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Volumn 36, Issue 5, 2008, Pages 858-863

Fos family protein degradation by the proteasome

Author keywords

Activator protein 1 (AP 1); c Fos; Fra 1; Proteasome; Protein degradation; Ubiquitin

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEASOME; PROTEIN C FOS; PROTEIN FOS; TRANSCRIPTION FACTOR FOSB; TRANSCRIPTION FACTOR FRA 1; TRANSCRIPTION FACTOR FRA 2;

EID: 53849104631     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST0360858     Document Type: Conference Paper
Times cited : (29)

References (53)
  • 1
    • 0035971433 scopus 로고    scopus 로고
    • Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity
    • Chinenov, Y. and Kerppola, T.K. (2001) Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity. Oncogene 20, 2438-2452
    • (2001) Oncogene , vol.20 , pp. 2438-2452
    • Chinenov, Y.1    Kerppola, T.K.2
  • 2
    • 0035971563 scopus 로고    scopus 로고
    • AP-1 proteins in the adult brain: Facts and fiction about effectors of neuroprotection and neurodegeneration
    • Herdegen, T. and Waetzig, V. (2001) AP-1 proteins in the adult brain: facts and fiction about effectors of neuroprotection and neurodegeneration. Oncogene 20, 2424-2437
    • (2001) Oncogene , vol.20 , pp. 2424-2437
    • Herdegen, T.1    Waetzig, V.2
  • 3
    • 12344252237 scopus 로고    scopus 로고
    • AP-1 subunits: Quarrel and harmony among siblings
    • Hess, J., Angel, P. and Schorpp-Kistner, M. (2004) AP-1 subunits: quarrel and harmony among siblings. J. Cell Sci. 117, 5965-5973
    • (2004) J. Cell Sci , vol.117 , pp. 5965-5973
    • Hess, J.1    Angel, P.2    Schorpp-Kistner, M.3
  • 4
    • 0035971432 scopus 로고    scopus 로고
    • AP-1 in mouse development and tumorigenesis
    • Jochum, W., Passegue, E. and Wagner, E.F. (2001) AP-1 in mouse development and tumorigenesis. Oncogene 20, 2401-2412
    • (2001) Oncogene , vol.20 , pp. 2401-2412
    • Jochum, W.1    Passegue, E.2    Wagner, E.F.3
  • 5
    • 0035971517 scopus 로고    scopus 로고
    • The mammalian Jun proteins: Redundancy and specificity
    • Mechta-Grigoriou, F., Gerald, D. and Yaniv, M. (2001) The mammalian Jun proteins: redundancy and specificity. Oncogene 20, 2378-2389
    • (2001) Oncogene , vol.20 , pp. 2378-2389
    • Mechta-Grigoriou, F.1    Gerald, D.2    Yaniv, M.3
  • 6
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian, E. and Karin, M. (2002) AP-1 as a regulator of cell life and death. Nat. Cell Biol. 4, E131-E136
    • (2002) Nat. Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 7
    • 28544434439 scopus 로고    scopus 로고
    • (200S) Fos/AP-1 proteins in bone and the immune system
    • Wagner, E.F. and Eferl, R. (200S) Fos/AP-1 proteins in bone and the immune system. Immunol. Rev. 208, 126-140
    • Immunol. Rev , vol.208 , pp. 126-140
    • Wagner, E.F.1    Eferl, R.2
  • 8
    • 27544468372 scopus 로고    scopus 로고
    • The Fos family of transcription factors and their role in tumourigenesis
    • Milde-Langosch, K. (2005) The Fos family of transcription factors and their role in tumourigenesis. Eur. J. Cancer 41, 2449-2461
    • (2005) Eur. J. Cancer , vol.41 , pp. 2449-2461
    • Milde-Langosch, K.1
  • 9
    • 0035971496 scopus 로고    scopus 로고
    • Distinct roles of Jun:fos and Jun:ATF dinners in oncogenesis
    • van Dam, H. and Castellazzi, M. (2001) Distinct roles of Jun:fos and Jun:ATF dinners in oncogenesis. Oncogene 20, 2453-2464
    • (2001) Oncogene , vol.20 , pp. 2453-2464
    • van Dam, H.1    Castellazzi, M.2
  • 10
    • 33747361621 scopus 로고    scopus 로고
    • Fra-1 a target for cancer prevention or intervention
    • Young, M.R. and Colburn, N.H. (2006) Fra-1 a target for cancer prevention or intervention. Gene 379, 1-11
    • (2006) Gene , vol.379 , pp. 1-11
    • Young, M.R.1    Colburn, N.H.2
  • 11
    • 0242691046 scopus 로고    scopus 로고
    • AP-1: A double-edged sword in tumorigenesis
    • Eferl, R. and Wagner, E.F. (2003) AP-1: a double-edged sword in tumorigenesis. Nat. Rev. Cancer 3, 859-868
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 859-868
    • Eferl, R.1    Wagner, E.F.2
  • 13
    • 0026328851 scopus 로고
    • 1 transition in mouse fibroblasts: In vitro and in vivo associations
    • 1 transition in mouse fibroblasts: in vitro and in vivo associations. Mal. Cell. Biol. 11, 2451-2459
    • (1991) Mal. Cell. Biol , vol.11 , pp. 2451-2459
    • Kovary, K.1    Bravo, R.2
  • 14
    • 0026686624 scopus 로고
    • 1 transition and during exponential growth in mouse fibroblasts: Differential role of Fos proteins
    • 1 transition and during exponential growth in mouse fibroblasts: differential role of Fos proteins. Mol. Cell. Biol. 12, 5015-5023
    • (1992) Mol. Cell. Biol , vol.12 , pp. 5015-5023
    • Kovary, K.1    Bravo, R.2
  • 15
    • 0031039206 scopus 로고    scopus 로고
    • Variations in Jun and Fos protein expression and AP-1 activity in cycling, resting and stimulated fibroblasts
    • Lallemand, D., Spyrou, G., Yaniv, M. and Pfarr, C.M. (1997) Variations in Jun and Fos protein expression and AP-1 activity in cycling, resting and stimulated fibroblasts. Oncogene 14, 819-830
    • (1997) Oncogene , vol.14 , pp. 819-830
    • Lallemand, D.1    Spyrou, G.2    Yaniv, M.3    Pfarr, C.M.4
  • 16
    • 0029058440 scopus 로고
    • Transcriptional activation of the fro-1 gene by AP-1 is mediated by regulatory sequences in the first intron
    • Bergers, G., Graninger, P., Braselmann, S., Wrighton, C. and Busslinger, M. (1995) Transcriptional activation of the fro-1 gene by AP-1 is mediated by regulatory sequences in the first intron. Mol. Cell. Biol. 15, 3748-3758
    • (1995) Mol. Cell. Biol , vol.15 , pp. 3748-3758
    • Bergers, G.1    Graninger, P.2    Braselmann, S.3    Wrighton, C.4    Busslinger, M.5
  • 18
    • 0347628826 scopus 로고    scopus 로고
    • Rhabdomyosarcoma development in mice lacking Trp53 and Fos: Tumor suppression by the Fos protooncogene
    • Fleischmann A., Jochum, W., Eferl, R., Witowsky, J. and Wagner, F.F. (2003) Rhabdomyosarcoma development in mice lacking Trp53 and Fos: tumor suppression by the Fos protooncogene. Cancer Cell 4, 477-482
    • (2003) Cancer Cell , vol.4 , pp. 477-482
    • Fleischmann, A.1    Jochum, W.2    Eferl, R.3    Witowsky, J.4    Wagner, F.F.5
  • 20
    • 0346882607 scopus 로고    scopus 로고
    • Elevated ERK-MAP kinase activity protects the FOS family member FRA-1 against proteasomal degradation in colon carcinoma cells
    • Vial, E. and Marshall, C.J. (2003) Elevated ERK-MAP kinase activity protects the FOS family member FRA-1 against proteasomal degradation in colon carcinoma cells. J. Cell Sci. 116, 4957-4963
    • (2003) J. Cell Sci , vol.116 , pp. 4957-4963
    • Vial, E.1    Marshall, C.J.2
  • 21
    • 14844290887 scopus 로고    scopus 로고
    • FRA-1 expression level regulates proliferation and invasiveness of breast cancer cells
    • Belguise, K., Kersual, N., Galtier, F. and Chalbos, D. (2005) FRA-1 expression level regulates proliferation and invasiveness of breast cancer cells. Oncogene 24, 1434-1444
    • (2005) Oncogene , vol.24 , pp. 1434-1444
    • Belguise, K.1    Kersual, N.2    Galtier, F.3    Chalbos, D.4
  • 22
    • 34247198505 scopus 로고    scopus 로고
    • Fra-1 promotes growth and survival in RAS-transformed thyroid cells by controlling cyclin A transcription
    • Casalino, L., Bakiri, L., Talotta, F., Weitzman, J.B., Fusco, A., Yaniv, M. and Verde, P. (2007) Fra-1 promotes growth and survival in RAS-transformed thyroid cells by controlling cyclin A transcription. EMBO J. 26, 1878-1890
    • (2007) EMBO J , vol.26 , pp. 1878-1890
    • Casalino, L.1    Bakiri, L.2    Talotta, F.3    Weitzman, J.B.4    Fusco, A.5    Yaniv, M.6    Verde, P.7
  • 23
    • 33646336602 scopus 로고    scopus 로고
    • MAPK signal specificity: The right place at the right time
    • Murphy, L.O. and Blenis, J. (2006) MAPK signal specificity: the right place at the right time. Trends Biochem. Sci. 31, 268-275
    • (2006) Trends Biochem. Sci , vol.31 , pp. 268-275
    • Murphy, L.O.1    Blenis, J.2
  • 24
    • 0345736001 scopus 로고    scopus 로고
    • Regulation of c-Fos and Fra-1 by the MEK5-ERK5 pathway
    • Terasawa, K., Okazaki, K. and Nishida, E. (2003) Regulation of c-Fos and Fra-1 by the MEK5-ERK5 pathway. Genes Cells 8, 263-273
    • (2003) Genes Cells , vol.8 , pp. 263-273
    • Terasawa, K.1    Okazaki, K.2    Nishida, E.3
  • 25
    • 0028108504 scopus 로고
    • Regulation of Fra-1 and Fra-2 phosphorylation differs during the cell cycle of fibroblasts and phosphorylation in vitro by MAP kinase affects DNA binding activity
    • Gruda, M.C., Kovary, K., Metz, R. and Bravo, R. (1994) Regulation of Fra-1 and Fra-2 phosphorylation differs during the cell cycle of fibroblasts and phosphorylation in vitro by MAP kinase affects DNA binding activity. Oncogene 9, 2537-2547
    • (1994) Oncogene , vol.9 , pp. 2537-2547
    • Gruda, M.C.1    Kovary, K.2    Metz, R.3    Bravo, R.4
  • 26
    • 0027361017 scopus 로고
    • Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal 56 kinase
    • Chen, R.H., Abate, C. and Blenis, J. (1993) Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal 56 kinase. Proc. Natl. Acad. Sci. U.S.A. 90, 10952-10956
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 10952-10956
    • Chen, R.H.1    Abate, C.2    Blenis, J.3
  • 27
    • 0029937701 scopus 로고    scopus 로고
    • Phosphorylation of c-Fos at the C-terminus enhances its transforming activity
    • Chen, R.H., Juo, P.C., Curran, T. and Blenis, J. (1996) Phosphorylation of c-Fos at the C-terminus enhances its transforming activity. Oncogene 12, 1493-1502
    • (1996) Oncogene , vol.12 , pp. 1493-1502
    • Chen, R.H.1    Juo, P.C.2    Curran, T.3    Blenis, J.4
  • 29
    • 0028787249 scopus 로고
    • The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki, K. and Sagata, N. (1995) The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J. 14, 5048-5059
    • (1995) EMBO J , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 30
    • 0141781040 scopus 로고    scopus 로고
    • Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor
    • Monje, P., Marinissen, M.J. and Gutkind, J.S. (2003) Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor. Mol. Cell. Biol. 23, 7030-7043
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7030-7043
    • Monje, P.1    Marinissen, M.J.2    Gutkind, J.S.3
  • 31
    • 27444440554 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1
    • Monje, P., Hernandez-Losa, J., Lyons, R.J., Castellone, M.D. and Gutkind, J.S. (2005) Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1. J. Biol. Chem. 280, 35081-35084
    • (2005) J. Biol. Chem , vol.280 , pp. 35081-35084
    • Monje, P.1    Hernandez-Losa, J.2    Lyons, R.J.3    Castellone, M.D.4    Gutkind, J.S.5
  • 32
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy, L.O., Smith, S., Chen, R.H., Fingar, D.C. and Blenis, J. (2002) Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 4, 556-564
    • (2002) Nat. Cell Biol , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 33
    • 0037435037 scopus 로고    scopus 로고
    • The structural determinants responsible for c-Fos protein proteasomal degradation differ according to the conditions of expression
    • Ferrara, P., Andermarcher, E., Bossis, G., Acquaviva, C., Brockly, F., Jariel-Encontre, I. and Piechaczyk, M. (2003) The structural determinants responsible for c-Fos protein proteasomal degradation differ according to the conditions of expression. Oncogene 22, 1461-1474
    • (2003) Oncogene , vol.22 , pp. 1461-1474
    • Ferrara, P.1    Andermarcher, E.2    Bossis, G.3    Acquaviva, C.4    Brockly, F.5    Jariel-Encontre, I.6    Piechaczyk, M.7
  • 34
    • 0032931259 scopus 로고    scopus 로고
    • 1 phase of the cell cycle is determined by the duration of mitogen-activated protein kinase activation
    • 1 phase of the cell cycle is determined by the duration of mitogen-activated protein kinase activation. Mol. Cell. Biol. 19, 330-341
    • (1999) Mol. Cell. Biol , vol.19 , pp. 330-341
    • Cook, S.J.1    Aziz, N.2    McMahon, M.3
  • 35
    • 0031039113 scopus 로고    scopus 로고
    • Transformation by ras modifies AP1 composition and activity
    • Mechta, F., Lallemand, D., Pfaff, C.M. and Yaniv, M. (1997) Transformation by ras modifies AP1 composition and activity. Oncogene 14, 837-847
    • (1997) Oncogene , vol.14 , pp. 837-847
    • Mechta, F.1    Lallemand, D.2    Pfaff, C.M.3    Yaniv, M.4
  • 36
    • 0032959647 scopus 로고    scopus 로고
    • Activated MEK stimulates expression of AP-1 components independently of phosphatidylinositol 3-kinase (P13-kinase) but requires a P13-kinase signal to stimulate DNA synthesis
    • Treinies, I., Paterson, H.F., Hooper, S., Wilson, R. and Marshall, C.J. (1999) Activated MEK stimulates expression of AP-1 components independently of phosphatidylinositol 3-kinase (P13-kinase) but requires a P13-kinase signal to stimulate DNA synthesis. Mol- Cell. Biol. 19, 321-329
    • (1999) Mol- Cell. Biol , vol.19 , pp. 321-329
    • Treinies, I.1    Paterson, H.F.2    Hooper, S.3    Wilson, R.4    Marshall, C.J.5
  • 37
    • 0032560789 scopus 로고    scopus 로고
    • Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts
    • Salvat, C., Jariel-Encontre, I., Acquaviva, C., Omura, S. and Piechaczyk, M. (1998) Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts. Oncogene 17, 327-337
    • (1998) Oncogene , vol.17 , pp. 327-337
    • Salvat, C.1    Jariel-Encontre, I.2    Acquaviva, C.3    Omura, S.4    Piechaczyk, M.5
  • 38
    • 0141752762 scopus 로고    scopus 로고
    • c-Fos proto-oncoprotein is degraded by the proteasome independently of its own ubiquitinylation in vivo
    • Bossis, G., Ferrara, P., Acquaviva, C., Jariel-Encontre, I,. and Piechaczyk, M. (2003) c-Fos proto-oncoprotein is degraded by the proteasome independently of its own ubiquitinylation in vivo. Mol. Cell- Biol. 23, 7425-7436
    • (2003) Mol. Cell- Biol , vol.23 , pp. 7425-7436
    • Bossis, G.1    Ferrara, P.2    Acquaviva, C.3    Jariel-Encontre, I.4    Piechaczyk, M.5
  • 40
    • 13944267647 scopus 로고    scopus 로고
    • Mechanisms of delivery of ubiquitylated proteins to the proteasome: New target for anti-cancer therapy?
    • Farras, R., Bossis, G., Andermarcher, E., Jariel-Encontre, I. and Piechaczyk, M. (2005) Mechanisms of delivery of ubiquitylated proteins to the proteasome: new target for anti-cancer therapy? Crit. Rev. Oncol. Hematol. 54, 31-51
    • (2005) Crit. Rev. Oncol. Hematol , vol.54 , pp. 31-51
    • Farras, R.1    Bossis, G.2    Andermarcher, E.3    Jariel-Encontre, I.4    Piechaczyk, M.5
  • 41
    • 33749057086 scopus 로고    scopus 로고
    • Sasaki, T., Kojima, H., Kishimoto, R., Ikeda, A., Kunimoto, H. and Nakajima, K. (2006) Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role. Mal. Cell 24, 63-75
    • Sasaki, T., Kojima, H., Kishimoto, R., Ikeda, A., Kunimoto, H. and Nakajima, K. (2006) Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role. Mal. Cell 24, 63-75
  • 42
    • 0025130815 scopus 로고
    • Nuclear localization of c-Fos, but not v-Fos proteins, is controlled by extracellular signals
    • Roux, P., Blanchard, J.M., Fernandez, A., Lamb, N., Jeanteur, P. and Piechaczyk, M. (1990) Nuclear localization of c-Fos, but not v-Fos proteins, is controlled by extracellular signals. Cell 63, 341-351
    • (1990) Cell , vol.63 , pp. 341-351
    • Roux, P.1    Blanchard, J.M.2    Fernandez, A.3    Lamb, N.4    Jeanteur, P.5    Piechaczyk, M.6
  • 43
    • 34347345040 scopus 로고    scopus 로고
    • Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer
    • Basbous, J., Chalbos, D., Hipskind, R., Jariel-Encontre, I. and Piechaczyk, M. (2007) Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer. Mol. Cell. Biol. 27, 3936-3950
    • (2007) Mol. Cell. Biol , vol.27 , pp. 3936-3950
    • Basbous, J.1    Chalbos, D.2    Hipskind, R.3    Jariel-Encontre, I.4    Piechaczyk, M.5
  • 44
    • 0345732643 scopus 로고    scopus 로고
    • A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration
    • Murphy, L.O., MacKeigan, J.P. and Blenis, J. (2004) A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration. Mol. Cell. Biol. 24, 144-153
    • (2004) Mol. Cell. Biol , vol.24 , pp. 144-153
    • Murphy, L.O.1    MacKeigan, J.P.2    Blenis, J.3
  • 45
    • 0038655412 scopus 로고    scopus 로고
    • Accumulation of Fra-1 in Ras-transformed cells depends on both transcriptional autoregulation and MEK-dependent posttranslational stabilization
    • Casalino, L., De Cesare, D. and Verde, P. (2003) Accumulation of Fra-1 in Ras-transformed cells depends on both transcriptional autoregulation and MEK-dependent posttranslational stabilization. Mol. Cell. Biol. 23, 4401-4415
    • (2003) Mol. Cell. Biol , vol.23 , pp. 4401-4415
    • Casalino, L.1    De Cesare, D.2    Verde, P.3
  • 46
    • 0034646289 scopus 로고    scopus 로고
    • Campbell, K.M., Terrell, A.R., Laybourn, P.J. and Lumb, K.J. (2000) Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. Biochemistry 39, 2708-2713
    • Campbell, K.M., Terrell, A.R., Laybourn, P.J. and Lumb, K.J. (2000) Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. Biochemistry 39, 2708-2713
  • 47
    • 3242732010 scopus 로고    scopus 로고
    • Ubiquitin-free routes into the proteasome
    • Hoyt, M.A. and Coffino, P. (2004) Ubiquitin-free routes into the proteasome. Cell. Mol. Life Sci. 61, 1596-1600
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 1596-1600
    • Hoyt, M.A.1    Coffino, P.2
  • 48
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner, M. and Hill, C.P. (2005) Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15, 27-33
    • (2005) Trends Cell Biol , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 49
    • 15744393216 scopus 로고    scopus 로고
    • MEK1-dependent delayed expression of Fos-related antigen-1 counteracts c-Fos and p65 NF-κB-mediated interleukin-8 transcription in response to cytokines or growth factors
    • Hoffmann, E., Thiefes, A., Buhrow, D., Dittrich-Breiholz, O., Schneider, H., Resch, K. and Kracht, M. (2005) MEK1-dependent delayed expression of Fos-related antigen-1 counteracts c-Fos and p65 NF-κB-mediated interleukin-8 transcription in response to cytokines or growth factors. J. Biol. Chem. 280, 9706-9718
    • (2005) J. Biol. Chem , vol.280 , pp. 9706-9718
    • Hoffmann, E.1    Thiefes, A.2    Buhrow, D.3    Dittrich-Breiholz, O.4    Schneider, H.5    Resch, K.6    Kracht, M.7
  • 50
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund, K. and Dikic, I. (2005) Ubiquitylation and cell signaling. EMBO J. 24, 3353-3359
    • (2005) EMBO J , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 51
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • Schnell, J.D. and Hicke, L. (2003) Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J. Biol. Chem. 278, 35857-35860
    • (2003) J. Biol. Chem , vol.278 , pp. 35857-35860
    • Schnell, J.D.1    Hicke, L.2
  • 52
    • 0036134934 scopus 로고    scopus 로고
    • Transactivation of Fra-1 and consequent activation of AP-1 occur extracellular signal-regulated kinase dependently
    • Young, M.R., Nair, R., Bucheimer, N., Tulsian, P., Brown, N., Chapp, C., Hsu, T.C. and Colburn, N.H. (2002) Transactivation of Fra-1 and consequent activation of AP-1 occur extracellular signal-regulated kinase dependently. Mol. Cell. Biol. 22, 587-598
    • (2002) Mol. Cell. Biol , vol.22 , pp. 587-598
    • Young, M.R.1    Nair, R.2    Bucheimer, N.3    Tulsian, P.4    Brown, N.5    Chapp, C.6    Hsu, T.C.7    Colburn, N.H.8
  • 53
    • 56249108370 scopus 로고    scopus 로고
    • Jariel-Encontre, I., Bossis, G. and Piechaczyk, M. (2008) Ubiquitin-independent degradation of proteins by the proteasome. Biochim. Biophys. Acta, doi:10-1016/j.bbcan.2008.05.004
    • Jariel-Encontre, I., Bossis, G. and Piechaczyk, M. (2008) Ubiquitin-independent degradation of proteins by the proteasome. Biochim. Biophys. Acta, doi:10-1016/j.bbcan.2008.05.004


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