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Volumn 55, Issue 3, 2011, Pages 249-260

Regulation of cell fate determination by Skp1-Cullin1-F-box (SCF) E3 ubiquitin ligases

Author keywords

Differentiation; SCF; Signaling; Ubiquitylation; UPS

Indexed keywords

ATROGIN 1; CELL PROTEIN; F BOX PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN BETA TRCP; PROTEIN FBW2; PROTEIN FBW7; PROTEIN PPA; S PHASE KINASE ASSOCIATED PROTEIN 2; SONIC HEDGEHOG PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; WNT1 PROTEIN;

EID: 79959469863     PISSN: 02146282     EISSN: None     Source Type: Journal    
DOI: 10.1387/ijdb.103171ch     Document Type: Review
Times cited : (15)

References (148)
  • 1
    • 0030978351 scopus 로고    scopus 로고
    • Beta-catenin is a target for the ubiquitin-proteasome pathway
    • ABERLE, H., BAUER, A., STAPPERT, J., KISPERT, A. and KEMLER, R. (1997). beta-catenin is a target for the ubiquitin-proteasome pathway. EMBO J 16: 3797-3804.
    • (1997) EMBO J , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 2
    • 0029856301 scopus 로고    scopus 로고
    • The gcm-motif: A novel DNA-binding motif conserved in Drosophila and mammals
    • AKIYAMA, Y., HOSOYA, T., POOLE, A.M. and HOTTA, Y. (1996). The gcm-motif: a novel DNA-binding motif conserved in Drosophila and mammals. Proc Natl Acad Sci USA 93: 14912-14916.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14912-14916
    • Akiyama, Y.1    Hosoya, T.2    Poole, A.M.3    Hotta, Y.4
  • 3
    • 0028970734 scopus 로고
    • Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway
    • ALKALAY, I., YARON, A., HATZUBAI, A., ORIAN, A., CIECHANOVER, A. and BEN-NERIAH, Y. (1995). Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA 92: 10599-10603.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10599-10603
    • Alkalay, I.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 4
    • 76749161882 scopus 로고    scopus 로고
    • The F-box protein Cdc4/Fbxw7 is a novel regulator of neural crest development in Xenopus laevis
    • ALMEIDA, A., WISE, H., HINDLEY, C., SLEVIN, M., HARTLEY, R. and PHILPOTT, A. (2010). The F-box protein Cdc4/Fbxw7 is a novel regulator of neural crest development in Xenopus laevis. Neural Dev 5: 1.
    • (2010) Neural Dev , vol.5 , Issue.1
    • Almeida, A.1    Wise, H.2    Hindley, C.3    Slevin, M.4    Hartley, R.5    Philpott, A.6
  • 6
    • 19344375385 scopus 로고    scopus 로고
    • Interwoven Ubiquitination Oscillators and Control of Cell Cycle Transitions
    • ANG, X.L. and HARPER, J.W. (2004). Interwoven Ubiquitination Oscillators and Control of Cell Cycle Transitions. Sci STKE 2004: pe31.
    • (2004) Sci STKE , vol.2004
    • Ang, X.L.1    Harper, J.W.2
  • 7
    • 18344386695 scopus 로고    scopus 로고
    • SCF-mediated protein degradation and cell cycle control
    • ANG, X.L. and WADE HARPER, J. (2005). SCF-mediated protein degradation and cell cycle control. Oncogene 24: 2860-2870.
    • (2005) Oncogene , vol.24 , pp. 2860-2870
    • Ang, X.L.1    Wade Harper, J.2
  • 8
    • 0033935126 scopus 로고    scopus 로고
    • The glial cells missing-1 protein is essential for branching morphogenesis in the chorioallantoic placenta
    • ANSON-CARTWRIGHT, L., DAWSON, K., HOLMYARD, D., FISHER, S.J., LAZZARINI, R.A. and CROSS, J.C. (2000). The glial cells missing-1 protein is essential for branching morphogenesis in the chorioallantoic placenta. Nat Genet 25: 311-314.
    • (2000) Nat Genet , vol.25 , pp. 311-314
    • Anson-Cartwright, L.1    Dawson, K.2    Holmyard, D.3    Fisher, S.J.4    Lazzarini, R.A.5    Cross, J.C.6
  • 10
    • 3042787711 scopus 로고    scopus 로고
    • Identification of positive and negative regulatory regions controlling expression of the Xenopus laevis betaTrCP gene
    • BALLARINO, M., FRUSCALZO, A., MARCHIONI, M. and CARNEVALI, F. (2004). Identification of positive and negative regulatory regions controlling expression of the Xenopus laevis betaTrCP gene. Gene 336: 275-285.
    • (2004) Gene , vol.336 , pp. 275-285
    • Ballarino, M.1    Fruscalzo, A.2    Marchioni, M.3    Carnevali, F.4
  • 11
    • 0037136236 scopus 로고    scopus 로고
    • The Xenopus laevis beta TrCP gene: Genomic organization, alternative splicing, 5' and 3' region characterization and comparison of its structure with that of human beta TrCP genes
    • BALLARINO, M., MARCHIONI, M. and CARNEVALI, F. (2002). The Xenopus laevis beta TrCP gene: genomic organization, alternative splicing, 5' and 3' region characterization and comparison of its structure with that of human beta TrCP genes. Biochim Biophys Acta 1577: 81-92.
    • (2002) Biochim Biophys Acta , vol.1577 , pp. 81-92
    • Ballarino, M.1    Marchioni, M.2    Carnevali, F.3
  • 12
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase
    • BASHIR, T., DORRELLO, N.V., AMADOR, V., GUARDAVACCARO, D. and PAGANO, M. (2004). Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase. Nature 428: 190-193.
    • (2004) Nature , vol.428 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amador, V.3    Guardavaccaro, D.4    Pagano, M.5
  • 14
    • 0028916254 scopus 로고
    • Cactus protein degradation mediates Drosophila dorsal-ventral signaling
    • BELVIN, M.P., JIN, Y. and ANDERSON, K.V. (1995). Cactus protein degradation mediates Drosophila dorsal-ventral signaling. Genes Dev 9: 783-793.
    • (1995) Genes Dev , vol.9 , pp. 783-793
    • Belvin, M.P.1    Jin, Y.2    Anderson, K.V.3
  • 15
    • 38849187293 scopus 로고    scopus 로고
    • CDK Inhibitors: Cell Cycle Regulators and Beyond
    • BESSON, A., DOWDY, S.F. and ROBERTS, J.M. (2008). CDK Inhibitors: Cell Cycle Regulators and Beyond. Dev Cell 14: 159-169.
    • (2008) Dev Cell , vol.14 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 18
    • 38949123365 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase skp2 regulates neural differentiation independent from the cell cycle
    • BOIX-PERALES, H., HORAN, I., WISE, H., LIN, H.R., CHUANG, L.C., YEW, P.R. and PHILPOTT, A. (2007). The E3 ubiquitin ligase skp2 regulates neural differentiation independent from the cell cycle. Neural Dev 2: 27.
    • (2007) Neural Dev , vol.2 , Issue.27
    • Boix-Perales, H.1    Horan, I.2    Wise, H.3    Lin, H.R.4    Chuang, L.C.5    Yew, P.R.6    Philpott, A.7
  • 21
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • CARRANO, A.C., EYTAN, E., HERSHKO, A. and PAGANO, M. (1999). SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1: 193-199.
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 22
    • 76749100683 scopus 로고    scopus 로고
    • Regulation of p53 family member isoform DeltaNp63alpha by the nuclear factor-kappaB targeting kinase IkappaB kinase beta
    • CHATTERJEE, A., CHANG, X., SEN, T., RAVI, R., BEDI, A. and SIDRANSKY, D. (2010). Regulation of p53 family member isoform DeltaNp63alpha by the nuclear factor-kappaB targeting kinase IkappaB kinase beta. Cancer Res 70: 10.
    • (2010) Cancer Res , vol.70 , Issue.10
    • Chatterjee, A.1    Chang, X.2    Sen, T.3    Ravi, R.4    Bedi, A.5    Sidransky, D.6
  • 23
    • 0034685767 scopus 로고    scopus 로고
    • The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation
    • CHEN, A., WU, K., FUCHS, S.Y., TAN, P., GOMEZ, C. and PAN, Z.Q. (2000). The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation. J Biol Chem 275: 15432-15439.
    • (2000) J Biol Chem , vol.275 , pp. 15432-15439
    • Chen, A.1    Wu, K.2    Fuchs, S.Y.3    Tan, P.4    Gomez, C.5    Pan, Z.Q.6
  • 24
    • 55549085912 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation
    • CHIANG, M.H., CHEN, L.F. and CHEN, H. (2008). Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation. Biol Reprod 79: 914-920.
    • (2008) Biol Reprod , vol.79 , pp. 914-920
    • Chiang, M.H.1    Chen, L.F.2    Chen, H.3
  • 26
    • 0019225640 scopus 로고
    • Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes
    • CIECHANOVER, A., ELIAS, S., HELLER, H., FERBER, S. and HERSHKO, A. (1980a). Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes. J Biol Chem 255: 7525-7528.
    • (1980) J Biol Chem , vol.255 , pp. 7525-7528
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Ferber, S.4    Hershko, A.5
  • 27
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • CIECHANOVER, A., FINLEY, D. and VARSHAVSKY, A. (1984). Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37: 57-66.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 28
    • 0018992813 scopus 로고
    • ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • CIECHANOVER, A., HELLER, H., ELIAS, S., HAAS, A.L. and HERSHKO, A. (1980b). ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc Natl Acad Sci USA 77: 1365-1368.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3    Haas, A.L.4    Hershko, A.5
  • 29
    • 0023663888 scopus 로고
    • Expression of a single transfected cDNA converts fibroblasts to myoblasts
    • DAVIS, R.L., WEINTRAUB, H. and LASSAR, A.B. (1987). Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 51: 987-1000.
    • (1987) Cell , vol.51 , pp. 987-1000
    • Davis, R.L.1    Weintraub, H.2    Lassar, A.B.3
  • 30
    • 67649964217 scopus 로고    scopus 로고
    • RING domain E3 ubiquitin ligases
    • DESHAIES, R.J. and JOAZEIRO, C.A. (2009). RING domain E3 ubiquitin ligases. Annu Rev Biochem 78: 399-434.
    • (2009) Annu Rev Biochem , vol.78 , pp. 399-434
    • Deshaies, R.J.1    Joazeiro, C.A.2
  • 31
    • 50449108516 scopus 로고    scopus 로고
    • Structural Insights into NEDD8 Activation of Cullin- RING Ligases: Conformational Control of Conjugation
    • DUDA, D.M., BORG, L.A., SCOTT, D.C., HUNT, H.W., HAMMEL, M. and SCHULMAN, B.A. (2008). Structural Insights into NEDD8 Activation of Cullin- RING Ligases: Conformational Control of Conjugation. Cell 134: 995-1006.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 32
    • 0029840669 scopus 로고    scopus 로고
    • Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila
    • DUSHAY, M.S., ASLING, B. and HULTMARK, D. (1996). Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila. Proc Natl Acad Sci USA 93: 10343-10347.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10343-10347
    • Dushay, M.S.1    Asling, B.2    Hultmark, D.3
  • 33
    • 0033602475 scopus 로고    scopus 로고
    • HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and betacatenin
    • FUCHS, S.Y., CHEN, A., XIONG, Y., PAN, Z.Q. and RONAI, Z. (1999). HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and betacatenin. Oncogene 18: 2039-2046.
    • (1999) Oncogene , vol.18 , pp. 2039-2046
    • Fuchs, S.Y.1    Chen, A.2    Xiong, Y.3    Pan, Z.Q.4    Ronai, Z.5
  • 34
    • 1942502180 scopus 로고    scopus 로고
    • The many faces of beta-TrCP E3 ubiquitin ligases: Reflections in the magic mirror of cancer
    • FUCHS, S.Y., SPIEGELMAN, V.S. and KUMAR, K.G. (2004). The many faces of beta-TrCP E3 ubiquitin ligases: reflections in the magic mirror of cancer. Oncogene 23: 2028-2036.
    • (2004) Oncogene , vol.23 , pp. 2028-2036
    • Fuchs, S.Y.1    Spiegelman, V.S.2    Kumar, K.G.3
  • 35
    • 0037013260 scopus 로고    scopus 로고
    • Activation of UBC5 ubiquitinconjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins
    • FURUKAWA, M., OHTA, T. and XIONG, Y. (2002). Activation of UBC5 ubiquitinconjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins. J Biol Chem 277: 15758-15765.
    • (2002) J Biol Chem , vol.277 , pp. 15758-15765
    • Furukawa, M.1    Ohta, T.2    Xiong, Y.3
  • 36
    • 0037143725 scopus 로고    scopus 로고
    • The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis
    • GAGNE, J.M., DOWNES, B.P., SHIU, S.H., DURSKI, A.M. and VIERSTRA, R.D. (2002). The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis. Proc Natl Acad Sci USA 99: 11519-11524.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11519-11524
    • Gagne, J.M.1    Downes, B.P.2    Shiu, S.H.3    Durski, A.M.4    Vierstra, R.D.5
  • 38
    • 0026486817 scopus 로고
    • Cactus, a gene involved in dorsoventral pattern formation of Drosophila, is related to the I kappa B gene family of vertebrates
    • GEISLER, R., BERGMANN, A., HIROMI, Y. and NUSSLEIN-VOLHARD, C. (1992). cactus, a gene involved in dorsoventral pattern formation of Drosophila, is related to the I kappa B gene family of vertebrates. Cell 71: 613-621.
    • (1992) Cell , vol.71 , pp. 613-621
    • Geisler, R.1    Bergmann, A.2    Hiromi, Y.3    Nusslein-Volhard, C.4
  • 39
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • GOMES, M.D., LECKER, S.H., JAGOE, R.T., NAVON, A. and GOLDBERG, A.L. (2001). Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci USA 98: 14440-14445.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 41
    • 10644225068 scopus 로고    scopus 로고
    • Identification and characterization of the IKKalpha promoter: Positive and negative regulation by ETS-1 and p53, respectively
    • GU, L., ZHU, N., FINDLEY, H.W., WOODS, W.G. and ZHOU, M. (2004). Identification and characterization of the IKKalpha promoter: positive and negative regulation by ETS-1 and p53, respectively. J Biol Chem 279: 52141-52149.
    • (2004) J Biol Chem , vol.279 , pp. 52141-52149
    • Gu, L.1    Zhu, N.2    Findley, H.W.3    Woods, W.G.4    Zhou, M.5
  • 44
    • 0035860804 scopus 로고    scopus 로고
    • Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor
    • GUPTA-ROSSI, N., LE BAIL, O., GONEN, H., BROU, C., LOGEAT, F., SIX, E., CIECHANOVER, A. and ISRAEL, A. (2001). Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor. J Biol Chem 276: 34371-34378.
    • (2001) J Biol Chem , vol.276 , pp. 34371-34378
    • Gupta-Rossi, N.1    le Bail, O.2    Gonen, H.3    Brou, C.4    Logeat, F.5    Six, E.6    Ciechanover, A.7    Israel, A.8
  • 46
    • 0024299087 scopus 로고
    • The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein
    • HASHIMOTO, C., HUDSON, K.L. and ANDERSON, K.V. (1988). The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein. Cell 52: 269-279.
    • (1988) Cell , vol.52 , pp. 269-279
    • Hashimoto, C.1    Hudson, K.L.2    Anderson, K.V.3
  • 47
    • 0026523562 scopus 로고
    • Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-kappa B subunit
    • HENKEL, T., ZABEL, U., VAN ZEE, K., MULLER, J.M., FANNING, E. and BAEUERLE, P.A. (1992). Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-kappa B subunit. Cell 68: 1121-1133.
    • (1992) Cell , vol.68 , pp. 1121-1133
    • Henkel, T.1    Zabel, U.2    van Zee, K.3    Muller, J.M.4    Fanning, E.5    Baeuerle, P.A.6
  • 48
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: Conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis
    • HERSHKO, A., CIECHANOVER, A., HELLER, H., HAAS, A.L. and ROSE, I.A. (1980). Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci USA 77: 1783-1786.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 49
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • HERSHKO, A., HELLER, H., ELIAS, S. and CIECHANOVER, A. (1983). Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem 258: 8206-8214.
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 52
    • 16244373679 scopus 로고    scopus 로고
    • Multiubiquitylation by E4 enzymes: [']one size' doesn't fit all
    • HOPPE, T. (2005). Multiubiquitylation by E4 enzymes: [']one size' doesn't fit all. Trends Biochem Sci 30: 183-187.
    • (2005) Trends Biochem Sci , vol.30 , pp. 183-187
    • Hoppe, T.1
  • 53
    • 0029087476 scopus 로고
    • Glial cells missing: A binary switch between neuronal and glial determination in Drosophila
    • HOSOYA, T., TAKIZAWA, K., NITTA, K. and HOTTA, Y. (1995). glial cells missing: a binary switch between neuronal and glial determination in Drosophila. Cell 82: 1025-1036.
    • (1995) Cell , vol.82 , pp. 1025-1036
    • Hosoya, T.1    Takizawa, K.2    Nitta, K.3    Hotta, Y.4
  • 55
    • 0033537767 scopus 로고    scopus 로고
    • Abnormal morphogenesis but intact IKK activation in mice lacking the IKKalpha subunit of IkappaB kinase
    • HU, Y., BAUD, V., DELHASE, M., ZHANG, P., DEERINCK, T., ELLISMAN, M., JOHNSON, R. and KARIN, M. (1999). Abnormal morphogenesis but intact IKK activation in mice lacking the IKKalpha subunit of IkappaB kinase. Science 284: 316-320.
    • (1999) Science , vol.284 , pp. 316-320
    • Hu, Y.1    Baud, V.2    Delhase, M.3    Zhang, P.4    Deerinck, T.5    Ellisman, M.6    Johnson, R.7    Karin, M.8
  • 56
    • 0030659821 scopus 로고    scopus 로고
    • Sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins
    • HUBBARD, E.J., WU, G., KITAJEWSKI, J. and GREENWALD, I. (1997). sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins. Genes Dev 11: 3182-3193.
    • (1997) Genes Dev , vol.11 , pp. 3182-3193
    • Hubbard, E.J.1    Wu, G.2    Kitajewski, J.3    Greenwald, I.4
  • 57
    • 77149120798 scopus 로고    scopus 로고
    • N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals
    • HWANG, C.-S., SHEMORRY, A. and VARSHAVSKY, A. (2010). N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals. Science 327: 973-977.
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.-S.1    Shemorry, A.2    Varshavsky, A.3
  • 58
    • 0033576547 scopus 로고    scopus 로고
    • Localization of membrane-associated guanylate kinase (MAGI)-1/BAI-associated protein (BAP) 1 at tight junctions of epithelial cells
    • IDE, N., HATA, Y., NISHIOKA, H., HIRAO, K., YAO, I., DEGUCHI, M., MIZOGUCHI, A., NISHIMORI, H., TOKINO, T., NAKAMURA, Y. et al. (1999). Localization of membrane-associated guanylate kinase (MAGI)-1/BAI-associated protein (BAP) 1 at tight junctions of epithelial cells. Oncogene 18: 7810-7815.
    • (1999) Oncogene , vol.18 , pp. 7810-7815
    • Ide, N.1    Hata, Y.2    Nishioka, H.3    Hirao, K.4    Yao, I.5    Deguchi, M.6    Mizoguchi, A.7    Nishimori, H.8    Tokino, T.9    Nakamura, Y.10
  • 59
    • 0035577854 scopus 로고    scopus 로고
    • Hedgehog signaling in animal development: Paradigms and principles
    • INGHAM, P.W. and MCMAHON, A.P. (2001). Hedgehog signaling in animal development: paradigms and principles. Genes Dev 15: 3059-3087.
    • (2001) Genes Dev , vol.15 , pp. 3059-3087
    • Ingham, P.W.1    McMahon, A.P.2
  • 60
    • 33750200389 scopus 로고    scopus 로고
    • Orchestrating ontogenesis: Variations on a theme by sonic hedgehog
    • INGHAM, P.W. and PLACZEK, M. (2006). Orchestrating ontogenesis: variations on a theme by sonic hedgehog. Nat Rev Genet 7: 841-850.
    • (2006) Nat Rev Genet , vol.7 , pp. 841-850
    • Ingham, P.W.1    Placzek, M.2
  • 62
    • 70350036218 scopus 로고    scopus 로고
    • A novel role of the glial fate determinant glial cells missing in hematopoiesis
    • JACQUES, C., SOUSTELLE, L., NAGY, I., DIEBOLD, C. and GIANGRANDE, A. (2009). A novel role of the glial fate determinant glial cells missing in hematopoiesis. Int J Dev Biol 53: 1013-1022.
    • (2009) Int J Dev Biol , vol.53 , pp. 1013-1022
    • Jacques, C.1    Soustelle, L.2    Nagy, I.3    Diebold, C.4    Giangrande, A.5
  • 63
    • 34249819663 scopus 로고    scopus 로고
    • F-box proteins in rice. Genome-wide analysis, classification, temporal and spatial gene expression during panicle and seed development, and regulation by light and abiotic stress
    • JAIN, M., NIJHAWAN, A., ARORA, R., AGARWAL, P., RAY, S., SHARMA, P., KAPOOR, S., TYAGI, A.K. and KHURANA, J.P. (2007). F-box proteins in rice. Genome-wide analysis, classification, temporal and spatial gene expression during panicle and seed development, and regulation by light and abiotic stress. Plant Physiol 143: 1467-1483.
    • (2007) Plant Physiol , vol.143 , pp. 1467-1483
    • Jain, M.1    Nijhawan, A.2    Arora, R.3    Agarwal, P.4    Ray, S.5    Sharma, P.6    Kapoor, S.7    Tyagi, A.K.8    Khurana, J.P.9
  • 64
    • 28444449828 scopus 로고    scopus 로고
    • Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus interruptus for Slimb/beta-TRCP-mediated proteolytic processing
    • JIA, J., ZHANG, L., ZHANG, Q., TONG, C., WANG, B., HOU, F., AMANAI, K. and JIANG, J. (2005). Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus interruptus for Slimb/beta-TRCP-mediated proteolytic processing. Dev Cell 9: 819-830.
    • (2005) Dev Cell , vol.9 , pp. 819-830
    • Jia, J.1    Zhang, L.2    Zhang, Q.3    Tong, C.4    Wang, B.5    Hou, F.6    Amanai, K.7    Jiang, J.8
  • 65
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb
    • JIANG, J. and STRUHL, G. (1998). Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb. Nature 391: 493-496.
    • (1998) Nature , vol.391 , pp. 493-496
    • Jiang, J.1    Struhl, G.2
  • 66
    • 0347361537 scopus 로고    scopus 로고
    • SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase
    • JIN, J., SHIROGANE, T., XU, L., NALEPA, G., QIN, J., ELLEDGE, S.J. and HARPER, J.W. (2003). SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase. Genes Dev 17: 3062-3074.
    • (2003) Genes Dev , vol.17 , pp. 3062-3074
    • Jin, J.1    Shirogane, T.2    Xu, L.3    Nalepa, G.4    Qin, J.5    Elledge, S.J.6    Harper, J.W.7
  • 67
    • 69249222488 scopus 로고    scopus 로고
    • Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase
    • JOGO, M., SHIRAISHI, S. and TAMURA, T.-A. (2009). Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase. FEBS Lett 583: 2715-2719.
    • (2009) FEBS Lett , vol.583 , pp. 2715-2719
    • Jogo, M.1    Shiraishi, S.2    Tamura, T.-A.3
  • 68
    • 0029084787 scopus 로고
    • Glial cells missing: A genetic switch that controls glial versus neuronal fate
    • JONES, B.W., FETTER, R.D., TEAR, G. and GOODMAN, C.S. (1995). Glial cells missing: a genetic switch that controls glial versus neuronal fate. Cell 82: 1013-1023.
    • (1995) Cell , vol.82 , pp. 1013-1023
    • Jones, B.W.1    Fetter, R.D.2    Tear, G.3    Goodman, C.S.4
  • 71
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • KARIN, M. and BEN-NERIAH, Y. (2000). Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 18: 621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 72
    • 4344656718 scopus 로고    scopus 로고
    • Auxin-induced SCFTIR1-Aux/IAA interaction involves stable modification of the SCFTIR1 complex
    • KEPINSKI, S. and LEYSER, O. (2004). Auxin-induced SCFTIR1-Aux/IAA interaction involves stable modification of the SCFTIR1 complex. Proc Natl Acad Sci USA 101: 12381-12386.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12381-12386
    • Kepinski, S.1    Leyser, O.2
  • 73
    • 0032514757 scopus 로고    scopus 로고
    • Isolation and characterization of mammalian homologs of the Drosophila gene glial cells missing
    • KIM, J., JONES, B.W., ZOCK, C., CHEN, Z., WANG, H., GOODMAN, C.S. and ANDERSON, D.J. (1998). Isolation and characterization of mammalian homologs of the Drosophila gene glial cells missing. Proc Natl Acad Sci USA 95: 12364-12369.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12364-12369
    • Kim, J.1    Jones, B.W.2    Zock, C.3    Chen, Z.4    Wang, H.5    Goodman, C.S.6    Anderson, D.J.7
  • 75
    • 38649108164 scopus 로고    scopus 로고
    • Skp2 suppresses p53-dependent apoptosis by inhibiting p300
    • KITAGAWA, M., LEE, S.H. and MCCORMICK, F. (2008). Skp2 suppresses p53-dependent apoptosis by inhibiting p300. Mol Cell 29: 217-231.
    • (2008) Mol Cell , vol.29 , pp. 217-231
    • Kitagawa, M.1    Lee, S.H.2    McCormick, F.3
  • 76
    • 21644477793 scopus 로고    scopus 로고
    • P63 and epithelial appendage development
    • KOSTER, M.I. and ROOP, D.R. (2004). P63 and epithelial appendage development. Differentiation 72: 364-370.
    • (2004) Differentiation , vol.72 , pp. 364-370
    • Koster, M.I.1    Roop, D.R.2
  • 77
    • 0036809968 scopus 로고    scopus 로고
    • Classification and expression analysis of Arabidopsis Fbox- containing protein genes
    • KURODA, H., TAKAHASHI, N., SHIMADA, H., SEKI, M., SHINOZAKI, K. and MATSUI, M. (2002). Classification and expression analysis of Arabidopsis Fbox- containing protein genes. Plant Cell Physiol 43: 1073-1085.
    • (2002) Plant Cell Physiol , vol.43 , pp. 1073-1085
    • Kuroda, H.1    Takahashi, N.2    Shimada, H.3    Seki, M.4    Shinozaki, K.5    Matsui, M.6
  • 78
    • 0034193218 scopus 로고    scopus 로고
    • Snail-related transcriptional repressors are required in Xenopus for both the induction of the neural crest and its subsequent migration
    • LABONNE, C. and BRONNER-FRASER, M. (2000). Snail-related transcriptional repressors are required in Xenopus for both the induction of the neural crest and its subsequent migration. Dev Biol 221: 195-205.
    • (2000) Dev Biol , vol.221 , pp. 195-205
    • Labonne, C.1    Bronner-Fraser, M.2
  • 80
    • 0032928229 scopus 로고    scopus 로고
    • Negative regulation of axis formation and Wnt signaling in Xenopus embryos by the F-box/WD40 protein beta TrCP
    • LAGNA, G., CARNEVALI, F., MARCHIONI, M. and HEMMATI-BRIVANLOU, A. (1999). Negative regulation of axis formation and Wnt signaling in Xenopus embryos by the F-box/WD40 protein beta TrCP. Mech Dev 80: 101-106.
    • (1999) Mech Dev , vol.80 , pp. 101-106
    • Lagna, G.1    Carnevali, F.2    Marchioni, M.3    Hemmati-Brivanlou, A.4
  • 81
    • 0030899553 scopus 로고    scopus 로고
    • Establishment of the dorso-ventral axis in Xenopus embryos is presaged by early asymmetries in beta-catenin that are modulated by the Wnt signaling pathway
    • LARABELL, C.A., TORRES, M., ROWNING, B.A., YOST, C., MILLER, J.R., WU, M., KIMELMAN, D. and MOON, R.T. (1997). Establishment of the dorso-ventral axis in Xenopus embryos is presaged by early asymmetries in beta-catenin that are modulated by the Wnt signaling pathway. J Cell Biol 136: 1123-1136.
    • (1997) J Cell Biol , vol.136 , pp. 1123-1136
    • Larabell, C.A.1    Torres, M.2    Rowning, B.A.3    Yost, C.4    Miller, J.R.5    Wu, M.6    Kimelman, D.7    Moon, R.T.8
  • 82
    • 0025808242 scopus 로고
    • Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/ E47-like proteins in vivo
    • LASSAR, A.B., DAVIS, R.L., WRIGHT, W.E., KADESCH, T., MURRE, C., VORONOVA, A., BALTIMORE, D. and WEINTRAUB, H. (1991). Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/ E47-like proteins in vivo. Cell 66: 305-315.
    • (1991) Cell , vol.66 , pp. 305-315
    • Lassar, A.B.1    Davis, R.L.2    Wright, W.E.3    Kadesch, T.4    Murre, C.5    Voronova, A.6    Baltimore, D.7    Weintraub, H.8
  • 83
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin
    • LATRES, E., CHIAUR, D.S. and PAGANO, M. (1999). The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin. Oncogene 18: 849-854.
    • (1999) Oncogene , vol.18 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 84
    • 0031045152 scopus 로고    scopus 로고
    • Basic helix-loop-helix genes in neural development
    • LEE, J.E. (1997). Basic helix-loop-helix genes in neural development. Curr Opin Neurobiol 7: 13-20.
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 13-20
    • Lee, J.E.1
  • 85
    • 35948951997 scopus 로고    scopus 로고
    • The dual effects of Cdh1/APC in myogenesis
    • LI, W., WU, G. and WAN, Y. (2007). The dual effects of Cdh1/APC in myogenesis. FASEB J 21: 3606-3617.
    • (2007) FASEB J , vol.21 , pp. 3606-3617
    • Li, W.1    Wu, G.2    Wan, Y.3
  • 86
    • 32244435431 scopus 로고    scopus 로고
    • Ubiquitination of cyclin-dependent kinase inhibitor, Xic1, is mediated by the Xenopus F-box protein xSkp2
    • LIN, H.R., CHUANG, L.C., BOIX-PERALES, H., PHILPOTT, A. and YEW, P.R. (2006). Ubiquitination of cyclin-dependent kinase inhibitor, Xic1, is mediated by the Xenopus F-box protein xSkp2. Cell Cycle 5: 304-314.
    • (2006) Cell Cycle , vol.5 , pp. 304-314
    • Lin, H.R.1    Chuang, L.C.2    Boix-Perales, H.3    Philpott, A.4    Yew, P.R.5
  • 87
    • 0028981050 scopus 로고
    • Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: Signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B
    • LIN, Y.C., BROWN, K. and SIEBENLIST, U. (1995). Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B. Proc Natl Acad Sci USA 92: 552-556.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 552-556
    • Lin, Y.C.1    Brown, K.2    Siebenlist, U.3
  • 88
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases
    • LIU, J., FURUKAWA, M., MATSUMOTO, T. and XIONG, Y. (2002). NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases. Mol Cell 10: 1511-1518.
    • (2002) Mol Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 89
    • 0032560515 scopus 로고    scopus 로고
    • Human CUL1 forms an evolutionarily conserved ubiquitin ligase complex (SCF) with SKP1 and an F-box protein
    • LYAPINA, S.A., CORRELL, C.C., KIPREOS, E.T. and DESHAIES, R.J. (1998). Human CUL1 forms an evolutionarily conserved ubiquitin ligase complex (SCF) with SKP1 and an F-box protein. Proc Natl Acad Sci USA 95: 7451-7456.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7451-7456
    • Lyapina, S.A.1    Correll, C.C.2    Kipreos, E.T.3    Deshaies, R.J.4
  • 90
    • 0033106149 scopus 로고    scopus 로고
    • A ubiquitin ligase complex essential for the NF-kappaB, Wnt/ Wingless, and Hedgehog signaling pathways
    • MANIATIS, T. (1999). A ubiquitin ligase complex essential for the NF-kappaB, Wnt/ Wingless, and Hedgehog signaling pathways. Genes Dev 13: 505-510.
    • (1999) Genes Dev , vol.13 , pp. 505-510
    • Maniatis, T.1
  • 91
    • 0142149094 scopus 로고    scopus 로고
    • Regulation of the discs large tumor suppressor by a phosphorylation-dependent interaction with the beta-TrCP ubiquitin ligase receptor
    • MANTOVANI, F. and BANKS, L. (2003). Regulation of the discs large tumor suppressor by a phosphorylation-dependent interaction with the beta-TrCP ubiquitin ligase receptor. J Biol Chem 278: 42477-42486.
    • (2003) J Biol Chem , vol.278 , pp. 42477-42486
    • Mantovani, F.1    Banks, L.2
  • 92
    • 0035207441 scopus 로고    scopus 로고
    • Proteasome-mediated regulation of the hDlg tumour suppressor protein
    • MANTOVANI, F., MASSIMI, P. and BANKS, L. (2001). Proteasome-mediated regulation of the hDlg tumour suppressor protein. J Cell Sci 114: 4285-4292.
    • (2001) J Cell Sci , vol.114 , pp. 4285-4292
    • Mantovani, F.1    Massimi, P.2    Banks, L.3
  • 94
    • 0032170327 scopus 로고    scopus 로고
    • Beta-TrCP is a negative regulator of Wnt/beta-catenin signaling pathway and dorsal axis formation in Xenopus embryos
    • MARIKAWA, Y. and ELINSON, R.P. (1998). Beta-TrCP is a negative regulator of Wnt/beta-catenin signaling pathway and dorsal axis formation in Xenopus embryos. Mech Dev 77: 75-80.
    • (1998) Mech Dev , vol.77 , pp. 75-80
    • Marikawa, Y.1    Elinson, R.P.2
  • 95
    • 0033594491 scopus 로고    scopus 로고
    • P63 is a p53 homologue required for limb and epidermal morphogenesis
    • MILLS, A.A., ZHENG, B., WANG, X.J., VOGEL, H., ROOP, D.R. and BRADLEY, A. (1999). P63 is a p53 homologue required for limb and epidermal morphogenesis. Nature 398: 708-713.
    • (1999) Nature , vol.398 , pp. 708-713
    • Mills, A.A.1    Zheng, B.2    Wang, X.J.3    Vogel, H.4    Roop, D.R.5    Bradley, A.6
  • 97
    • 0017157413 scopus 로고
    • Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe
    • NURSE, P., THURIAUX, P. and NASMYTH, K. (1976). Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe. Mol Gen Genet 146: 167-178.
    • (1976) Mol Gen Genet , vol.146 , pp. 167-178
    • Nurse, P.1    Thuriaux, P.2    Nasmyth, K.3
  • 99
    • 0033120027 scopus 로고    scopus 로고
    • ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity
    • OHTA, T., MICHEL, J.J., SCHOTTELIUS, A.J. and XIONG, Y. (1999). ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol Cell 3: 535-541.
    • (1999) Mol Cell , vol.3 , pp. 535-541
    • Ohta, T.1    Michel, J.J.2    Schottelius, A.J.3    Xiong, Y.4
  • 100
    • 36549071481 scopus 로고    scopus 로고
    • Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis
    • ONOYAMA, I., TSUNEMATSU, R., MATSUMOTO, A., KIMURA, T., DE ALBORAN, I.M., NAKAYAMA, K. and NAKAYAMA, K.I. (2007). Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis. J Exp Med 204: 2875-2888.
    • (2007) J Exp Med , vol.204 , pp. 2875-2888
    • Onoyama, I.1    Tsunematsu, R.2    Matsumoto, A.3    Kimura, T.4    de Alboran, I.M.5    Nakayama, K.6    Nakayama, K.I.7
  • 101
    • 33646270662 scopus 로고    scopus 로고
    • Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation
    • PAN, Y., BAI, C.B., JOYNER, A.L. and WANG, B. (2006). Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation. Mol Cell Biol 26: 3365-3377.
    • (2006) Mol Cell Biol , vol.26 , pp. 3365-3377
    • Pan, Y.1    Bai, C.B.2    Joyner, A.L.3    Wang, B.4
  • 102
    • 28944435024 scopus 로고    scopus 로고
    • Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCFCdc34
    • PETROSKI, M.D. and DESHAIES, R.J. (2005). Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCFCdc34. Cell 123: 1107-1120.
    • (2005) Cell , vol.123 , pp. 1107-1120
    • Petroski, M.D.1    Deshaies, R.J.2
  • 103
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • PICKART, C.M. and COHEN, R.E. (2004). Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 5: 177-187.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 104
    • 0021996450 scopus 로고
    • Functional heterogeneity of ubiquitin carrier proteins
    • PICKART, C.M. and ROSE, I.A. (1985). Functional heterogeneity of ubiquitin carrier proteins. J Biol Chem 260: 1573-1581.
    • (1985) J Biol Chem , vol.260 , pp. 1573-1581
    • Pickart, C.M.1    Rose, I.A.2
  • 106
    • 0031966321 scopus 로고    scopus 로고
    • E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton
    • REUVER, S.M. and GARNER, C.C. (1998). E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton. J Cell Sci 111: 1071-1080.
    • (1998) J Cell Sci , vol.111 , pp. 1071-1080
    • Reuver, S.M.1    Garner, C.C.2
  • 108
    • 0028968802 scopus 로고
    • The neuron-restrictive silencer factor (NRSF): A coordinate repressor of multiple neuron-specific genes
    • SCHOENHERR, C.J. and ANDERSON, D.J. (1995). The neuron-restrictive silencer factor (NRSF): a coordinate repressor of multiple neuron-specific genes. Science 267: 1360-1363.
    • (1995) Science , vol.267 , pp. 1360-1363
    • Schoenherr, C.J.1    Anderson, D.J.2
  • 111
    • 0037673562 scopus 로고    scopus 로고
    • The comparative proteomics of ubiquitination in mouse
    • SEMPLE, C.A. (2003). The comparative proteomics of ubiquitination in mouse. Genome Res 13: 1389-1394.
    • (2003) Genome Res , vol.13 , pp. 1389-1394
    • Semple, C.A.1
  • 112
    • 0022930702 scopus 로고
    • Inducibility of [kappa] immunoglobulin enhancer-binding protein NF-[kappa]B by a posttranslational mechanism
    • SEN, R. and BALTIMORE, D. (1986). Inducibility of [kappa] immunoglobulin enhancer-binding protein NF-[kappa]B by a posttranslational mechanism. Cell 47: 921-928.
    • (1986) Cell , vol.47 , pp. 921-928
    • Sen, R.1    Baltimore, D.2
  • 113
    • 56949098738 scopus 로고    scopus 로고
    • Multiple isoforms of [beta]-TrCP display differential activities in the regulation of Wnt signaling
    • SEO, E., KIM, H., KIM, R., YUN, S., KIM, M., HAN, J.-K., COSTANTINI, F. and JHO, E.-H. (2009). Multiple isoforms of [beta]-TrCP display differential activities in the regulation of Wnt signaling. Cellular Signalling 21: 43-51.
    • (2009) Cellular Signalling , vol.21 , pp. 43-51
    • Seo, E.1    Kim, H.2    Kim, R.3    Yun, S.4    Kim, M.5    Han, J.-K.6    Costantini, F.7    Jho, E.-H.8
  • 115
    • 1942484963 scopus 로고    scopus 로고
    • IkappaB kinase-alpha acts in the epidermis to control skeletal and craniofacial morphogenesis
    • SIL, A.K., MAEDA, S., SANO, Y., ROOP, D.R. and KARIN, M. (2004). IkappaB kinase-alpha acts in the epidermis to control skeletal and craniofacial morphogenesis. Nature 428: 660-664.
    • (2004) Nature , vol.428 , pp. 660-664
    • Sil, A.K.1    Maeda, S.2    Sano, Y.3    Roop, D.R.4    Karin, M.5
  • 116
    • 66449110553 scopus 로고    scopus 로고
    • SnapShot: F box proteins II
    • 1358.e1351-e1358.e1352
    • SKAAR, J.R., D'ANGIOLELLA, V., PAGAN, J.K. and PAGANO, M. (2009a). SnapShot: F Box Proteins II. Cell 137: 1358.e1351-1358.e1352.
    • (2009) Cell , vol.137
    • Skaar, J.R.1    D'Angiolella, V.2    Pagan, J.K.3    Pagano, M.4
  • 117
    • 66449110553 scopus 로고    scopus 로고
    • SnapShot: F Box Proteins I
    • SKAAR, J.R., PAGAN, J.K. and PAGANO, M. (2009b). SnapShot: F Box Proteins I. Cell 137: 1160-1160.e1161.
    • (2009) Cell , vol.137
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 118
    • 70549105793 scopus 로고    scopus 로고
    • Control of cell growth by the SCF and APC/ C ubiquitin ligases
    • SKAAR, J.R. and PAGANO, M. (2009). Control of cell growth by the SCF and APC/ C ubiquitin ligases. Current Opinion in Cell Biology 21: 816-824.
    • (2009) Current Opinion in Cell Biology , vol.21 , pp. 816-824
    • Skaar, J.R.1    Pagano, M.2
  • 119
    • 34848892735 scopus 로고    scopus 로고
    • Regulation of Ci- SCFSlimb binding, Ci proteolysis, and hedgehog pathway activity by Ci phosphorylation
    • SMELKINSON, M.G., ZHOU, Q. and KALDERON, D. (2007). Regulation of Ci- SCFSlimb binding, Ci proteolysis, and hedgehog pathway activity by Ci phosphorylation. Dev Cell 13: 481-495.
    • (2007) Dev Cell , vol.13 , pp. 481-495
    • Smelkinson, M.G.1    Zhou, Q.2    Kalderon, D.3
  • 120
    • 0023619362 scopus 로고
    • Dorsal, an embryonic polarity gene in Drosophila, is homologous to the vertebrate proto-oncogene, c-rel
    • STEWARD, R. (1987). Dorsal, an embryonic polarity gene in Drosophila, is homologous to the vertebrate proto-oncogene, c-rel. Science 238: 692-694.
    • (1987) Science , vol.238 , pp. 692-694
    • Steward, R.1
  • 121
  • 126
    • 0037207504 scopus 로고    scopus 로고
    • The cdk inhibitor p27Xic1 is required for differentiation of primary neurones in Xenopus
    • VERNON, A.E., DEVINE, C. and PHILPOTT, A. (2003). The cdk inhibitor p27Xic1 is required for differentiation of primary neurones in Xenopus. Development 130: 85-92.
    • (2003) Development , vol.130 , pp. 85-92
    • Vernon, A.E.1    Devine, C.2    Philpott, A.3
  • 127
    • 33749391866 scopus 로고    scopus 로고
    • Slug stability is dynamically regulated during neural crest development by the F-box protein Ppa
    • VERNON, A.E. and LABONNE, C. (2006). Slug stability is dynamically regulated during neural crest development by the F-box protein Ppa. Development 133: 3359-3370.
    • (2006) Development , vol.133 , pp. 3359-3370
    • Vernon, A.E.1    Labonne, C.2
  • 128
    • 0037207503 scopus 로고    scopus 로고
    • A single cdk inhibitor, p27Xic1, functions beyond cell cycle regulation to promote muscle differentiation in Xenopus
    • VERNON, A.E. and PHILPOTT, A. (2003). A single cdk inhibitor, p27Xic1, functions beyond cell cycle regulation to promote muscle differentiation in Xenopus. Development 130: 71-83.
    • (2003) Development , vol.130 , pp. 71-83
    • Vernon, A.E.1    Philpott, A.2
  • 130
    • 30444437000 scopus 로고    scopus 로고
    • Evidence for the direct involvement of {beta}TrCP in Gli3 protein processing
    • WANG, B. and LI, Y. (2006). Evidence for the direct involvement of {beta}TrCP in Gli3 protein processing. Proc Natl Acad Sci USA 103: 33-38.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 33-38
    • Wang, B.1    Li, Y.2
  • 131
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
    • WEI, W., AYAD, N.G., WAN, Y., ZHANG, G.J., KIRSCHNER, M.W. and KAELIN, W.G., Jr. (2004). Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature 428: 194-198.
    • (2004) Nature , vol.428 , pp. 194-198
    • Wei, W.1    Ayad, N.G.2    Wan, Y.3    Zhang, G.J.4    Kirschner, M.W.5    Kaelin Jr., W.G.6
  • 133
    • 0019174693 scopus 로고
    • Ubiquitin is the ATPdependent proteolysis factor I of rabbit reticulocytes
    • WILKINSON, K.D., URBAN, M.K. and HAAS, A.L. (1980). Ubiquitin is the ATPdependent proteolysis factor I of rabbit reticulocytes. J Biol Chem 255: 7529-7532.
    • (1980) J Biol Chem , vol.255 , pp. 7529-7532
    • Wilkinson, K.D.1    Urban, M.K.2    Haas, A.L.3
  • 134
    • 0033068154 scopus 로고    scopus 로고
    • The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
    • WINSTON, J.T., STRACK, P., BEER-ROMERO, P., CHU, C.Y., ELLEDGE, S.J. and HARPER, J.W. (1999). The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro. GenesDev 13: 270-283.
    • (1999) GenesDev , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 135
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • WOLF, D.H. and HILT, W. (2004). The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochim Biophys Acta 1695: 19-31.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 136
    • 0029819449 scopus 로고    scopus 로고
    • Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia
    • WOODS, D.F., HOUGH, C., PEEL, D., CALLAINI, G. and BRYANT, P.J. (1996). Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia. J Cell Biol 134: 1469-1482.
    • (1996) J Cell Biol , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callaini, G.4    Bryant, P.J.5
  • 137
    • 0034791336 scopus 로고    scopus 로고
    • SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation
    • WU, G., LYAPINA, S., DAS, I., LI, J., GURNEY, M., PAULEY, A., CHUI, I., DESHAIES, R.J. and KITAJEWSKI, J. (2001). SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation. Mol Cell Biol 21: 7403-7415.
    • (2001) Mol Cell Biol , vol.21 , pp. 7403-7415
    • Wu, G.1    Lyapina, S.2    Das, I.3    Li, J.4    Gurney, M.5    Pauley, A.6    Chui, I.7    Deshaies, R.J.8    Kitajewski, J.9
  • 138
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a beta-TrCP1-Skp1-beta-catenin complex: Destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase
    • WU, G., XU, G., SCHULMAN, B.A., JEFFREY, P.D., HARPER, J.W. and PAVLETICH, N.P. (2003). Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. Mol Cell 11: 1445-1456.
    • (2003) Mol Cell , vol.11 , pp. 1445-1456
    • Wu, G.1    Xu, G.2    Schulman, B.A.3    Jeffrey, P.D.4    Harper, J.W.5    Pavletich, N.P.6
  • 139
    • 0033956753 scopus 로고    scopus 로고
    • The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation
    • WU, K., FUCHS, S.Y., CHEN, A., TAN, P., GOMEZ, C., RONAI, Z. and PAN, Z.Q. (2000). The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation. Mol Cell Biol 20: 1382-1393.
    • (2000) Mol Cell Biol , vol.20 , pp. 1382-1393
    • Wu, K.1    Fuchs, S.Y.2    Chen, A.3    Tan, P.4    Gomez, C.5    Ronai, Z.6    Pan, Z.Q.7
  • 140
    • 0032485392 scopus 로고    scopus 로고
    • Regulated nuclear import of Rel proteins in the Drosophila immune response
    • WU, L.P. and ANDERSON, K.V. (1998). Regulated nuclear import of Rel proteins in the Drosophila immune response. Nature 392: 93-97.
    • (1998) Nature , vol.392 , pp. 93-97
    • Wu, L.P.1    Anderson, K.V.2
  • 141
    • 0032052253 scopus 로고    scopus 로고
    • Signal-dependent degradation of IkappaBalpha is mediated by an inducible destruction box that can be transferred to NF-kappaB, bcl-3 or p53
    • WULCZYN, F.G., KRAPPMANN, D. and SCHEIDEREIT, C. (1998). Signal-dependent degradation of IkappaBalpha is mediated by an inducible destruction box that can be transferred to NF-kappaB, bcl-3 or p53. Nucleic Acids Res 26: 1724-1730.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1724-1730
    • Wulczyn, F.G.1    Krappmann, D.2    Scheidereit, C.3
  • 144
    • 15744374449 scopus 로고    scopus 로고
    • Wntdependent regulation of the E-cadherin repressor snail
    • YOOK, J.I., LI, X.Y., OTA, I., FEARON, E.R. and WEISS, S.J. (2005). Wntdependent regulation of the E-cadherin repressor snail. J Biol Chem 280: 11740-11748.
    • (2005) J Biol Chem , vol.280 , pp. 11740-11748
    • Yook, J.I.1    Li, X.Y.2    Ota, I.3    Fearon, E.R.4    Weiss, S.J.5
  • 145
    • 76249092490 scopus 로고    scopus 로고
    • Structural Basis of Selective Ubiquitination of TRF1 by SCFFbx4
    • ZENG, Z., WANG, W., YANG, Y., CHEN, Y., YANG, X., DIEHL, J.A., LIU, X. and LEI, M. (2010). Structural Basis of Selective Ubiquitination of TRF1 by SCFFbx4. Dev Cell 18: 214-225.
    • (2010) Dev Cell , vol.18 , pp. 214-225
    • Zeng, Z.1    Wang, W.2    Yang, Y.3    Chen, Y.4    Yang, X.5    Diehl, J.A.6    Liu, X.7    Lei, M.8
  • 146
    • 0033556237 scopus 로고    scopus 로고
    • P21(CIP1) and p57(KIP2) control muscle differentiation at the myogenin step
    • ZHANG, P., WONG, C., LIU, D., FINEGOLD, M., HARPER, J.W. and ELLEDGE, S.J. (1999). P21(CIP1) and p57(KIP2) control muscle differentiation at the myogenin step. Genes Dev 13: 213-224.
    • (1999) Genes Dev , vol.13 , pp. 213-224
    • Zhang, P.1    Wong, C.2    Liu, D.3    Finegold, M.4    Harper, J.W.5    Elledge, S.J.6
  • 148
    • 5444269904 scopus 로고    scopus 로고
    • Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition
    • ZHOU, B.P., DENG, J., XIA, W., XU, J., LI, Y.M., GUNDUZ, M. and HUNG, M.C. (2004). Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat Cell Biol 6: 931-940.
    • (2004) Nat Cell Biol , vol.6 , pp. 931-940
    • Zhou, B.P.1    Deng, J.2    Xia, W.3    Xu, J.4    Li, Y.M.5    Gunduz, M.6    Hung, M.C.7


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