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Volumn 24, Issue 20, 2004, Pages 9092-9101

SOCS-1 localizes to the microtubule organizing complex-associated 20S proteasome

Author keywords

[No Author keywords available]

Indexed keywords

JANUS KINASE; NOCODAZOLE; PROTEASOME; PROTEIN SH2; STAT PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 1;

EID: 4744363325     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.20.9092-9101.2004     Document Type: Article
Times cited : (41)

References (54)
  • 1
    • 0036595049 scopus 로고    scopus 로고
    • Suppressors of cytokine signalling (SOCS) in the immune system
    • Alexander, W. S. 2002. Suppressors of cytokine signalling (SOCS) in the immune system. Nat. Rev. Immunol. 2:410-416.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 410-416
    • Alexander, W.S.1
  • 3
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen, J. S., C. J. Wilkinson, T. Mayor, P. Mortensen, E. A. Nigg, and M. Mann. 2003. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426:570-574.
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 4
    • 0036413509 scopus 로고    scopus 로고
    • Preparation and expression of biologically active prolactin and growth hormone receptors and suppressor of cytokine signaling proteins 1, 2, 3, and 6 tagged with cyan and yellow fluorescent proteins
    • Ben-Yair, L., R. Slaaby, A. Herman, Y. Cohen, E. Biener, N. Moran, A. Yoshimura, J. Whittaker, P. D. Meyts, B. Herman, and A. Gertler. 2002. Preparation and expression of biologically active prolactin and growth hormone receptors and suppressor of cytokine signaling proteins 1, 2, 3, and 6 tagged with cyan and yellow fluorescent proteins. Protein Expr. Purif. 25:456-464.
    • (2002) Protein Expr. Purif. , vol.25 , pp. 456-464
    • Ben-Yair, L.1    Slaaby, R.2    Herman, A.3    Cohen, Y.4    Biener, E.5    Moran, N.6    Yoshimura, A.7    Whittaker, J.8    Meyts, P.D.9    Herman, B.10    Gertler, A.11
  • 5
    • 0036646099 scopus 로고    scopus 로고
    • Cytoplasmic transport of Stat3 by receptor-mediated endocytosis
    • Bild, A. H., J. Turkson, and R. Jove. 2002. Cytoplasmic transport of Stat3 by receptor-mediated endocytosis. EMBO J. 21:3255-3263.
    • (2002) EMBO J. , vol.21 , pp. 3255-3263
    • Bild, A.H.1    Turkson, J.2    Jove, R.3
  • 7
    • 0034640526 scopus 로고    scopus 로고
    • Suppressor of cyokine signaling-1 inhibits VAV function through protein degradation
    • De Sepulveda, P., S. Ilangumaran, and R. Rottapel. 2000. Suppressor of cyokine signaling-1 inhibits VAV function through protein degradation. J. Biol. Chem. 275:14005-14008.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14005-14008
    • De Sepulveda, P.1    Ilangumaran, S.2    Rottapel, R.3
  • 9
    • 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
    • Frantsve, J., J. Schwaller, D. W. Sternberg, J. Kutok, and D. G. Gilliland. 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.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3547-3557
    • Frantsve, J.1    Schwaller, J.2    Sternberg, D.W.3    Kutok, J.4    Gilliland, D.G.5
  • 10
    • 0033200397 scopus 로고    scopus 로고
    • Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle
    • Freed, E., K. R. Lacey, P. Huie, S. A. Lyapina, R. J. Deshaies, T. Stearns, and P. K. Jackson. 1999. Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle. Genes Dev. 13:2242-2257.
    • (1999) Genes Dev. , vol.13 , pp. 2242-2257
    • Freed, E.1    Lacey, K.R.2    Huie, P.3    Lyapina, S.A.4    Deshaies, R.J.5    Stearns, T.6    Jackson, P.K.7
  • 12
    • 0033558808 scopus 로고    scopus 로고
    • Association of human SCFskp2 subunit p19skp1 with interphase centrosomes and mitotic spindle poles
    • Gstaiger, M., A. Marti, and W. Krek. 1999. Association of human SCFskp2 subunit p19skp1 with interphase centrosomes and mitotic spindle poles. Exp. Cell Res. 247:554-562.
    • (1999) Exp. Cell Res. , vol.247 , pp. 554-562
    • Gstaiger, M.1    Marti, A.2    Krek, W.3
  • 13
    • 0035798660 scopus 로고    scopus 로고
    • A mutant form of JAB/SOCS1 augments the cytokine-induced JAK/STAT pathway by accelerating degradation of wild-type JAB/CIS family proteins through the SOCS-box
    • Hanada, T., T. Yoshida, I. Kinjyo, S. Minoguchi, H. Yasukawa, S. Kato, H. Mimata, Y. Nomura, Y. Seki, M. Kubo, and A. Yoshimura. 2001. A mutant form of JAB/SOCS1 augments the cytokine-induced JAK/STAT pathway by accelerating degradation of wild-type JAB/CIS family proteins through the SOCS-box. J. Biol. Chem. 276:40746-40754.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40746-40754
    • Hanada, T.1    Yoshida, T.2    Kinjyo, I.3    Minoguchi, S.4    Yasukawa, H.5    Kato, S.6    Mimata, H.7    Nomura, Y.8    Seki, Y.9    Kubo, M.10    Yoshimura, A.11
  • 15
    • 0032880969 scopus 로고    scopus 로고
    • γ-Tubulin complexes: Size does matter
    • Jeng, R., and T. Stearns. 1999. γ-Tubulin complexes: size does matter. Trends Cell Biol. 9:339-342.
    • (1999) Trends Cell Biol. , vol.9 , pp. 339-342
    • Jeng, R.1    Stearns, T.2
  • 18
    • 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., S. Sato, D. Haque, L. Liu, W. G. Kaelin, Jr., R. C. Conaway, and J. W. Conaway. 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.
    • (1998) Genes Dev. , vol.12 , 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
  • 19
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1a ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex
    • Kamura, T., S. Sato, K. Iwai, M. Czyzyk-Krzeska, R. C. Conaway, and J. W. Conaway. 2000. Activation of HIF1a ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc. Natl. Acad. Sci. USA 97:10430-10435.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10430-10435
    • Kamura, T.1    Sato, S.2    Iwai, K.3    Czyzyk-Krzeska, M.4    Conaway, R.C.5    Conaway, J.W.6
  • 20
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S., and E. L. Holzbaur. 1999. Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol. 11:45-53.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 21
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., G. Odorizzi, and S. D. Emr. 2002. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3:893-905.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 23
    • 1342272916 scopus 로고    scopus 로고
    • How the cyclin became a cyclin: Regulated proteolysis in the cell cycle
    • Koepp, D. M., J. W. Harper, and S. J. Elledge. 1999. How the cyclin became a cyclin: regulated proteolysis in the cell cycle. Cell 97:431-434.
    • (1999) Cell , vol.97 , pp. 431-434
    • Koepp, D.M.1    Harper, J.W.2    Elledge, S.J.3
  • 24
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J., and D. Cowburn. 1997. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26:259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 26
    • 0141865509 scopus 로고    scopus 로고
    • Negative regulation of FAK signaling by SOCS proteins
    • Liu, E., J. F. Cote, and K. Vuori. 2003. Negative regulation of FAK signaling by SOCS proteins. EMBO J. 22:5036-5046.
    • (2003) EMBO J. , vol.22 , pp. 5036-5046
    • Liu, E.1    Cote, J.F.2    Vuori, K.3
  • 27
    • 0033120880 scopus 로고    scopus 로고
    • SOCS-1 is a potent inhibitor of IL-4 signal transduction
    • Losman, J. A., X. P. Chen, D. Hilton, and P. Rothman. 1999. SOCS-1 is a potent inhibitor of IL-4 signal transduction. J. Immunol. 162:3770-3774.
    • (1999) J. Immunol. , vol.162 , pp. 3770-3774
    • Losman, J.A.1    Chen, X.P.2    Hilton, D.3    Rothman, P.4
  • 28
    • 0032559586 scopus 로고    scopus 로고
    • Cytoskeletal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motifdependent mechanism
    • Lowin-Kropf, B., V. S. Shapiro, and A. Weiss. 1998. Cytoskeletal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motifdependent mechanism. J. Cell Biol. 140:861-871.
    • (1998) J. Cell Biol. , vol.140 , pp. 861-871
    • Lowin-Kropf, B.1    Shapiro, V.S.2    Weiss, A.3
  • 29
    • 0142211201 scopus 로고    scopus 로고
    • An SH2 domain-dependent, phosphotyrosine-independent interaction between Vav1 and the Mer receptor tyrosine kinase: A mechanism for localizing guanine nucleotide-exchange factor action
    • Mahajan, N. P., and H. S. Earp. 2003. An SH2 domain-dependent, phosphotyrosine-independent interaction between Vav1 and the Mer receptor tyrosine kinase: a mechanism for localizing guanine nucleotide-exchange factor action. J. Biol. Chem. 278:42596-42603.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42596-42603
    • Mahajan, N.P.1    Earp, H.S.2
  • 31
    • 0001367697 scopus 로고    scopus 로고
    • Method of centrosome isolation from cultured animal cells
    • J. E. Celis (ed.), Academic Press, Inc., New York, N. Y.
    • Moudjou, M., and M. Bornens. 1998. Method of centrosome isolation from cultured animal cells, p. 111-119. In J. E. Celis (ed.), Cell biology: a laboratory handbook, vol. 2. Academic Press, Inc., New York, N. Y.
    • (1998) Cell Biology: A Laboratory Handbook , vol.2 , pp. 111-119
    • Moudjou, M.1    Bornens, M.2
  • 35
    • 0033555258 scopus 로고    scopus 로고
    • Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction
    • Nicholson, S. E., T. A. Wilson, A. Farley, R. Starr, J.-G. Zhang, M. Baca, W. S. Alexander, D. Metcalf, D. J. Hilton, and N. A. Nicola. 1999. Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction. EMBO J. 18:375-385.
    • (1999) EMBO J. , vol.18 , pp. 375-385
    • Nicholson, S.E.1    Wilson, T.A.2    Farley, A.3    Starr, R.4    Zhang, J.-G.5    Baca, M.6    Alexander, W.S.7    Metcalf, D.8    Hilton, D.J.9    Nicola, N.A.10
  • 36
    • 0033212986 scopus 로고    scopus 로고
    • Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition
    • Poy, F., M. B. Yaffe, J. Sayos, K. Saxena, M. Morra, J. Sumegi, L. C. Cantley, C. Terhorst, and M. J. Eck. 1999. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol. Cell 4:555-561.
    • (1999) Mol. Cell , vol.4 , pp. 555-561
    • Poy, F.1    Yaffe, M.B.2    Sayos, J.3    Saxena, K.4    Morra, M.5    Sumegi, J.6    Cantley, L.C.7    Terhorst, C.8    Eck, M.J.9
  • 37
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and 1RS2
    • Rui, L., M. Yuan, D. Frantz, S. Shoelson, and M. F. White. 2002. SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and 1RS2. J. Biol. Chem. 277:42394-42398.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42394-42398
    • Rui, L.1    Yuan, M.2    Frantz, D.3    Shoelson, S.4    White, M.F.5
  • 38
    • 0034120709 scopus 로고    scopus 로고
    • IFN regulatory factor-1-mediated transcriptional activation of mouse STAT-induced STAT inhibitor-1 gene promoter by IFN-γ
    • Saito, H., Y. Morita, M. Fujimoto, M. Narazaki, T. Naka, and T. Kishimoto. 2000. IFN regulatory factor-1-mediated transcriptional activation of mouse STAT-induced STAT inhibitor-1 gene promoter by IFN-γ. J. Immunol. 164:5833-5843.
    • (2000) J. Immunol. , vol.164 , pp. 5833-5843
    • Saito, H.1    Morita, Y.2    Fujimoto, M.3    Narazaki, M.4    Naka, T.5    Kishimoto, T.6
  • 39
    • 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
    • Sasaki, A., H. Yasukawa, A. Suzuki, S. Kaminzono, T. Syoda, I. Kinjyo, M. Sasaki, J. A. Jobnston, and A. Yoshimura. 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.
    • (1999) Genes Cells , vol.4 , pp. 339-351
    • Sasaki, A.1    Yasukawa, H.2    Suzuki, A.3    Kaminzono, S.4    Syoda, T.5    Kinjyo, I.6    Sasaki, M.7    Jobnston, J.A.8    Yoshimura, A.9
  • 40
    • 0034682465 scopus 로고    scopus 로고
    • Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products
    • Schoenfeld, A. R., E. J. Davidowitz, and R. D. Burk. 2000. Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products. Proc. Natl. Acad. Sci. USA 97:8507-8512.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8507-8512
    • Schoenfeld, A.R.1    Davidowitz, E.J.2    Burk, R.D.3
  • 42
    • 0037329054 scopus 로고    scopus 로고
    • The role of ubiquitylation in signaling by growth factors: Implications to cancer
    • Shtiegman, K., and Y. Yarden. 2003. The role of ubiquitylation in signaling by growth factors: implications to cancer. Semin. Cancer Biol. 13:29-40.
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 29-40
    • Shtiegman, K.1    Yarden, Y.2
  • 43
    • 0001421104 scopus 로고    scopus 로고
    • Different protein turnover of interleukin-6-type cytokine signalling components
    • Siewert, E., W. Muller-Esterl, R. Starr, P. C. Heinrich, and F. Schaper. 1999. Different protein turnover of interleukin-6-type cytokine signalling components. Eur. J. Biochem. 265:251-257.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 251-257
    • Siewert, E.1    Muller-Esterl, W.2    Starr, R.3    Heinrich, P.C.4    Schaper, F.5
  • 44
    • 0033054154 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and endocytosis
    • Strous, G. J., and R. Govers. 1999. The ubiquitin-proteasome system and endocytosis. J. Cell Sci. 112:1417-1423.
    • (1999) J. Cell Sci. , vol.112 , pp. 1417-1423
    • Strous, G.J.1    Govers, R.2
  • 47
    • 0036233985 scopus 로고    scopus 로고
    • Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1
    • Ungureanu, D., P. Saharinen, I. Junttila, D. J. Hilton, and O. Silvennoinen. 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.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3316-3326
    • Ungureanu, D.1    Saharinen, P.2    Junttila, I.3    Hilton, D.J.4    Silvennoinen, O.5
  • 48
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • Online
    • van Roessel, P., and A. H. Brand. 2002. Imaging into the future: visualizing gene expression and protein interactions with fluorescent proteins. Nat. Cell Biol. 4:E15-E20. [Online.]
    • (2002) Nat. Cell Biol. , vol.4
    • Van Roessel, P.1    Brand, A.H.2
  • 50
    • 0037131428 scopus 로고    scopus 로고
    • The N-terminal SH2 domains of Syk and ZAP-70 mediate phosphotyrosine- independent binding to integrin beta cytoplasmic domains
    • Woodside, D. G., A. Obergfell, A. Talapatra, D. A. Calderwood, S. J. Shattil, and M. H. Ginsberg. 2002. The N-terminal SH2 domains of Syk and ZAP-70 mediate phosphotyrosine-independent binding to integrin beta cytoplasmic domains. J. Biol. Chem. 277:39401-39408.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39401-39408
    • Woodside, D.G.1    Obergfell, A.2    Talapatra, A.3    Calderwood, D.A.4    Shattil, S.J.5    Ginsberg, M.H.6
  • 51
    • 0038237514 scopus 로고    scopus 로고
    • Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein
    • Xia, Y., G. M. Pao, H.-W. Chen, I. M. Verma, and T. Hunter. 2003. Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein. J. Biol. Chem. 278:5255-5263.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5255-5263
    • Xia, Y.1    Pao, G.M.2    Chen, H.-W.3    Verma, I.M.4    Hunter, T.5


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