메뉴 건너뛰기




Volumn 289, Issue 50, 2014, Pages 34838-34850

Regulation of USP28 deubiquitinating activity by SUMO conjugation

Author keywords

[No Author keywords available]

Indexed keywords

CHAINS; STABILIZATION;

EID: 84918508168     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.601849     Document Type: Article
Times cited : (28)

References (48)
  • 1
  • 2
    • 0032539909 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death
    • Ciechanover, A., and Schwartz, A. L. (1998) The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death. Proc. Natl. Acad. Sci. U.S.A. 95, 2727-2730
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2727-2730
    • Ciechanover, A.1    Schwartz, A.L.2
  • 4
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M. (2009) Origin and function of ubiquitin-like proteins. Nature 458, 422-429
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 5
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001) Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 6
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and deconjugation
    • Gareau, J. R., and Lima, C. D. (2010) The SUMO pathway: emerging mechanisms that shape specificity, conjugation and deconjugation. Nat. Rev. Mol. Cell Biol. 11, 861-871
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 7
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander, D., Clague, M. J., and Urbé, S. (2009) Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 10, 550-563
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 8
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu, F. E., Ventii, K. H., and Wilkinson, K. D. (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 78, 363-397
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 9
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J. W., Gu, W., Cohen, R. E., and Shi, Y. (2002) Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 10
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu, M., Li, P., Song, L., Jeffrey, P. D., Chenova, T. A., Wilkinson, K. D., Cohen, R. E., and Shi, Y. (2005) Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J. 24, 3747-3756
    • (2005) EMBO J , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5    Wilkinson, K.D.6    Cohen, R.E.7    Shi, Y.8
  • 12
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov, G. V., Walker, J. R., Xue, S., Finerty, P. J. Jr., Mackenzie, F., Newman, E. M., and Dhe-Paganon, S. (2006) Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J. Biol. Chem. 281, 38061-38070
    • (2006) J. Biol. Chem. , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6    Dhe-Paganon, S.7
  • 14
    • 79953314427 scopus 로고    scopus 로고
    • Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21
    • Ye, Y., Akutsu, M., Reyes-Turcu, F., Enchev, R. I., Wilkinson, K. D., and Komander, D. (2011) Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21. EMBO Rep. 12, 350-357
    • (2011) EMBO Rep. , vol.12 , pp. 350-357
    • Ye, Y.1    Akutsu, M.2    Reyes-Turcu, F.3    Enchev, R.I.4    Wilkinson, K.D.5    Komander, D.6
  • 17
    • 35848942129 scopus 로고    scopus 로고
    • Fbw7 and Usp28 regulate myc protein stability in response to DNA damage
    • Popov, N., Herold, S., Llamazares, M., Schülein, C., and Eilers, M. (2007) Fbw7 and Usp28 regulate myc protein stability in response to DNA damage. Cell Cycle 6, 2327-2331
    • (2007) Cell Cycle , vol.6 , pp. 2327-2331
    • Popov, N.1    Herold, S.2    Llamazares, M.3    Schülein, C.4    Eilers, M.5
  • 18
    • 84883458147 scopus 로고    scopus 로고
    • Deubiquitylating enzymes and DNA damage response pathways
    • Jacq, X., Kemp, M., Martin, N. M., and Jackson, S. P. (2013) Deubiquitylating enzymes and DNA damage response pathways. Cell Biochem. Biophys. 67, 25-43
    • (2013) Cell Biochem. Biophys. , vol.67 , pp. 25-43
    • Jacq, X.1    Kemp, M.2    Martin, N.M.3    Jackson, S.P.4
  • 19
    • 84885868036 scopus 로고    scopus 로고
    • The deubiquitinase USP28 stabilizes LSD1 and confers stem-cell-like traits to breast cancer cells
    • Wu, Y., Wang, Y., Yang, X. H., Kang, T., Zhao, Y., Wang, C., Evers, B. M., and Zhou, B. P. (2013) The deubiquitinase USP28 stabilizes LSD1 and confers stem-cell-like traits to breast cancer cells. Cell Rep. 5, 224-236
    • (2013) Cell Rep. , vol.5 , pp. 224-236
    • Wu, Y.1    Wang, Y.2    Yang, X.H.3    Kang, T.4    Zhao, Y.5    Wang, C.6    Evers, B.M.7    Zhou, B.P.8
  • 21
    • 84856604061 scopus 로고    scopus 로고
    • GSK-3β regulates cell growth, migration, and angiogenesis via Fbw7 and USP28-dependent degradation of HIF-1α
    • Flügel, D., Görlach, A., and Kietzmann, T. (2012) GSK-3β regulates cell growth, migration, and angiogenesis via Fbw7 and USP28-dependent degradation of HIF-1α. Blood 119, 1292-1301
    • (2012) Blood , vol.119 , pp. 1292-1301
    • Flügel, D.1    Görlach, A.2    Kietzmann, T.3
  • 25
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • Zhang, D., Zaugg, K., Mak, T. W., and Elledge, S. J. (2006) A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 126, 529-542
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 26
    • 84899880562 scopus 로고    scopus 로고
    • USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism
    • Knobel, P. A., Belotserkovskaya, R., Galanty, Y., Schmidt, C. K., Jackson, S. P., and Stracker, T. H. (2014) USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism. Mol. Cell. Biol. 34, 2062-2074
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 2062-2074
    • Knobel, P.A.1    Belotserkovskaya, R.2    Galanty, Y.3    Schmidt, C.K.4    Jackson, S.P.5    Stracker, T.H.6
  • 28
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro, J. M., Rodriguez, M. S., and Hay, R. T. (1998) SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell. 2, 233-239
    • (1998) Mol. Cell. , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 29
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 31
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • Sun, H., Leverson, J. D., and Hunter, T. (2007) Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 26, 4102-4112
    • (2007) EMBO J , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 32
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie, Y., Kerscher, O., Kroetz, M. B., McConchie, H. F., Sung, P., and Hochstrasser, M. (2007) The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J. Biol. Chem. 282, 34176-34184
    • (2007) J. Biol. Chem. , vol.282 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 35
    • 68149163523 scopus 로고    scopus 로고
    • The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition
    • Denuc, A., Bosch-Comas, A., Gonzàlez-Duarte, R., and Marfany, G. (2009) The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition. PLoS One 4, e5571
    • (2009) PLoS One , vol.4 , pp. e5571
    • Denuc, A.1    Bosch-Comas, A.2    Gonzàlez-Duarte, R.3    Marfany, G.4
  • 36
    • 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., and Melchior, F. (2008) Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol. Cell 30, 610-619
    • (2008) Mol. Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 37
    • 4143083663 scopus 로고    scopus 로고
    • A basis forSUMOprotease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Reverter, D., and Lima, C. D. (2004) A basis forSUMOprotease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure 12, 1519-1531
    • (2004) Structure , vol.12 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 44
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., and Harper, J. W. (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 45
    • 57649198342 scopus 로고    scopus 로고
    • SUMO binding determines substrate recognition and paralog-selective SUMO modification
    • Zhu, J., Zhu, S., Guzzo, C. M., Ellis, N. A., Sung, K. S., Choi, C. Y., and Matunis, M. (2008) SUMO binding determines substrate recognition and paralog-selective SUMO modification. J. Biol. Chem. 283, 29405-29415
    • (2008) J. Biol. Chem. , vol.283 , pp. 29405-29415
    • Zhu, J.1    Zhu, S.2    Guzzo, C.M.3    Ellis, N.A.4    Sung, K.S.5    Choi, C.Y.6    Matunis, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.