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Volumn 64, Issue 4, 2012, Pages 316-323

The SOCS box-Adapting proteins for ubiquitination and proteasomal degradation

Author keywords

cullin; E3 ligase; proteasome; SOCS box; ubiquitin

Indexed keywords

ANKYRIN; CULLIN; CULLIN 5; ELONGIN B; ELONGIN C; GUANOSINE TRIPHOSPHATASE; LEUCINE; PROTEASOME; SUPPRESSOR OF CYTOKINE SIGNALING; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84859062753     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1011     Document Type: Review
Times cited : (103)

References (83)
  • 1
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander, D., (2009) The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37, 937-953.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 2
    • 80054848955 scopus 로고    scopus 로고
    • TRIM proteins and cancer
    • Hatakeyama, S., (2011) TRIM proteins and cancer. Nat. Rev. Cancer 11, 792-804.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 792-804
    • Hatakeyama, S.1
  • 3
    • 79959275773 scopus 로고    scopus 로고
    • Mechanisms that regulate peripheral immune responses to control organ-specific autoimmunity
    • 2011
    • Hoyne, G. F., (2011) Mechanisms that regulate peripheral immune responses to control organ-specific autoimmunity. Clin. Dev. Immunol. 2011, 294968.
    • (2011) Clin. Dev. Immunol. , pp. 294968
    • Hoyne, G.F.1
  • 4
    • 79959539790 scopus 로고    scopus 로고
    • Ubiquitylation in apoptosis: A post-translational modification at the edge of life and death
    • Vucic, D., Dixit, V. M., and, Wertz, I. E., (2011) Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death. Nat. Rev. Mol. Cell Biol. 12, 439-452.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 439-452
    • Vucic, D.1    Dixit, V.M.2    Wertz, I.E.3
  • 5
    • 78650915537 scopus 로고    scopus 로고
    • Deubiquitinases in the regulation of NF-ÎB signaling
    • Harhaj, E. W., and, Dixit, V. M., (2011) Deubiquitinases in the regulation of NF-ÎB signaling. Cell Res. 21, 22-39.
    • (2011) Cell Res. , vol.21 , pp. 22-39
    • Harhaj, E.W.1    Dixit, V.M.2
  • 9
    • 52949090018 scopus 로고    scopus 로고
    • SOCS regulation of the JAK/STAT signalling pathway
    • Croker, B. A., Kiu, H., and, Nicholson, S. E., (2008) SOCS regulation of the JAK/STAT signalling pathway. Semin. Cell Dev. Biol. 19, 414-422.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 414-422
    • Croker, B.A.1    Kiu, H.2    Nicholson, S.E.3
  • 10
    • 34249660614 scopus 로고    scopus 로고
    • SOCS proteins, cytokine signalling and immune regulation
    • DOI 10.1038/nri2093, PII NRI2093
    • Yoshimura, A., Naka, T., and, Kubo, M., (2007) SOCS proteins, cytokine signalling and immune regulation. Nat. Rev. Immunol. 7, 454-465. (Pubitemid 46834848)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.6 , pp. 454-465
    • Yoshimura, A.1    Naka, T.2    Kubo, M.3
  • 12
    • 0029147430 scopus 로고
    • Binding of the von Hippel-Lindau tumor suppressor protein to elongin B and C
    • Kibel, A., Iliopoulos, O., DeCaprio, J. A., and, Kaelin, W. G., Jr., (1995) Binding of the von Hippel-Lindau tumor suppressor protein to elongin B and C. Science 269, 1444-1446.
    • (1995) Science , vol.269 , pp. 1444-1446
    • Kibel, A.1    Iliopoulos, O.2    Decaprio, J.A.3    Kaelin Jr., W.G.4
  • 14
    • 0032535364 scopus 로고    scopus 로고
    • The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families
    • Kamura, T., Sato, S., Haque, D., Liu, L., Kaelin, W. G., Jr., et al. (1998) The elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev. 12, 3872-3881. (Pubitemid 29024849)
    • (1998) Genes and Development , vol.12 , Issue.24 , pp. 3872-3881
    • Kamura, T.1    Sato, S.2    Haque, D.3    Liu, L.4    Kaelin Jr., W.G.5    Conaway, R.C.6    Conaway, J.W.7
  • 16
    • 48449086930 scopus 로고    scopus 로고
    • The SOCS box domain of SOCS3: Structure and interaction with the elonginBC-cullin5 ubiquitin ligase
    • Babon, J. J., Sabo, J. K., Soetopo, A., Yao, S., Bailey, M. F., et al. (2008) The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase. J. Mol. Biol. 381, 928-940.
    • (2008) J. Mol. Biol. , vol.381 , pp. 928-940
    • Babon, J.J.1    Sabo, J.K.2    Soetopo, A.3    Yao, S.4    Bailey, M.F.5
  • 17
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-elonginC-elonginB complex: Implications for VHL tumor suppressor function
    • DOI 10.1126/science.284.5413.455
    • Stebbins, C. E., Kaelin, W. G., Jr., and, Pavletich, N. P., (1999) Structure of the VHL-elonginC-elonginB complex: implications for VHL tumor suppressor function. Science 284, 455-461. (Pubitemid 29289612)
    • (1999) Science , vol.284 , Issue.5413 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 18
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • Bullock, A. N., Debreczeni, J. E., Edwards, A. M., Sundstrom, M., and, Knapp, S., (2006) Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc. Natl. Acad. Sci. USA 103, 7637-7642.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 20
    • 35748984946 scopus 로고    scopus 로고
    • Structure of the SOCS4-ElonginB/C Complex Reveals a Distinct SOCS Box Interface and the Molecular Basis for SOCS-Dependent EGFR Degradation
    • DOI 10.1016/j.str.2007.09.016, PII S096921260700367X
    • Bullock, A. N., Rodriguez, M. C., Debreczeni, J. E., Songyang, Z., and, Knapp, S., (2007) Structure of the SOCS4-elonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation. Structure 15, 1493-1504. (Pubitemid 350051927)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1493-1504
    • Bullock, A.N.1    Rodriguez, M.C.2    Debreczeni, J.E.3    Songyang, Z.4    Knapp, S.5
  • 22
    • 78649653568 scopus 로고    scopus 로고
    • Structural assembly of cullin-RING ubiquitin ligase complexes
    • Zimmerman, E. S., Schulman, B. A., and, Zheng, N., (2010) Structural assembly of cullin-RING ubiquitin ligase complexes. Curr. Opin. Struct. Biol. 20, 714-721.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 24
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B. A., Carrano, A. C., Jeffrey, P. D., Bowen, Z., Kinnucan, E. R., et al. (2000) Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 408, 381-386.
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.A.1    Carrano, A.C.2    Jeffrey, P.D.3    Bowen, Z.4    Kinnucan, E.R.5
  • 26
    • 0032803530 scopus 로고    scopus 로고
    • Cytokine-inducible SH2 protein-3 (CIS3/SOCS3) inhibits Janus tyrosine kinase by binding through the N-terminal kinase inhibitory region as well as SH2 domain
    • DOI 10.1046/j.1365-2443.1999.00263.x
    • Sasaki, A., Yasukawa, H., Suzuki, A., Kamizono, S., Syoda, T., et al. (1999) Cytokine-inducible SH2 protein-3 (CIS3/SOCS3) inhibits janus tyrosine kinase by binding through the N-terminal kinase inhibitory region as well as SH2 domain. Genes Cells 4, 339-351. (Pubitemid 29359449)
    • (1999) Genes to Cells , vol.4 , Issue.6 , pp. 339-351
    • Sasaki, A.1    Yasukawa, H.2    Suzuki, A.3    Kamizono, S.4    Syoda, T.5    Kinjyo, I.6    Sasaki, M.7    Johnston, J.A.8    Yoshimura, A.9
  • 33
    • 61349119266 scopus 로고    scopus 로고
    • The SOCS box encodes a hierarchy of affinities for Cullin5: Implications for ubiquitin ligase formation and cytokine signalling suppression
    • Babon, J. J., Sabo, J. K., Zhang, J. G., Nicola, N. A., and, Norton, R. S., (2009) The SOCS box encodes a hierarchy of affinities for Cullin5: implications for ubiquitin ligase formation and cytokine signalling suppression. J. Mol. Biol. 387, 162-174.
    • (2009) J. Mol. Biol. , vol.387 , pp. 162-174
    • Babon, J.J.1    Sabo, J.K.2    Zhang, J.G.3    Nicola, N.A.4    Norton, R.S.5
  • 35
    • 0034640526 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling-1 inhibits VAV function through protein degradation
    • DOI 10.1074/jbc.C000106200
    • De Sepulveda, P., Ilangumaran, S., and, Rottapel, R., (2000) Suppressor of cytokine signaling-1 inhibits VAV function through protein degradation. J. Biol. Chem. 275, 14005-14008. (Pubitemid 30339671)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14005-14008
    • De Sepulveda, P.1    Ilangumaran, S.2    Rottapel, R.3
  • 36
    • 0036233985 scopus 로고    scopus 로고
    • Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1
    • DOI 10.1128/MCB.22.10.3316-3326.2002
    • Ungureanu, D., Saharinen, P., Junttila, I., Hilton, D. J., and, Silvennoinen, O., (2002) Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol. Cell. Biol. 22, 3316-3326. (Pubitemid 34453973)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.10 , pp. 3316-3326
    • Ungureanu, D.1    Saharinen, P.2    Junttila, I.3    Hilton, D.J.4    Silvennoinen, O.5
  • 37
    • 0035918239 scopus 로고    scopus 로고
    • The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2
    • Kamizono, S., Hanada, T., Yasukawa, H., Minoguchi, S., Kato, R., et al. (2001) The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2. J. Biol. Chem. 276, 12530-12538.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12530-12538
    • Kamizono, S.1    Hanada, T.2    Yasukawa, H.3    Minoguchi, S.4    Kato, R.5
  • 38
    • 0035036625 scopus 로고    scopus 로고
    • Socs-1 inhibits TEL-JAK2-mediated transformation of hematopoietic cells through inhibition of JAK2 kinase activity and induction of proteasome-mediated degradation
    • DOI 10.1128/MCB.21.10.3547-3557.2001
    • Frantsve, J., Schwaller, J., Sternberg, D. W., Kutok, J., and, Gilliland, D. G., (2001) Socs-1 inhibits TEL-JAK2-mediated transformation of hematopoietic cells through inhibition of JAK2 kinase activity and induction of proteasome-mediated degradation. Mol. Cell. Biol. 21, 3547-3557. (Pubitemid 32381790)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.10 , pp. 3547-3557
    • Frantsve, J.1    Schwaller, J.2    Sternberg, D.W.3    Kutok, J.4    Gilliland, D.G.5
  • 39
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
    • DOI 10.1074/jbc.C200444200
    • Rui, L., Yuan, M., Frantz, D., Shoelson, S., and, White, M. F., (2002) SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2. J. Biol. Chem. 277, 42394-42398. (Pubitemid 35257562)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 42394-42398
    • Rui, L.1    Yuan, M.2    Frantz, D.3    Shoelson, S.4    White, M.F.5
  • 40
    • 80053210241 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling (SOCS) 1 inhibits type i interferon (IFN) signaling via the interferon α receptor (IFNAR1)-associated tyrosine kinase Tyk2
    • Piganis, R. A., De Weerd, N. A., Gould, J. A., Schindler, C. W., Mansell, A., et al. (2011) Suppressor of cytokine signaling (SOCS) 1 inhibits type I interferon (IFN) signaling via the interferon α receptor (IFNAR1)-associated tyrosine kinase Tyk2. J. Biol. Chem. 286, 33811-33818.
    • (2011) J. Biol. Chem. , vol.286 , pp. 33811-33818
    • Piganis, R.A.1    De Weerd, N.A.2    Gould, J.A.3    Schindler, C.W.4    Mansell, A.5
  • 42
    • 80053321496 scopus 로고    scopus 로고
    • The SOCS2 ubiquitin ligase complex regulates growth hormone receptor levels
    • Vesterlund, M., Zadjali, F., Persson, T., Nielsen, M. L., Kessler, B. M., et al. (2011) The SOCS2 ubiquitin ligase complex regulates growth hormone receptor levels. PLoS One 6, e25358.
    • (2011) PLoS One , vol.6
    • Vesterlund, M.1    Zadjali, F.2    Persson, T.3    Nielsen, M.L.4    Kessler, B.M.5
  • 43
    • 77955484577 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 2 regulates IL-15-primed human NK cell function via control of phosphorylated Pyk2
    • Lee, S. H., Yun, S., Piao, Z. H., Jeong, M., Kim, D. O., et al. (2010) Suppressor of cytokine signaling 2 regulates IL-15-primed human NK cell function via control of phosphorylated Pyk2. J. Immunol. 185, 917-928.
    • (2010) J. Immunol. , vol.185 , pp. 917-928
    • Lee, S.H.1    Yun, S.2    Piao, Z.H.3    Jeong, M.4    Kim, D.O.5
  • 45
    • 47949124200 scopus 로고    scopus 로고
    • C-Cbl-dependent monoubiquitination and lysosomal degradation of gp130
    • Tanaka, Y., Tanaka, N., Saeki, Y., Tanaka, K., Murakami, M., et al. (2008) c-Cbl-dependent monoubiquitination and lysosomal degradation of gp130. Mol. Cell. Biol. 28, 4805-4818.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4805-4818
    • Tanaka, Y.1    Tanaka, N.2    Saeki, Y.3    Tanaka, K.4    Murakami, M.5
  • 46
    • 58249133797 scopus 로고    scopus 로고
    • Deletion of the SOCS box of suppressor of cytokine signaling 3 (SOCS3) in embryonic stem cells reveals SOCS box-dependent regulation of JAK but not STAT phosphorylation
    • Boyle, K., Zhang, J. G., Nicholson, S. E., Trounson, E., Babon, J. J., et al. (2009) Deletion of the SOCS box of suppressor of cytokine signaling 3 (SOCS3) in embryonic stem cells reveals SOCS box-dependent regulation of JAK but not STAT phosphorylation. Cell Signal. 21, 394-404.
    • (2009) Cell Signal. , vol.21 , pp. 394-404
    • Boyle, K.1    Zhang, J.G.2    Nicholson, S.E.3    Trounson, E.4    Babon, J.J.5
  • 47
    • 34247242299 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 3 controls lysosomal routing of G-CSF receptor
    • DOI 10.1038/sj.emboj.7601640, PII 7601640
    • Irandoust, M. I., Aarts, L. H., Roovers, O., Gits, J., Erkeland, S. J., et al. (2007) Suppressor of cytokine signaling 3 controls lysosomal routing of G-CSF receptor. EMBO J. 26, 1782-1793. (Pubitemid 46624051)
    • (2007) EMBO Journal , vol.26 , Issue.7 , pp. 1782-1793
    • Irandoust, M.I.1    Aarts, L.H.J.2    Roovers, O.3    Gits, J.4    Erkeland, S.J.5    Touw, I.P.6
  • 48
    • 67649888820 scopus 로고    scopus 로고
    • Site-specific ubiquitination determines lysosomal sorting and signal attenuation of the granulocyte colony-stimulating factor receptor
    • Wolfler, A., Irandoust, M., Meenhuis, A., Gits, J., Roovers, O., et al. (2009) Site-specific ubiquitination determines lysosomal sorting and signal attenuation of the granulocyte colony-stimulating factor receptor. Traffic 10, 1168-1179.
    • (2009) Traffic , vol.10 , pp. 1168-1179
    • Wolfler, A.1    Irandoust, M.2    Meenhuis, A.3    Gits, J.4    Roovers, O.5
  • 51
    • 1842478134 scopus 로고    scopus 로고
    • Suppressor of Cytokine Signaling 6 Associates with KIT and Regulates KIT Receptor Signaling
    • DOI 10.1074/jbc.M313381200
    • Bayle, J., Letard, S., Frank, R., Dubreuil, P., and, De Sepulveda, P., (2004) Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling. J. Biol. Chem. 279, 12249-12259. (Pubitemid 38445790)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12249-12259
    • Bayle, J.1    Letard, S.2    Frank, R.3    Dubreuil, P.4    De Sepulveda, P.5
  • 52
    • 78650938219 scopus 로고    scopus 로고
    • Structural basis for c-KIT inhibition by the suppressor of cytokine signaling 6 (SOCS6) ubiquitin ligase
    • Zadjali, F., Pike, A. C., Vesterlund, M., Sun, J., Wu, C., et al. (2011) Structural basis for c-KIT inhibition by the suppressor of cytokine signaling 6 (SOCS6) ubiquitin ligase. J. Biol. Chem. 286, 480-490.
    • (2011) J. Biol. Chem. , vol.286 , pp. 480-490
    • Zadjali, F.1    Pike, A.C.2    Vesterlund, M.3    Sun, J.4    Wu, C.5
  • 53
    • 77951240458 scopus 로고    scopus 로고
    • SOCS-6 negatively regulates T cell activation through targeting p56lck to proteasomal degradation
    • Choi, Y. B., Son, M., Park, M., Shin, J., and, Yun, Y., (2010) SOCS-6 negatively regulates T cell activation through targeting p56lck to proteasomal degradation. J. Biol. Chem. 285, 7271-7280.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7271-7280
    • Choi, Y.B.1    Son, M.2    Park, M.3    Shin, J.4    Yun, Y.5
  • 54
    • 28844473943 scopus 로고    scopus 로고
    • ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes
    • DOI 10.1016/j.febslet.2005.11.016, PII S0014579305013761
    • Kohroki, J., Nishiyama, T., Nakamura, T., and, Masuho, Y., (2005) ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin ligase complexes. FEBS Lett. 579, 6796-6802. (Pubitemid 41773689)
    • (2005) FEBS Letters , vol.579 , Issue.30 , pp. 6796-6802
    • Kohroki, J.1    Nishiyama, T.2    Nakamura, T.3    Masuho, Y.4
  • 55
    • 14044267523 scopus 로고    scopus 로고
    • ASB2 is an elongin BC-interacting protein that can assemble with cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex
    • DOI 10.1074/jbc.M413040200
    • Heuze, M. L., Guibal, F. C., Banks, C. A., Conaway, J. W., Conaway, R. C., et al. (2005) ASB2 is an elongin BC-interacting protein that can assemble with Cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex. J. Biol. Chem. 280, 5468-5474. (Pubitemid 40280022)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5468-5474
    • Heuze, M.L.1    Guibal, F.C.2    Banks, C.A.3    Conaway, J.W.4    Conaway, R.C.5    Cayre, Y.E.6    Benecke, A.7    Lutz, P.G.8
  • 57
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: A diversity of interactions on a common structural framework
    • DOI 10.1016/S0968-0004(99)01426-7, PII S0968000499014267
    • Sedgwick, S. G., and, Smerdon, S. J., (1999) The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24, 311-316. (Pubitemid 29366805)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.8 , pp. 311-316
    • Sedgwick, S.G.1    Smerdon, S.J.2
  • 58
    • 0026607234 scopus 로고
    • The ANK repeat: A ubiquitous motif involved in macromolecular recognition
    • Michaely, P., and, Bennett, V., (1992) The ANK repeat: a ubiquitous motif involved in macromolecular recognition. Trends Cell. Biol. 2, 127-129.
    • (1992) Trends Cell. Biol. , vol.2 , pp. 127-129
    • Michaely, P.1    Bennett, V.2
  • 59
    • 67349184333 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase specificity subunit ASB2β is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation
    • Bello, N. F., Lamsoul, I., Heuze, M. L., Metais, A., Moreaux, G., et al. (2009) The E3 ubiquitin ligase specificity subunit ASB2β is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation. Cell Death Differ. 16, 921-932.
    • (2009) Cell Death Differ. , vol.16 , pp. 921-932
    • Bello, N.F.1    Lamsoul, I.2    Heuze, M.L.3    Metais, A.4    Moreaux, G.5
  • 60
    • 58149386407 scopus 로고    scopus 로고
    • ASB2 targets filamins A and B to proteasomal degradation
    • Heuze, M. L., Lamsoul, I., Baldassarre, M., Lad, Y., Leveque, S., et al. (2008) ASB2 targets filamins A and B to proteasomal degradation. Blood 112, 5130-5140.
    • (2008) Blood , vol.112 , pp. 5130-5140
    • Heuze, M.L.1    Lamsoul, I.2    Baldassarre, M.3    Lad, Y.4    Leveque, S.5
  • 61
    • 79961149492 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain
    • Razinia, Z., Baldassarre, M., Bouaouina, M., Lamsoul, I., Lutz, P. G., et al. (2011) The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain. J. Cell Sci. 124, 2631-2641.
    • (2011) J. Cell Sci. , vol.124 , pp. 2631-2641
    • Razinia, Z.1    Baldassarre, M.2    Bouaouina, M.3    Lamsoul, I.4    Lutz, P.G.5
  • 62
    • 18944380864 scopus 로고    scopus 로고
    • Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and degradation of tumor necrosis factor receptor II
    • DOI 10.1128/MCB.25.11.4716-4726.2005
    • Chung, A. S., Guan, Y. J., Yuan, Z. L., Albina, J. E., and, Chin, Y. E., (2005) Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and degradation of tumor necrosis factor receptor II. Mol. Cell. Biol. 25, 4716-4726. (Pubitemid 40705774)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.11 , pp. 4716-4726
    • Chung, A.S.1    Guan, Y.-J.2    Yuan, Z.-L.3    Albina, J.E.4    Chin, Y.E.5
  • 63
    • 73649094138 scopus 로고    scopus 로고
    • Expression of ankyrin repeat and suppressor of cytokine signaling box protein 4 (Asb-4) in proopiomelanocortin neurons of the arcuate nucleus of mice produces a hyperphagic, lean phenotype
    • Li, J. Y., Chai, B. X., Zhang, W., Wang, H., and, Mulholland, M. W., (2010) Expression of ankyrin repeat and suppressor of cytokine signaling box protein 4 (Asb-4) in proopiomelanocortin neurons of the arcuate nucleus of mice produces a hyperphagic, lean phenotype. Endocrinology 151, 134-142.
    • (2010) Endocrinology , vol.151 , pp. 134-142
    • Li, J.Y.1    Chai, B.X.2    Zhang, W.3    Wang, H.4    Mulholland, M.W.5
  • 64
    • 80053364119 scopus 로고    scopus 로고
    • Ankyrin repeat and SOCS box containing protein 4 (Asb-4) colocalizes with insulin receptor substrate 4 (IRS4) in the hypothalamic neurons and mediates IRS4 degradation
    • Li, J. Y., Chai, B., Zhang, W., Wu, X., Zhang, C., et al. (2011) Ankyrin repeat and SOCS box containing protein 4 (Asb-4) colocalizes with insulin receptor substrate 4 (IRS4) in the hypothalamic neurons and mediates IRS4 degradation. BMC Neurosci. 12, 95.
    • (2011) BMC Neurosci. , vol.12 , pp. 95
    • Li, J.Y.1    Chai, B.2    Zhang, W.3    Wu, X.4    Zhang, C.5
  • 66
    • 77951936368 scopus 로고    scopus 로고
    • ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial function
    • Kwon, S., Kim, D., Rhee, J. W., Park, J. A., Kim, D. W., et al. (2010) ASB9 interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial function. BMC Biol. 8, 23.
    • (2010) BMC Biol. , vol.8 , pp. 23
    • Kwon, S.1    Kim, D.2    Rhee, J.W.3    Park, J.A.4    Kim, D.W.5
  • 69
    • 79955653594 scopus 로고    scopus 로고
    • Essential role for the d-Asb11 cul5 Box domain for proper notch signaling and neural cell fate decisions in vivo
    • Sartori da Silva, M. A., Tee, J. M., Paridaen, J., Brouwers, A., Runtuwene, V., et al. (2010) Essential role for the d-Asb11 cul5 Box domain for proper notch signaling and neural cell fate decisions in vivo. PLoS One 5, e14023.
    • (2010) PLoS One , vol.5
    • Sartori Da Silva, M.A.1    Tee, J.M.2    Paridaen, J.3    Brouwers, A.4    Runtuwene, V.5
  • 70
    • 80053491919 scopus 로고    scopus 로고
    • TLR regulation of SPSB1 controls inducible nitric oxide synthase induction
    • Lewis, R. S., Kolesnik, T. B., Kuang, Z., D'Cruz, A. A., Blewitt, M. E., et al. (2011) TLR regulation of SPSB1 controls inducible nitric oxide synthase induction. J. Immunol. 187, 3798-3805.
    • (2011) J. Immunol. , vol.187 , pp. 3798-3805
    • Lewis, R.S.1    Kolesnik, T.B.2    Kuang, Z.3    D'Cruz, A.A.4    Blewitt, M.E.5
  • 71
    • 77954709822 scopus 로고    scopus 로고
    • The SPRY domain-containing SOCS box protein SPSB2 targets iNOS for proteasomal degradation
    • Kuang, Z., Lewis, R. S., Curtis, J. M., Zhan, Y., Saunders, B. M., et al. (2010) The SPRY domain-containing SOCS box protein SPSB2 targets iNOS for proteasomal degradation. J. Cell Biol. 190, 129-141.
    • (2010) J. Cell Biol. , vol.190 , pp. 129-141
    • Kuang, Z.1    Lewis, R.S.2    Curtis, J.M.3    Zhan, Y.4    Saunders, B.M.5
  • 72
    • 79953192137 scopus 로고    scopus 로고
    • Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS box-containing proteins
    • Nishiya, T., Matsumoto, K., Maekawa, S., Kajita, E., Horinouchi, T., et al. (2011) Regulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS box-containing proteins. J. Biol. Chem. 286, 9009-9019.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9009-9019
    • Nishiya, T.1    Matsumoto, K.2    Maekawa, S.3    Kajita, E.4    Horinouchi, T.5
  • 73
    • 77949346488 scopus 로고    scopus 로고
    • Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors
    • Kugler, J. M., Woo, J. S., Oh, B. H., and, Lasko, P., (2010) Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors. Mol. Cell. Biol. 30, 1769-1782.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1769-1782
    • Kugler, J.M.1    Woo, J.S.2    Oh, B.H.3    Lasko, P.4
  • 74
    • 41949130508 scopus 로고    scopus 로고
    • Ubiquitination and degradation of homeodomain-interacting protein kinase 2 by WD40 repeat/SOCS box protein WSB-1
    • Choi, D. W., Seo, Y. M., Kim, E. A., Sung, K. S., Ahn, J. W., et al. (2008) Ubiquitination and degradation of homeodomain-interacting protein kinase 2 by WD40 repeat/SOCS box protein WSB-1. J. Biol. Chem. 283, 4682-4689.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4682-4689
    • Choi, D.W.1    Seo, Y.M.2    Kim, E.A.3    Sung, K.S.4    Ahn, J.W.5
  • 76
    • 34047123668 scopus 로고    scopus 로고
    • Novel role of WD40 and SOCS box protein-2 in steady-state distribution of granulocyte colony-stimulating factor receptor and G-CSF-controlled proliferation and differentiation signaling
    • DOI 10.1038/sj.onc.1210004, PII 1210004
    • Erkeland, S. J., Aarts, L. H., Irandoust, M., Roovers, O., Klomp, A., et al. (2007) Novel role of WD40 and SOCS box protein-2 in steady-state distribution of granulocyte colony-stimulating factor receptor and G-CSF-controlled proliferation and differentiation signaling. Oncogene 26, 1985-1994. (Pubitemid 46514741)
    • (2007) Oncogene , vol.26 , Issue.14 , pp. 1985-1994
    • Erkeland, S.J.1    Aarts, L.H.2    Irandoust, M.3    Roovers, O.4    Klomp, A.5    Valkhof, M.6    Gits, J.7    Eyckerman, S.8    Tavernier, J.9    Touw, I.P.10
  • 78
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA
    • DOI 10.1016/S1097-2765(03)00490-8
    • Ryo, A., Suizu, F., Yoshida, Y., Perrem, K., Liou, Y. C., et al. (2003) Regulation of NF-ÎB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell 12, 1413-1426. (Pubitemid 38037011)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1413-1426
    • Ryo, A.1    Suizu, F.2    Yoshida, Y.3    Perrem, K.4    Liou, Y.-C.5    Wulf, G.6    Rottapel, R.7    Yamaoka, S.8    Lu, K.P.9
  • 81
    • 84856603153 scopus 로고    scopus 로고
    • ECSASB2 mediates MLL degradation during hematopoietic differentiation
    • Wang, J., Muntean, A. G., Hess, J. L., (2012) ECSASB2 mediates MLL degradation during hematopoietic differentiation. Blood 119, 1151-1161.
    • (2012) Blood , vol.119 , pp. 1151-1161
    • Wang, J.1    Muntean, A.G.2    Hess, J.L.3
  • 82
    • 79955580832 scopus 로고    scopus 로고
    • Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes
    • Nie, L., Zhao, Y., Wu, W., Yang, Y. Z., Wang, H. C., et al. (2011) Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes. Cell Res. 21, 754-769.
    • (2011) Cell Res. , vol.21 , pp. 754-769
    • Nie, L.1    Zhao, Y.2    Wu, W.3    Yang, Y.Z.4    Wang, H.C.5
  • 83
    • 82355171881 scopus 로고    scopus 로고
    • A mechanism underlying NOTCH-induced and ubiquitin-mediated JAK3 degradation
    • Wu, W., Sun, X. H., (2011) A mechanism underlying NOTCH-induced and ubiquitin-mediated JAK3 degradation. J. Biol. Chem. 286, 41153-41162.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41153-41162
    • Wu, W.1    Sun, X.H.2


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