast. Proc. Natl Acad. Sci. USA 111, 5950-5955 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 5950-5955
    • Miyagawa, K.1
  • 63
    • 84905409125 scopus 로고    scopus 로고
    • Tpz1TPP1 SUMOylation reveals evolutionary conservation of SUMO-dependent Stn1 telomere association
    • Garg, M. et al. Tpz1TPP1 SUMOylation reveals evolutionary conservation of SUMO-dependent Stn1 telomere association. EMBO Rep. 15, 871-877 (2014).
    • (2014) EMBO Rep. , vol.15 , pp. 871-877
    • Garg, M.1
  • 64
    • 84900322882 scopus 로고    scopus 로고
    • Rapid, efficient and precise allele replacement in the fission yeast Schizosaccharomyces pombe
    • Gao, J. et al. Rapid, efficient and precise allele replacement in the fission yeast Schizosaccharomyces pombe. Curr. Genet. 60, 109-119 (2014).
    • (2014) Curr. Genet. , vol.60 , pp. 109-119
    • Gao, J.1
  • 65
    • 84940540249 scopus 로고    scopus 로고
    • Proteome-wide identification of SUMO modification sites by mass spectrometry
    • Tammsalu, T. et al. Proteome-wide identification of SUMO modification sites by mass spectrometry. Nat. Protoc. 10, 1374-1388 (2015).
    • (2015) Nat. Protoc. , vol.10 , pp. 1374-1388
    • Tammsalu, T.1
  • 66
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski, J. R., Zougman, A. & Mann, M. Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J. Proteome Res. 8, 5674-5678 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 67
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M. & Ishihama, Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 68
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox, J. et al. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol. Cell Proteomics 13, 2513-2526 (2014).
    • (2014) Mol. Cell Proteomics , vol.13 , pp. 2513-2526
    • Cox, J.1
  • 69
    • 84888872901 scopus 로고    scopus 로고
    • PLogo: A probabilistic approach to visualizing sequence motifs
    • O'Shea, J. P. et al. pLogo: a probabilistic approach to visualizing sequence motifs. Nat. Methods 10, 1211-1212 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 1211-1212
    • O'Shea, J.P.1
  • 70
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292, 195-202 (1999).
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.