메뉴 건너뛰기




Volumn 22, Issue 12, 2008, Pages 4296-4305

Identification of a nuclear localization signal in suppressor of cytokine signaling 1

Author keywords

Cell activation; Cytokine receptors; Inflammation; Signal transduction

Indexed keywords

GAMMA INTERFERON; INTERCELLULAR ADHESION MOLECULE 1; PROTEIN SH2; STAT1 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 1;

EID: 57349102472     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.08-116079     Document Type: Article
Times cited : (39)

References (39)
  • 1
    • 23744506255 scopus 로고    scopus 로고
    • Negative regulation of cytokine and TLR signalings by SOCS and others
    • Naka, T., Fujimoto, M., Tsutsui, H., and Yoshimura, A. (2005) Negative regulation of cytokine and TLR signalings by SOCS and others. Adv. Immunol. 87, 61-122
    • (2005) Adv. Immunol , vol.87 , pp. 61-122
    • Naka, T.1    Fujimoto, M.2    Tsutsui, H.3    Yoshimura, A.4
  • 2
    • 2542478996 scopus 로고    scopus 로고
    • The role of suppressors of cytokine signaling (SOCS) proteins in regulation of the immune response
    • Alexander, W. S., and Hilton, D. J. (2003) The role of suppressors of cytokine signaling (SOCS) proteins in regulation of the immune response. Annu. Rev. Immunol. 22, 503-529
    • (2003) Annu. Rev. Immunol , vol.22 , pp. 503-529
    • Alexander, W.S.1    Hilton, D.J.2
  • 5
    • 0034724677 scopus 로고    scopus 로고
    • SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130
    • Schmitz, J., Weissenbach, M., Haan, S., Heinrich, P. C., and Schaper, F. (2000) SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130. J. Biol. Chem. 275, 12848-12856
    • (2000) J. Biol. Chem , vol.275 , pp. 12848-12856
    • Schmitz, J.1    Weissenbach, M.2    Haan, S.3    Heinrich, P.C.4    Schaper, F.5
  • 7
    • 10644276385 scopus 로고    scopus 로고
    • VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
    • Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., and Nakayama, K. I. (2004) VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev. 18, 3055-3065
    • (2004) Genes Dev , vol.18 , pp. 3055-3065
    • Kamura, T.1    Maenaka, K.2    Kotoshiba, S.3    Matsumoto, M.4    Kohda, D.5    Conaway, R.C.6    Conaway, J.W.7    Nakayama, K.I.8
  • 8
    • 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. J., Conaway, R. C., and Conaway, J. W. (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, W.G.J.5    Conaway, R.C.6    Conaway, J.W.7
  • 9
    • 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. U. S. A. 103, 7637-7642
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 11
    • 33846475712 scopus 로고    scopus 로고
    • COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase
    • Maine, G. N., Mao, X., Komarck, C. M., and Burstein, E. (2007) COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase. EMBO J. 26, 436-447
    • (2007) EMBO J , vol.26 , pp. 436-447
    • Maine, G.N.1    Mao, X.2    Komarck, C.M.3    Burstein, E.4
  • 12
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA
    • Ryo, A., Suizu, F., Yoshida, Y., Perrem, K., Liou, Y. C., Wulf, G., Rottapel, R., Yamaoka, S., and Lu, K. P. (2003) Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell. 12, 1413-1426
    • (2003) Mol. Cell , vol.12 , 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
  • 13
    • 3142771914 scopus 로고    scopus 로고
    • Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response
    • Saccani, S., Marazzi, I., Beg, A. A., and Natoli, G. (2004) Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response. J. Exp. Med. 200, 107-113
    • (2004) J. Exp. Med , vol.200 , pp. 107-113
    • Saccani, S.1    Marazzi, I.2    Beg, A.A.3    Natoli, G.4
  • 17
    • 0038807434 scopus 로고    scopus 로고
    • Negative regulation of interleukin-12 signaling by suppressor of cytokine signaling-1
    • Eyles, J. L., Metcalf, D., Grusby, M. J., Hilton, D. J., and Starr, R. (2002) Negative regulation of interleukin-12 signaling by suppressor of cytokine signaling-1. J. Biol. Chem. 277, 43735-43740
    • (2002) J. Biol. Chem , vol.277 , pp. 43735-43740
    • Eyles, J.L.1    Metcalf, D.2    Grusby, M.J.3    Hilton, D.J.4    Starr, R.5
  • 19
    • 0037154210 scopus 로고    scopus 로고
    • Polycystic kidneys and chronic inflammatory lesions are the delayed consequences of loss of the suppressor of cytokine signaling-1 (SOCS-1)
    • Metcalf, D., Mifsud, S., Di Rago, L., Nicola, N. A., Hilton, D. J., and Alexander, W. S. (2002) Polycystic kidneys and chronic inflammatory lesions are the delayed consequences of loss of the suppressor of cytokine signaling-1 (SOCS-1). Proc. Natl. Acad. Sci. U. S. A. 99, 943-948
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 943-948
    • Metcalf, D.1    Mifsud, S.2    Di Rago, L.3    Nicola, N.A.4    Hilton, D.J.5    Alexander, W.S.6
  • 21
    • 0034331073 scopus 로고    scopus 로고
    • Finding nuclear localization signals
    • Cokol, M., Nair, R., and Rost, B. (2000) Finding nuclear localization signals. EMBO Rep. 1, 411-415
    • (2000) EMBO Rep , vol.1 , pp. 411-415
    • Cokol, M.1    Nair, R.2    Rost, B.3
  • 23
    • 0001421104 scopus 로고    scopus 로고
    • Different protein turnover of interleukin-6-type cytokine signalling components
    • Siewert, E., Muller-Esterl, W., Starr, R., Heinrich, P. C., and Schaper, F. (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
  • 24
    • 0035877256 scopus 로고    scopus 로고
    • Suppressors of cytokine signaling (SOCS)-1 and SOCS-3 are induced by CpG-DNA and modulate cytokine responses in APCs
    • Dalpke, A. H., Opper, S., Zimmermann, S., and Heeg, K. (2001) Suppressors of cytokine signaling (SOCS)-1 and SOCS-3 are induced by CpG-DNA and modulate cytokine responses in APCs. J. Immunol. 166, 7082-7089
    • (2001) J. Immunol , vol.166 , pp. 7082-7089
    • Dalpke, A.H.1    Opper, S.2    Zimmermann, S.3    Heeg, K.4
  • 25
    • 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., Slaaby, R., Herman, A., Cohen, Y., Biener, E., Moran, N., Yoshimura, A., Whittaker, J., De Meyts, P., Herman, B., and Gertler, A. (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
    • (2002) Protein Expr. Purif , vol.25 , pp. 456
    • 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    De Meyts, P.9    Herman, B.10    Gertler, A.11
  • 26
    • 46549086459 scopus 로고    scopus 로고
    • Increased cytoplasmic levels of CIS, SOCS1, SOCS2, or SOCS3 are required for nuclear translocation
    • Lee, K. H., Moon, K. J., Kim, H. S., Yoo, B. C., Park, S., Lee, H., Kwon, S., Lee, E. S., and Yoon, S. (2008) Increased cytoplasmic levels of CIS, SOCS1, SOCS2, or SOCS3 are required for nuclear translocation. FEBS Lett. 582, 2319-2324
    • (2008) FEBS Lett , vol.582 , pp. 2319-2324
    • Lee, K.H.1    Moon, K.J.2    Kim, H.S.3    Yoo, B.C.4    Park, S.5    Lee, H.6    Kwon, S.7    Lee, E.S.8    Yoon, S.9
  • 28
    • 0037462735 scopus 로고    scopus 로고
    • The cytokine-inducible Scr homology domain-containing protein negatively regulates signaling by promoting apoptosis in erythroid progenitor cells
    • Ketteler, R., Moghraby, C. S., Hsiao, J. G., Sandra, O., Lodish, H. F., and Klingmuller, U. (2003) The cytokine-inducible Scr homology domain-containing protein negatively regulates signaling by promoting apoptosis in erythroid progenitor cells. J. Biol. Chem. 278, 2654-2660
    • (2003) J. Biol. Chem , vol.278 , pp. 2654-2660
    • Ketteler, R.1    Moghraby, C.S.2    Hsiao, J.G.3    Sandra, O.4    Lodish, H.F.5    Klingmuller, U.6
  • 29
    • 0027365762 scopus 로고
    • Nuclear localization signals (NLS)
    • Boulikas, T. (1993) Nuclear localization signals (NLS). Crit. Rev. Eukaryot. Gene Expr. 3, 193-227
    • (1993) Crit. Rev. Eukaryot. Gene Expr , vol.3 , pp. 193-227
    • Boulikas, T.1
  • 30
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
    • Conti, E., Uy, M., Leighton, L., Blobel, G., and Kuriyan, J. (1998) Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell 94, 193-204
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 31
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D., Kutay, U. (1999) Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 607-660
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 32
    • 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
    • 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
    • (2007) Structure , vol.15 , pp. 1493-1504
    • Bullock, A.N.1    Rodriguez, M.C.2    Debreczeni, J.E.3    Songyang, Z.4    Knapp, S.5
  • 33
    • 4844219763 scopus 로고    scopus 로고
    • Regulated proteolysis of the IFNaR2 subunit of the interferon-alpha receptor
    • Saleh, A. Z., Fang, A. T., Arch, A. E., Neupane, D., El Fiky, A., and Krolewski, J. J. (2004) Regulated proteolysis of the IFNaR2 subunit of the interferon-alpha receptor. Oncogene 23, 7076-7086
    • (2004) Oncogene , vol.23 , pp. 7076-7086
    • Saleh, A.Z.1    Fang, A.T.2    Arch, A.E.3    Neupane, D.4    El Fiky, A.5    Krolewski, J.J.6
  • 34
    • 10044228385 scopus 로고    scopus 로고
    • The IFNAR1 subunit of the type I IFN receptor complex contains a functional nuclear localization sequence
    • Subramaniam, P. S., Johnson, H. M. (2004) The IFNAR1 subunit of the type I IFN receptor complex contains a functional nuclear localization sequence. FEBS Lett. 578, 207-210
    • (2004) FEBS Lett , vol.578 , pp. 207-210
    • Subramaniam, P.S.1    Johnson, H.M.2
  • 35
    • 33745320296 scopus 로고    scopus 로고
    • IFN-γ and its receptor subunit IFNGR1 are recruited to the IFN-γ-activated sequence element at the promoter site of IFN-γ-activated genes: Evidence of transactivational activity in IFNGR1
    • Ahmed, C. M. I., Johnson, H. M. (2006) IFN-γ and its receptor subunit IFNGR1 are recruited to the IFN-γ-activated sequence element at the promoter site of IFN-γ-activated genes: evidence of transactivational activity in IFNGR1. J. Immunol. 177, 315-321
    • (2006) J. Immunol , vol.177 , pp. 315-321
    • Ahmed, C.M.I.1    Johnson, H.M.2
  • 36
    • 0000413462 scopus 로고    scopus 로고
    • Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
    • Kim, T. K., Maniatis, T. (1996) Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273, 1717-1719
    • (1996) Science , vol.273 , pp. 1717-1719
    • Kim, T.K.1    Maniatis, T.2
  • 37
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon- mediated signalling
    • Platanias, L. C. (2005) Mechanisms of type-I- and type-II-interferon- mediated signalling. Nat. Rev. Immunol. 5, 375-386
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 39
    • 0033454739 scopus 로고    scopus 로고
    • Regulation of intercellular adhesion molecule-1 (CD54) gene expression
    • Roebuck, K. A., Finnegan, A. (1999) Regulation of intercellular adhesion molecule-1 (CD54) gene expression. J. Leukoc. Biol. 66, 876-888
    • (1999) J. Leukoc. Biol , vol.66 , pp. 876-888
    • Roebuck, K.A.1    Finnegan, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.