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Volumn 1863, Issue 1, 2016, Pages 139-147

Evaluation of the activity and substrate specificity of the human SENP family of SUMO proteases

Author keywords

PolySUMO chains; RanGAP1; SENPs; Sentrin SUMO specific proteases; SUMO; SUMO precursors

Indexed keywords

SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; SUMO PROTEIN; SUMO SPECIFIC PROTEASE; SUMO SPECIFIC PROTEASE 1; SUMO SPECIFIC PROTEASE 2; SUMO SPECIFIC PROTEASE 3; SUMO SPECIFIC PROTEASE 5; SUMO SPECIFIC PROTEASE 6; SUMO SPECIFIC PROTEASE 7; UNCLASSIFIED DRUG; PROTEINASE; RECOMBINANT PROTEIN;

EID: 84946593598     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.10.020     Document Type: Article
Times cited : (31)

References (58)
  • 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. 2013, 82:357-385. 10.1146/annurev-biochem-061909-093311.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 3
    • 0032433265 scopus 로고    scopus 로고
    • Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes
    • Chen A., Mannen H., Li S.S. Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes. Biochem. Mol. Biol. Int. 1998, 46:1161-1174.
    • (1998) Biochem. Mol. Biol. Int. , vol.46 , pp. 1161-1174
    • Chen, A.1    Mannen, H.2    Li, S.S.3
  • 4
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin-like proteins
    • Kamitani T., Kito K., Nguyen H.P., Fukuda-Kamitani T., Yeh E.T. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 1998, 273:11349-11353. 10.1074/jbc.273.18.11349.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 5
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis M.J., Coutavas E., Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 1996, 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 6
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
    • Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M., Botting C.H., Naismith J.H., Hay R.T. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J. Biol. Chem. 2001, 276:35368-35374. 10.1074/jbc.M104214200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35368-35374
    • Tatham, M.H.1    Jaffray, E.2    Vaughan, O.A.3    Desterro, J.M.4    Botting, C.H.5    Naismith, J.H.6    Hay, R.T.7
  • 7
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh H., Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 2000, 275:6252-6258. 10.1074/jbc.275.9.6252.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 8
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
    • Desterro J.M., Rodriguez M.S., Kemp G.D., Hay R.T. Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J. Biol. Chem. 1999, 274:10618-10624. 10.1074/jbc.274.15.10618.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10618-10624
    • Desterro, J.M.1    Rodriguez, M.S.2    Kemp, G.D.3    Hay, R.T.4
  • 10
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson E.S., Gupta A.A. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 2001, 106:735-744. 10.1016/S0092-8674(01)00491-3.
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 11
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau J.R., Lima C.D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 2010, 11:861-871. 10.1038/nrm3011.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 12
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • Matic I., van Hagen M., Schimmel J., Macek B., Ogg S.C., Tatham M.H., Hay R.T., Lamond A.I., Mann M., Vertegaal A.C. In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol. Cell. Proteomics 2008, 7:132-144. 10.1074/mcp.M700173-MCP200.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 132-144
    • Matic, I.1    van Hagen, M.2    Schimmel, J.3    Macek, B.4    Ogg, S.C.5    Tatham, M.H.6    Hay, R.T.7    Lamond, A.I.8    Mann, M.9    Vertegaal, A.C.10
  • 13
    • 58149347461 scopus 로고    scopus 로고
    • DeSUMOylating enzymes-SENPs
    • Drag M., Salvesen G.S. DeSUMOylating enzymes-SENPs. IUBMB Life 2008, 60:734-742. 10.1002/iub.113.
    • (2008) IUBMB Life , vol.60 , pp. 734-742
    • Drag, M.1    Salvesen, G.S.2
  • 14
    • 34548483908 scopus 로고    scopus 로고
    • SUMO-specific proteases: a twist in the tail
    • Hay R.T. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 2007, 17:370-376. 10.1016/j.tcb.2007.08.002.
    • (2007) Trends Cell Biol. , vol.17 , pp. 370-376
    • Hay, R.T.1
  • 15
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: the SUMO proteases
    • Mukhopadhyay D., Dasso M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 2007, 32:286-295. 10.1016/j.tibs.2007.05.002.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 16
    • 0346422441 scopus 로고    scopus 로고
    • Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1
    • Bailey D., O'Hare P. Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1. J. Biol. Chem. 2004, 279:692-703. 10.1074/jbc.M306195200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 692-703
    • Bailey, D.1    O'Hare, P.2
  • 17
    • 84055176117 scopus 로고    scopus 로고
    • The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex
    • Goeres J., Chan P.K., Mukhopadhyay D., Zhang H., Raught B., Matunis M.J. The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex. Mol. Biol. Cell 2011, 22:4868-4882. 10.1091/mbc.E10-12-0953.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4868-4882
    • Goeres, J.1    Chan, P.K.2    Mukhopadhyay, D.3    Zhang, H.4    Raught, B.5    Matunis, M.J.6
  • 18
    • 0037205460 scopus 로고    scopus 로고
    • Association of the human SUMO-1 protease SENP2 with the nuclear pore
    • Hang J., Dasso M. Association of the human SUMO-1 protease SENP2 with the nuclear pore. J. Biol. Chem. 2002, 277:19961-19966. 10.1074/jbc.M201799200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 19
    • 33745049415 scopus 로고    scopus 로고
    • The SUMO-specific protease SENP5 is required for cell division
    • Di Bacco A., Ouyang J., Lee H.Y., Catic A., Ploegh H., Gill G. The SUMO-specific protease SENP5 is required for cell division. Mol. Cell. Biol. 2006, 26:4489-4498. 10.1128/MCB.02301-05.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4489-4498
    • Di Bacco, A.1    Ouyang, J.2    Lee, H.Y.3    Catic, A.4    Ploegh, H.5    Gill, G.6
  • 20
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • Gong L., Yeh E.T. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J. Biol. Chem. 2006, 281:15869-15877. 10.1074/jbc.M511658200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.2
  • 22
    • 67650911884 scopus 로고    scopus 로고
    • Characterization of SENP7, a SUMO-2/3-specific isopeptidase
    • Shen L.N., Geoffroy M.C., Jaffray E.G., Hay R.T. Characterization of SENP7, a SUMO-2/3-specific isopeptidase. Biochem. J. 2009, 421:223-230. 10.1042/BJ20090246.
    • (2009) Biochem. J. , vol.421 , pp. 223-230
    • Shen, L.N.1    Geoffroy, M.C.2    Jaffray, E.G.3    Hay, R.T.4
  • 23
    • 84862798314 scopus 로고    scopus 로고
    • DeSUMOylating isopeptidase: a second class of SUMO protease
    • Shin E.J., Shin H.M., Nam E., Kim W.S., Kim J.H., Oh B.H., Yun Y. DeSUMOylating isopeptidase: a second class of SUMO protease. EMBO Rep. 2012, 13:339-346. 10.1038/embor.2012.3.
    • (2012) EMBO Rep. , vol.13 , pp. 339-346
    • Shin, E.J.1    Shin, H.M.2    Nam, E.3    Kim, W.S.4    Kim, J.H.5    Oh, B.H.6    Yun, Y.7
  • 25
    • 84878597289 scopus 로고    scopus 로고
    • SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia
    • Guo C., Hildick K.L., Luo J., Dearden L., Wilkinson K.A., Henley J.M. SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia. EMBO J. 2013, 32:1514-1528. 10.1038/emboj.2013.65.
    • (2013) EMBO J. , vol.32 , pp. 1514-1528
    • Guo, C.1    Hildick, K.L.2    Luo, J.3    Dearden, L.4    Wilkinson, K.A.5    Henley, J.M.6
  • 26
    • 78651084831 scopus 로고    scopus 로고
    • The SUMO protease SENP6 is a direct regulator of PML nuclear bodies
    • Hattersley N., Shen L., Jaffray E.G., Hay R.T. The SUMO protease SENP6 is a direct regulator of PML nuclear bodies. Mol. Biol. Cell 2011, 22:78-90. 10.1091/mbc.E10-06-0504.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 78-90
    • Hattersley, N.1    Shen, L.2    Jaffray, E.G.3    Hay, R.T.4
  • 27
    • 77950907937 scopus 로고    scopus 로고
    • SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development
    • Kang X., Qi Y., Zuo Y., Wang Q., Zou Y., Schwartz R.J., Cheng J., Yeh E.T. SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development. Mol. Cell 2010, 38:191-201. 10.1016/j.molcel.2010.03.005.
    • (2010) Mol. Cell , vol.38 , pp. 191-201
    • Kang, X.1    Qi, Y.2    Zuo, Y.3    Wang, Q.4    Zou, Y.5    Schwartz, R.J.6    Cheng, J.7    Yeh, E.T.8
  • 28
    • 79960468868 scopus 로고    scopus 로고
    • NF-kappaB induction of the SUMO protease SENP2: a negative feedback loop to attenuate cell survival response to genotoxic stress
    • Lee M.H., Mabb A.M., Gill G.B., Yeh E.T., Miyamoto S. NF-kappaB induction of the SUMO protease SENP2: a negative feedback loop to attenuate cell survival response to genotoxic stress. Mol. Cell 2011, 43:180-191. 10.1016/j.molcel.2011.06.017.
    • (2011) Mol. Cell , vol.43 , pp. 180-191
    • Lee, M.H.1    Mabb, A.M.2    Gill, G.B.3    Yeh, E.T.4    Miyamoto, S.5
  • 29
    • 84878616564 scopus 로고    scopus 로고
    • Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo
    • Sharma P., Yamada S., Lualdi M., Dasso M., Kuehn M.R. Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo. Cell Rep. 2013, 3:1640-1650. 10.1016/j.celrep.2013.04.016.
    • (2013) Cell Rep. , vol.3 , pp. 1640-1650
    • Sharma, P.1    Yamada, S.2    Lualdi, M.3    Dasso, M.4    Kuehn, M.R.5
  • 30
    • 34548848530 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs
    • Mikolajczyk J., Drag M., Bekes M., Cao J.T., Ronai Z., Salvesen G.S. Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs. J. Biol. Chem. 2007, 282:26217-26224. 10.1074/jbc.M702444200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26217-26224
    • Mikolajczyk, J.1    Drag, M.2    Bekes, M.3    Cao, J.T.4    Ronai, Z.5    Salvesen, G.S.6
  • 31
    • 14844299866 scopus 로고    scopus 로고
    • Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
    • Xu Z., Au S.W. Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. Biochem. J. 2005, 386:325-330. 10.1042/BJ20041210.
    • (2005) Biochem. J. , vol.386 , pp. 325-330
    • Xu, Z.1    Au, S.W.2
  • 32
    • 0036724599 scopus 로고    scopus 로고
    • Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
    • Zhang H., Saitoh H., Matunis M.J. Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol. Cell. Biol. 2002, 22:6498-6508. 10.1128/MCB.22.18.6498-6508.2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 33
    • 57649138450 scopus 로고    scopus 로고
    • Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7
    • Lima C.D., Reverter D. Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7. J. Biol. Chem. 2008, 283:32045-32055. 10.1074/jbc.M805655200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32045-32055
    • Lima, C.D.1    Reverter, D.2
  • 34
    • 4143083663 scopus 로고    scopus 로고
    • A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Reverter D., Lima C.D. A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure 2004, 12:1519-1531. 10.1016/j.str.2004.05.023.
    • (2004) Structure , vol.12 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 35
    • 33845370047 scopus 로고    scopus 로고
    • Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
    • Reverter D., Lima C.D. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nat. Struct. Mol. Biol. 2006, 13:1060-1068. 10.1038/nsmb1168.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1060-1068
    • Reverter, D.1    Lima, C.D.2
  • 37
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem. J. 2006, 397:279-288. 10.1042/BJ20052030.
    • (2006) Biochem. J. , vol.397 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 39
    • 58149195377 scopus 로고    scopus 로고
    • Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases
    • Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A., Wilkinson K.D., Dasso M. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases. J. Cell Biol. 2008, 183:589-595. 10.1083/jcb.200807185.
    • (2008) J. Cell Biol. , vol.183 , pp. 589-595
    • Yun, C.1    Wang, Y.2    Mukhopadhyay, D.3    Backlund, P.4    Kolli, N.5    Yergey, A.6    Wilkinson, K.D.7    Dasso, M.8
  • 42
    • 0037128207 scopus 로고    scopus 로고
    • SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles
    • Joseph J., Tan S.H., Karpova T.S., McNally J.G., Dasso M. SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. J. Cell Biol. 2002, 156:595-602. 10.1083/jcb.200110109.
    • (2002) J. Cell Biol. , vol.156 , pp. 595-602
    • Joseph, J.1    Tan, S.H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 43
    • 47249159844 scopus 로고    scopus 로고
    • Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor
    • Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E., Warscheid B., Sa-Miranda C., Azevedo J.E. Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor. J. Biol. Chem. 2008, 283:14190-14197. 10.1074/jbc.M800402200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14190-14197
    • Grou, C.P.1    Carvalho, A.F.2    Pinto, M.P.3    Wiese, S.4    Piechura, H.5    Meyer, H.E.6    Warscheid, B.7    Sa-Miranda, C.8    Azevedo, J.E.9
  • 44
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky A., Ovaa H., Kolli N., Gan-Erdene T., Wilkinson K.D., Ploegh H.L., Kessler B.M. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 2002, 9:1149-1159. 10.1016/S1074-5521(02)00248-X.
    • (2002) Chem. Biol. , vol.9 , pp. 1149-1159
    • Borodovsky, A.1    Ovaa, H.2    Kolli, N.3    Gan-Erdene, T.4    Wilkinson, K.D.5    Ploegh, H.L.6    Kessler, B.M.7
  • 45
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25
    • Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol. Cell 2008, 30:610-619. 10.1016/j.molcel.2008.03.021.
    • (2008) Mol. Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 46
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler A., Gast A., Seeler J.S., Dejean A., Melchior F. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 2002, 108:109-120. 10.1016/S0092-8674(01)00633-X.
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 47
    • 59249102963 scopus 로고    scopus 로고
    • Performing in vitro sumoylation reactions using recombinant enzymes
    • Werner A., Moutty M.C., Moller U., Melchior F. Performing in vitro sumoylation reactions using recombinant enzymes. Methods Mol. Biol. 2009, 497:187-199. 10.1007/978-1-59745-566-4_12.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 187-199
    • Werner, A.1    Moutty, M.C.2    Moller, U.3    Melchior, F.4
  • 48
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang X.D., Goeres J., Zhang H., Yen T.J., Porter A.C., Matunis M.J. SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol. Cell 2008, 29:729-741. 10.1016/j.molcel.2008.01.013.
    • (2008) Mol. Cell , vol.29 , pp. 729-741
    • Zhang, X.D.1    Goeres, J.2    Zhang, H.3    Yen, T.J.4    Porter, A.C.5    Matunis, M.J.6
  • 49
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1997, 88:97-107. 10.1016/S0092-8674(00)81862-0.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 50
    • 33644865231 scopus 로고    scopus 로고
    • Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1
    • Takeda E., Hieda M., Katahira J., Yoneda Y. Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1. Cell Struct. Funct. 2005, 30:69-80. 10.1247/csf.30.69.
    • (2005) Cell Struct. Funct. , vol.30 , pp. 69-80
    • Takeda, E.1    Hieda, M.2    Katahira, J.3    Yoneda, Y.4
  • 51
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O. SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep. 2007, 8:550-555. 10.1038/sj.embor.7400980.
    • (2007) EMBO Rep. , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 52
    • 20344379921 scopus 로고    scopus 로고
    • Mutation of SENP1/SuPr-2 reveals an essential role for desumoylation in mouse development
    • Yamaguchi T., Sharma P., Athanasiou M., Kumar A., Yamada S., Kuehn M.R. Mutation of SENP1/SuPr-2 reveals an essential role for desumoylation in mouse development. Mol. Cell. Biol. 2005, 25:5171-5182. 10.1128/MCB.25.12.5171-5182.2005.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5171-5182
    • Yamaguchi, T.1    Sharma, P.2    Athanasiou, M.3    Kumar, A.4    Yamada, S.5    Kuehn, M.R.6
  • 53
    • 79953183354 scopus 로고    scopus 로고
    • The dynamics and mechanism of SUMO chain deconjugation by SUMO-specific proteases
    • Bekes M., Prudden J., Srikumar T., Raught B., Boddy M.N., Salvesen G.S. The dynamics and mechanism of SUMO chain deconjugation by SUMO-specific proteases. J. Biol. Chem. 2011, 286:10238-10247. 10.1074/jbc.M110.205153.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10238-10247
    • Bekes, M.1    Prudden, J.2    Srikumar, T.3    Raught, B.4    Boddy, M.N.5    Salvesen, G.S.6
  • 54
    • 76449092386 scopus 로고    scopus 로고
    • SUMO chains: polymeric signals
    • Vertegaal A.C. SUMO chains: polymeric signals. Biochem. Soc. Trans. 2010, 38:46-49. 10.1042/BST0380046.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 46-49
    • Vertegaal, A.C.1
  • 55
    • 0033760171 scopus 로고    scopus 로고
    • A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase
    • Nishida T., Tanaka H., Yasuda H. A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. Eur. J. Biochem. 2000, 267:6423-6427. 10.1046/j.1432-1327.2000.01729.x.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6423-6427
    • Nishida, T.1    Tanaka, H.2    Yasuda, H.3
  • 56
    • 14244260623 scopus 로고    scopus 로고
    • Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae
    • Hannich J.T., Lewis A., Kroetz M.B., Li S.J., Heide H., Emili A., Hochstrasser M. Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J. Biol. Chem. 2005, 280:4102-4110. 10.1074/jbc.M413209200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4102-4110
    • Hannich, J.T.1    Lewis, A.2    Kroetz, M.B.3    Li, S.J.4    Heide, H.5    Emili, A.6    Hochstrasser, M.7
  • 57
    • 33744940842 scopus 로고    scopus 로고
    • Specification of SUMO1- and SUMO2-interacting motifs
    • Hecker C.M., Rabiller M., Haglund K., Bayer P., Dikic I. Specification of SUMO1- and SUMO2-interacting motifs. J. Biol. Chem. 2006, 281:16117-16127. 10.1074/jbc.M512757200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16117-16127
    • Hecker, C.M.1    Rabiller, M.2    Haglund, K.3    Bayer, P.4    Dikic, I.5


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