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Volumn 433, Issue 4, 2013, Pages 390-395

An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

Author keywords

Proteasomal degradation; SIAH degron; SIAH1 ligase; USP19

Indexed keywords

SEVEN IN ABSENTIA HOMOLOG 1; SEVEN IN ABSENTIA HOMOLOG 2; UBIQUITIN; UBIQUITIN SPECIFIC PROTEASE 19; UNCLASSIFIED DRUG;

EID: 84876466143     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.02.094     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart C.M. Back to the future with ubiquitin. Cell 2004, 116:181-190.
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 2
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D., Clague M.J., Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 2009, 10:550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 4
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 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
  • 5
    • 50949126350 scopus 로고    scopus 로고
    • Protein partners of deubiquitinating enzymes
    • Ventii K.H., Wilkinson K.D. Protein partners of deubiquitinating enzymes. Biochem. J. 2008, 414:161-175.
    • (2008) Biochem. J. , vol.414 , pp. 161-175
    • Ventii, K.H.1    Wilkinson, K.D.2
  • 6
    • 69649103904 scopus 로고    scopus 로고
    • DUBs at a glance
    • Wilkinson K.D. DUBs at a glance. J. Cell Sci. 2009, 122:2325-2329.
    • (2009) J. Cell Sci. , vol.122 , pp. 2325-2329
    • Wilkinson, K.D.1
  • 7
    • 84863449135 scopus 로고    scopus 로고
    • Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes
    • Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., et al. Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes. ChemBioChem 2012, 13:1416-1420.
    • (2012) ChemBioChem , vol.13 , pp. 1416-1420
    • Iphofer, A.1    Kummer, A.2    Nimtz, M.3    Ritter, A.4    Arnold, T.5
  • 9
    • 58249113974 scopus 로고    scopus 로고
    • USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1
    • Lu Y., Adegoke O.A., Nepveu A., Nakayama K.I., Bedard N., et al. USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1. Mol. Cell. Biol. 2009, 29:547-558.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 547-558
    • Lu, Y.1    Adegoke, O.A.2    Nepveu, A.3    Nakayama, K.I.4    Bedard, N.5
  • 10
    • 84864288635 scopus 로고    scopus 로고
    • Viral immune modulators perturb the human molecular network by common and unique strategies
    • Pichlmair A., Kandasamy K., Alvisi G., Mulhern O., Sacco R., et al. Viral immune modulators perturb the human molecular network by common and unique strategies. Nature 2012, 487:486-490.
    • (2012) Nature , vol.487 , pp. 486-490
    • Pichlmair, A.1    Kandasamy, K.2    Alvisi, G.3    Mulhern, O.4    Sacco, R.5
  • 11
    • 80053911021 scopus 로고    scopus 로고
    • The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2
    • Mei Y., Hahn A.A., Hu S., Yang X. The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2. J. Biol. Chem. 2011, 286:35380-35387.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35380-35387
    • Mei, Y.1    Hahn, A.A.2    Hu, S.3    Yang, X.4
  • 12
    • 67650087753 scopus 로고    scopus 로고
    • The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates
    • Hassink G.C., Zhao B., Sompallae R., Altun M., Gastaldello S., et al. The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates. EMBO Rep. 2009, 10:755-761.
    • (2009) EMBO Rep. , vol.10 , pp. 755-761
    • Hassink, G.C.1    Zhao, B.2    Sompallae, R.3    Altun, M.4    Gastaldello, S.5
  • 13
    • 84862973169 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia
    • Altun M., Zhao B., Velasco K., Liu H., Hassink G., et al. Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia. J. Biol. Chem. 2012, 287:1962-1969.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1962-1969
    • Altun, M.1    Zhao, B.2    Velasco, K.3    Liu, H.4    Hassink, G.5
  • 14
    • 34249947699 scopus 로고    scopus 로고
    • ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
    • Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R., Hurov K.E., et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 2007, 316:1160-1166.
    • (2007) Science , vol.316 , pp. 1160-1166
    • Matsuoka, S.1    Ballif, B.A.2    Smogorzewska, A.3    McDonald, E.R.4    Hurov, K.E.5
  • 15
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy S.R. Profile hidden Markov models. Bioinformatics 1998, 14:755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 16
    • 0032724487 scopus 로고    scopus 로고
    • A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans
    • Shirasu K., Lahaye T., Tan M.W., Zhou F., Azevedo C., et al. A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. Cell 1999, 99:355-366.
    • (1999) Cell , vol.99 , pp. 355-366
    • Shirasu, K.1    Lahaye, T.2    Tan, M.W.3    Zhou, F.4    Azevedo, C.5
  • 17
    • 0037048699 scopus 로고    scopus 로고
    • P23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families
    • Garcia-Ranea J.A., Mirey G., Camonis J., Valencia A. P23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families. FEBS Lett. 2002, 529:162-167.
    • (2002) FEBS Lett. , vol.529 , pp. 162-167
    • Garcia-Ranea, J.A.1    Mirey, G.2    Camonis, J.3    Valencia, A.4
  • 18
    • 0034619767 scopus 로고    scopus 로고
    • SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis
    • Germani A., Bruzzoni-Giovanelli H., Fellous A., Gisselbrecht S., Varin-Blank N., et al. SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis. Oncogene 2000, 19:5997-6006.
    • (2000) Oncogene , vol.19 , pp. 5997-6006
    • Germani, A.1    Bruzzoni-Giovanelli, H.2    Fellous, A.3    Gisselbrecht, S.4    Varin-Blank, N.5
  • 19
    • 0035947080 scopus 로고    scopus 로고
    • Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses
    • Matsuzawa S.I., Reed J.C. Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. Mol. Cell 2001, 7:915-926.
    • (2001) Mol. Cell , vol.7 , pp. 915-926
    • Matsuzawa, S.I.1    Reed, J.C.2
  • 20
    • 14644433599 scopus 로고    scopus 로고
    • Siah: new players in the cellular response to hypoxia
    • Nakayama K., Ronai Z. Siah: new players in the cellular response to hypoxia. Cell Cycle 2004, 3:1345-1347.
    • (2004) Cell Cycle , vol.3 , pp. 1345-1347
    • Nakayama, K.1    Ronai, Z.2
  • 21
    • 71549155940 scopus 로고    scopus 로고
    • Siah proteins: novel drug targets in the Ras and hypoxia pathways
    • House C.M., Moller A., Bowtell D.D. Siah proteins: novel drug targets in the Ras and hypoxia pathways. Cancer Res. 2009, 69:8835-8838.
    • (2009) Cancer Res. , vol.69 , pp. 8835-8838
    • House, C.M.1    Moller, A.2    Bowtell, D.D.3
  • 22
    • 0036143826 scopus 로고    scopus 로고
    • Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling
    • Polekhina G., House C.M., Traficante N., Mackay J.P., Relaix F., et al. Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling. Nat. Struct. Biol. 2002, 9:68-75.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 68-75
    • Polekhina, G.1    House, C.M.2    Traficante, N.3    Mackay, J.P.4    Relaix, F.5
  • 23
    • 0032933351 scopus 로고    scopus 로고
    • Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins
    • Hu G., Fearon E.R. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mol. Cell. Biol. 1999, 19:724-732.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 724-732
    • Hu, G.1    Fearon, E.R.2
  • 24
    • 33645958587 scopus 로고    scopus 로고
    • Elucidation of the substrate binding site of Siah ubiquitin ligase
    • House C.M., Hancock N.C., Moller A., Cromer B.A., Fedorov V., et al. Elucidation of the substrate binding site of Siah ubiquitin ligase. Structure 2006, 14:695-701.
    • (2006) Structure , vol.14 , pp. 695-701
    • House, C.M.1    Hancock, N.C.2    Moller, A.3    Cromer, B.A.4    Fedorov, V.5
  • 25
    • 33845673574 scopus 로고    scopus 로고
    • Regulation of Sprouty2 stability by mammalian Seven-in-Absentia homolog 2
    • Nadeau R.J., Toher J.L., Yang X., Kovalenko D., Friesel R. Regulation of Sprouty2 stability by mammalian Seven-in-Absentia homolog 2. J. Cell. Biochem. 2007, 100:151-160.
    • (2007) J. Cell. Biochem. , vol.100 , pp. 151-160
    • Nadeau, R.J.1    Toher, J.L.2    Yang, X.3    Kovalenko, D.4    Friesel, R.5
  • 26
    • 0031573441 scopus 로고    scopus 로고
    • Characterization of human homologs of the Drosophila Seven in Absentia (sina) gene
    • Hu G., Chung Y.L., Glover T., Valentine V., Look A.T., et al. Characterization of human homologs of the Drosophila Seven in Absentia (sina) gene. Genomics 1997, 46:103-111.
    • (1997) Genomics , vol.46 , pp. 103-111
    • Hu, G.1    Chung, Y.L.2    Glover, T.3    Valentine, V.4    Look, A.T.5
  • 27
    • 65549139358 scopus 로고    scopus 로고
    • The ubiquitin ligase Siah2 and the hypoxia response
    • Nakayama K., Qi J., Ronai Z. The ubiquitin ligase Siah2 and the hypoxia response. Mol. Cancer Res. 2009, 7:443-451.
    • (2009) Mol. Cancer Res. , vol.7 , pp. 443-451
    • Nakayama, K.1    Qi, J.2    Ronai, Z.3
  • 28
    • 79961116969 scopus 로고    scopus 로고
    • Siah1/SIP regulates p27(kip1) stability and cell migration under metabolic stress
    • Nagano Y., Fukushima T., Okemoto K., Tanaka K., Bowtell D.D., et al. Siah1/SIP regulates p27(kip1) stability and cell migration under metabolic stress. Cell Cycle 2011, 10:2592-2602.
    • (2011) Cell Cycle , vol.10 , pp. 2592-2602
    • Nagano, Y.1    Fukushima, T.2    Okemoto, K.3    Tanaka, K.4    Bowtell, D.D.5
  • 29
    • 78650746228 scopus 로고    scopus 로고
    • ARTS and Siah collaborate in a pathway for XIAP degradation
    • Garrison J.B., Correa R.G., Gerlic M., Yip K.W., Krieg A., et al. ARTS and Siah collaborate in a pathway for XIAP degradation. Mol. Cell 2011, 41:107-116.
    • (2011) Mol. Cell , vol.41 , pp. 107-116
    • Garrison, J.B.1    Correa, R.G.2    Gerlic, M.3    Yip, K.W.4    Krieg, A.5
  • 30
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 2004, 431:873-878.
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1    Wang, L.2    Erdjument-Bromage, H.3    Vidal, M.4    Tempst, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.