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Volumn 1835, Issue 1, 2013, Pages 119-128

Smurf E3 ubiquitin ligases at the cross roads of oncogenesis and tumor suppression

Author keywords

Carcinogenesis; HECT E3 ligase; Smurf1; Smurf2; Tumor suppressor

Indexed keywords

BONE MORPHOGENETIC PROTEIN; CELL PROTEIN; HEAT SHOCK PROTEIN; HISTONE; INHIBITOR OF DIFFERENTIATION 1; KRUPPEL LIKE FACTOR; NEDD9 PROTEIN; NERVE CELL ADHESION MOLECULE; PROTEIN HPEM 2; PROTEIN P16; PROTEIN P53; PROTEIN RNF20; RAP1 PROTEIN; RAP1B PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SMAD UBIQUITIN REGULATORY FACTOR 1; SMAD UBIQUITIN REGULATORY FACTOR 2; TALIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 1; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84871028971     PISSN: 0304419X     EISSN: 18792561     Source Type: Journal    
DOI: 10.1016/j.bbcan.2012.11.003     Document Type: Review
Times cited : (73)

References (91)
  • 1
    • 78651321769 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system as a prospective molecular target for cancer treatment and prevention
    • Chen D., Ping Dou Q. The ubiquitin-proteasome system as a prospective molecular target for cancer treatment and prevention. Curr. Protein Pept. Sci. 2010, 11:459-470.
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 459-470
    • Chen, D.1    Ping Dou, Q.2
  • 2
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: multiple players in cancer development
    • Bernassola F., Karin M., Ciechanover A., Melino G. The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell 2008, 14:10-21.
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 4
    • 0033549789 scopus 로고    scopus 로고
    • A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H. A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 1999, 400:687-693.
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 5
    • 0034711290 scopus 로고    scopus 로고
    • Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-β signaling
    • Lin X., Liang M., Feng X.H. Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-β signaling. J. Biol. Chem. 2000, 275:36818-36822.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36818-36822
    • Lin, X.1    Liang, M.2    Feng, X.H.3
  • 6
    • 55949109059 scopus 로고    scopus 로고
    • The HECT E3 ligase Smurf2 is required for Mad2-dependent spindle assembly checkpoint
    • Osmundson E.C., Ray D., Moore F.E., Gao Q., Thomsen G.H., Kiyokawa H. The HECT E3 ligase Smurf2 is required for Mad2-dependent spindle assembly checkpoint. J. Cell Biol. 2008, 183:267-277.
    • (2008) J. Cell Biol. , vol.183 , pp. 267-277
    • Osmundson, E.C.1    Ray, D.2    Moore, F.E.3    Gao, Q.4    Thomsen, G.H.5    Kiyokawa, H.6
  • 8
    • 77449137856 scopus 로고    scopus 로고
    • Roles of E3 ubiquitin ligases in cell adhesion and migration
    • Huang C. Roles of E3 ubiquitin ligases in cell adhesion and migration. Cell Adh. Migr. 2010, 4:10.
    • (2010) Cell Adh. Migr. , vol.4 , pp. 10
    • Huang, C.1
  • 9
    • 10644263286 scopus 로고    scopus 로고
    • Smurf2 up-regulation activates telomere-dependent senescence
    • Zhang H., Cohen S.N. Smurf2 up-regulation activates telomere-dependent senescence. Genes Dev. 2004, 18:3028-3040.
    • (2004) Genes Dev. , vol.18 , pp. 3028-3040
    • Zhang, H.1    Cohen, S.N.2
  • 10
    • 42949129144 scopus 로고    scopus 로고
    • Suppression of human tumor cell proliferation by Smurf2-induced senescence
    • Zhang H., Teng Y., Kong Y., Kowalski P.E., Cohen S.N. Suppression of human tumor cell proliferation by Smurf2-induced senescence. J. Cell. Physiol. 2008, 215:613-620.
    • (2008) J. Cell. Physiol. , vol.215 , pp. 613-620
    • Zhang, H.1    Teng, Y.2    Kong, Y.3    Kowalski, P.E.4    Cohen, S.N.5
  • 11
    • 59149091922 scopus 로고    scopus 로고
    • Smad ubiquitination regulatory factor 2 promotes metastasis of breast cancer cells by enhancing migration and invasiveness
    • Jin C., Yang Y., Anver M.R., Morris N., Wang X., Zhang Y.E. Smad ubiquitination regulatory factor 2 promotes metastasis of breast cancer cells by enhancing migration and invasiveness. Cancer Res. 2009, 69:735.
    • (2009) Cancer Res. , vol.69 , pp. 735
    • Jin, C.1    Yang, Y.2    Anver, M.R.3    Morris, N.4    Wang, X.5    Zhang, Y.E.6
  • 12
    • 0037115624 scopus 로고    scopus 로고
    • High-level expression of the Smad ubiquitin ligase Smurf2 correlates with poor prognosis in patients with esophageal squamous cell carcinoma
    • Fukuchi M., Fukai Y., Masuda N., Miyazaki T., Nakajima M., Sohda M., Manda R., Tsukada K., Kato H., Kuwano H. High-level expression of the Smad ubiquitin ligase Smurf2 correlates with poor prognosis in patients with esophageal squamous cell carcinoma. Cancer Res. 2002, 62:7162.
    • (2002) Cancer Res. , vol.62 , pp. 7162
    • Fukuchi, M.1    Fukai, Y.2    Masuda, N.3    Miyazaki, T.4    Nakajima, M.5    Sohda, M.6    Manda, R.7    Tsukada, K.8    Kato, H.9    Kuwano, H.10
  • 13
    • 33846653317 scopus 로고    scopus 로고
    • Genome-wide array-based comparative genomic hybridization analysis of pancreatic adenocarcinoma: identification of genetic indicators that predict patient outcome
    • Loukopoulos P., Shibata T., Katoh H., Kokubu A., Sakamoto M., Yamazaki K., Kosuge T., Kanai Y., Hosoda F., Imoto I. Genome-wide array-based comparative genomic hybridization analysis of pancreatic adenocarcinoma: identification of genetic indicators that predict patient outcome. Cancer Sci. 2007, 98:392-400.
    • (2007) Cancer Sci. , vol.98 , pp. 392-400
    • Loukopoulos, P.1    Shibata, T.2    Katoh, H.3    Kokubu, A.4    Sakamoto, M.5    Yamazaki, K.6    Kosuge, T.7    Kanai, Y.8    Hosoda, F.9    Imoto, I.10
  • 14
    • 77956566522 scopus 로고    scopus 로고
    • Reduction of transforming growth factor-β type II receptor is caused by the enhanced ubiquitin-dependent degradation in human renal cell carcinoma
    • Fukasawa H., Yamamoto T., Fujigaki Y., Misaki T., Ohashi N., Takayama T., Suzuki S., Mugiya S., Oda T., Uchida C. Reduction of transforming growth factor-β type II receptor is caused by the enhanced ubiquitin-dependent degradation in human renal cell carcinoma. Int. J. Cancer 2010, 127:1517-1525.
    • (2010) Int. J. Cancer , vol.127 , pp. 1517-1525
    • Fukasawa, H.1    Yamamoto, T.2    Fujigaki, Y.3    Misaki, T.4    Ohashi, N.5    Takayama, T.6    Suzuki, S.7    Mugiya, S.8    Oda, T.9    Uchida, C.10
  • 15
    • 45149101298 scopus 로고    scopus 로고
    • Smad ubiquitination regulatory factor-2 in the fibrotic kidney: regulation, target specificity, and functional implication
    • Tan R., He W., Lin X., Kiss L.P., Liu Y. Smad ubiquitination regulatory factor-2 in the fibrotic kidney: regulation, target specificity, and functional implication. Am. J. Physiol. Renal Physiol. 2008, 294:F1076-F1083.
    • (2008) Am. J. Physiol. Renal Physiol. , vol.294
    • Tan, R.1    He, W.2    Lin, X.3    Kiss, L.P.4    Liu, Y.5
  • 16
    • 33749261981 scopus 로고    scopus 로고
    • Downregulation of SnoN expression in obstructive nephropathy is mediated by an enhanced ubiquitin-dependent degradation
    • Tan R., Zhang J., Tan X., Zhang X., Yang J., Liu Y. Downregulation of SnoN expression in obstructive nephropathy is mediated by an enhanced ubiquitin-dependent degradation. J. Am. Soc. Nephrol. 2006, 17:2781-2791.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 2781-2791
    • Tan, R.1    Zhang, J.2    Tan, X.3    Zhang, X.4    Yang, J.5    Liu, Y.6
  • 17
    • 84856691330 scopus 로고    scopus 로고
    • A tumor suppressor function of Smurf2 associated with controlling chromatin landscape and genome stability through RNF20
    • Blank M., Tang Y., Yamashita M., Burkett S.S., Cheng S.Y., Zhang Y.E. A tumor suppressor function of Smurf2 associated with controlling chromatin landscape and genome stability through RNF20. Nat. Med. 2012, 18:227-234.
    • (2012) Nat. Med. , vol.18 , pp. 227-234
    • Blank, M.1    Tang, Y.2    Yamashita, M.3    Burkett, S.S.4    Cheng, S.Y.5    Zhang, Y.E.6
  • 18
    • 36248989248 scopus 로고    scopus 로고
    • The Nedd4-like family of E3 ubiquitin ligases and cancer
    • Chen C., Matesic L.E. The Nedd4-like family of E3 ubiquitin ligases and cancer. Cancer Metastasis Rev. 2007, 26:587-604.
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 587-604
    • Chen, C.1    Matesic, L.E.2
  • 19
    • 33745193280 scopus 로고    scopus 로고
    • An expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2
    • Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D. An expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2. J. Biol. Chem. 2006, 281:17069-17075.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17069-17075
    • Chong, P.A.1    Lin, H.2    Wrana, J.L.3    Forman-Kay, J.D.4
  • 20
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation
    • Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation. Mol. Cell 2000, 6:1365-1375.
    • (2000) Mol. Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6    Wrana, J.L.7
  • 21
    • 78649875435 scopus 로고    scopus 로고
    • Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity
    • Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D. Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity. Proc. Natl. Acad. Sci. 2010, 107:18404-18409.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 18404-18409
    • Chong, P.A.1    Lin, H.2    Wrana, J.L.3    Forman-Kay, J.D.4
  • 22
    • 0038363366 scopus 로고    scopus 로고
    • Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-β signaling by Smad7
    • Tajima Y., Goto K., Yoshida M., Shinomiya K., Sekimoto T., Yoneda Y., Miyazono K., Imamura T. Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-β signaling by Smad7. J. Biol. Chem. 2003, 278:10716-10721.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10716-10721
    • Tajima, Y.1    Goto, K.2    Yoshida, M.3    Shinomiya, K.4    Sekimoto, T.5    Yoneda, Y.6    Miyazono, K.7    Imamura, T.8
  • 23
    • 77953797876 scopus 로고    scopus 로고
    • Smurf1 ubiquitin ligase causes downregulation of BMP receptors and is induced in monocrotaline and hypoxia models of pulmonary arterial hypertension
    • Murakami K., Mathew R., Huang J., Farahani R., Peng H., Olson S.C., Etlinger J.D. Smurf1 ubiquitin ligase causes downregulation of BMP receptors and is induced in monocrotaline and hypoxia models of pulmonary arterial hypertension. Exp. Biol. Med. 2010, 235:805-813.
    • (2010) Exp. Biol. Med. , vol.235 , pp. 805-813
    • Murakami, K.1    Mathew, R.2    Huang, J.3    Farahani, R.4    Peng, H.5    Olson, S.C.6    Etlinger, J.D.7
  • 24
  • 25
    • 78751697205 scopus 로고    scopus 로고
    • Phosphorylation of E3 ligase Smurf1 switches its substrate preference in support of axon development
    • Cheng P., Lu H., Shelly M., Gao H., Poo M. Phosphorylation of E3 ligase Smurf1 switches its substrate preference in support of axon development. Neuron 2011, 69:231-243.
    • (2011) Neuron , vol.69 , pp. 231-243
    • Cheng, P.1    Lu, H.2    Shelly, M.3    Gao, H.4    Poo, M.5
  • 27
    • 33846497347 scopus 로고    scopus 로고
    • Regulation of catalytic activities of HECT ubiquitin ligases
    • Kee Y., Huibregtse J.M. Regulation of catalytic activities of HECT ubiquitin ligases. Biochem. Biophys. Res. Commun. 2007, 354:329-333.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 329-333
    • Kee, Y.1    Huibregtse, J.M.2
  • 30
    • 77954894530 scopus 로고    scopus 로고
    • Smad ubiquitylation regulatory factor 1/2 (Smurf1/2) promotes p53 degradation by stabilizing the E3 ligase MDM2
    • Nie J., Xie P., Liu L., Xing G., Chang Z., Yin Y., Tian C., He F., Zhang L. Smad ubiquitylation regulatory factor 1/2 (Smurf1/2) promotes p53 degradation by stabilizing the E3 ligase MDM2. J. Biol. Chem. 2010, 285:22818.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22818
    • Nie, J.1    Xie, P.2    Liu, L.3    Xing, G.4    Chang, Z.5    Yin, Y.6    Tian, C.7    He, F.8    Zhang, L.9
  • 31
    • 58149216052 scopus 로고    scopus 로고
    • Signaling cross-talk between TGF-β/BMP and other pathways
    • Guo X., Wang X.F. Signaling cross-talk between TGF-β/BMP and other pathways. Cell Res. 2008, 19:71-88.
    • (2008) Cell Res. , vol.19 , pp. 71-88
    • Guo, X.1    Wang, X.F.2
  • 33
    • 0141866700 scopus 로고    scopus 로고
    • Smurf1 facilitates myogenic differentiation and antagonizes the bone morphogenetic protein-2-induced osteoblast conversion by targeting Smad5 for degradation
    • Ying S.X., Hussain Z.J., Zhang Y.E. Smurf1 facilitates myogenic differentiation and antagonizes the bone morphogenetic protein-2-induced osteoblast conversion by targeting Smad5 for degradation. J. Biol. Chem. 2003, 278:39029-39036.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39029-39036
    • Ying, S.X.1    Hussain, Z.J.2    Zhang, Y.E.3
  • 34
    • 1942534004 scopus 로고    scopus 로고
    • Regulation of the TGFβ signalling pathway by ubiquitin-mediated degradation
    • Izzi L., Attisano L. Regulation of the TGFβ signalling pathway by ubiquitin-mediated degradation. Oncogene 2004, 23:2071-2078.
    • (2004) Oncogene , vol.23 , pp. 2071-2078
    • Izzi, L.1    Attisano, L.2
  • 35
    • 85047692249 scopus 로고    scopus 로고
    • Impaired Smad7-Smurf-mediated negative regulation of TGF-beta signaling in scleroderma fibroblasts
    • Asano Y., Ihn H., Yamane K., Kubo M., Tamaki K. Impaired Smad7-Smurf-mediated negative regulation of TGF-beta signaling in scleroderma fibroblasts. J. Clin. Invest. 2004, 113:253-264.
    • (2004) J. Clin. Invest. , vol.113 , pp. 253-264
    • Asano, Y.1    Ihn, H.2    Yamane, K.3    Kubo, M.4    Tamaki, K.5
  • 36
    • 0034976149 scopus 로고    scopus 로고
    • TGF-β induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation
    • Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K., Wrana J.L. TGF-β induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation. Nat. Cell Biol. 2001, 3:587-595.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 587-595
    • Bonni, S.1    Wang, H.R.2    Causing, C.G.3    Kavsak, P.4    Stroschein, S.L.5    Luo, K.6    Wrana, J.L.7
  • 37
    • 10444279104 scopus 로고    scopus 로고
    • Direct interaction between Smad3, APC10, CDH1 and HEF1 in proteasomal degradation of HEF1
    • Nourry C., Maksumova L., Pang M., Liu X., Wang T. Direct interaction between Smad3, APC10, CDH1 and HEF1 in proteasomal degradation of HEF1. BMC Cell Biol. 2004, 5:20.
    • (2004) BMC Cell Biol. , vol.5 , pp. 20
    • Nourry, C.1    Maksumova, L.2    Pang, M.3    Liu, X.4    Wang, T.5
  • 38
    • 20444439172 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases
    • Morén A., Imamura T., Miyazono K., Heldin C.H., Moustakas A. Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases. J. Biol. Chem. 2005, 280:22115-22123.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22115-22123
    • Morén, A.1    Imamura, T.2    Miyazono, K.3    Heldin, C.H.4    Moustakas, A.5
  • 41
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: cell-cycle control and cancer
    • Nakayama K.I., Nakayama K. Ubiquitin ligases: cell-cycle control and cancer. Nat. Rev. Cancer 2006, 6:369-381.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 42
    • 33644868709 scopus 로고    scopus 로고
    • Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle
    • Dadke D., Jarnik M., Pugacheva E.N., Singh M.K., Golemis E.A. Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle. Mol. Biol. Cell 2006, 17:1204-1217.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1204-1217
    • Dadke, D.1    Jarnik, M.2    Pugacheva, E.N.3    Singh, M.K.4    Golemis, E.A.5
  • 43
    • 13944253623 scopus 로고    scopus 로고
    • MAD2 dependent mitotic checkpoint defects in tumorigenesis and tumor cell death: a double edged sword
    • Michel L., Benezra R., Diaz-Rodriguez E. MAD2 dependent mitotic checkpoint defects in tumorigenesis and tumor cell death: a double edged sword. Cell Cycle 2004, 3:990.
    • (2004) Cell Cycle , vol.3 , pp. 990
    • Michel, L.1    Benezra, R.2    Diaz-Rodriguez, E.3
  • 44
    • 79953164289 scopus 로고    scopus 로고
    • Smurf1 ubiquitin ligase targets Kruppel-like factor KLF2 for ubiquitination and degradation in human lung cancer H1299 cells
    • Xie P., Tang Y., Shen S., Wang Y., Xing G., Yin Y., He F., Zhang L. Smurf1 ubiquitin ligase targets Kruppel-like factor KLF2 for ubiquitination and degradation in human lung cancer H1299 cells. Biochem. Biophys. Res. Commun. 2011, 407:254-259.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 254-259
    • Xie, P.1    Tang, Y.2    Shen, S.3    Wang, Y.4    Xing, G.5    Yin, Y.6    He, F.7    Zhang, L.8
  • 45
    • 81155132209 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase SMAD ubiquitination regulatory factor 2 negatively regulates Krüppel-like factor 5 protein
    • Du J.X., Hagos E.G., Nandan M.O., Bialkowska A.B., Yu B., Yang V.W. The E3 ubiquitin ligase SMAD ubiquitination regulatory factor 2 negatively regulates Krüppel-like factor 5 protein. J. Biol. Chem. 2011, 286:40354-40364.
    • (2011) J. Biol. Chem. , vol.286 , pp. 40354-40364
    • Du, J.X.1    Hagos, E.G.2    Nandan, M.O.3    Bialkowska, A.B.4    Yu, B.5    Yang, V.W.6
  • 50
    • 0035831436 scopus 로고    scopus 로고
    • Intestinal-enriched Krüppel-like factor (Krüppel-like factor 5) is a positive regulator of cellular proliferation
    • Sun R., Chen X., Yang V.W. Intestinal-enriched Krüppel-like factor (Krüppel-like factor 5) is a positive regulator of cellular proliferation. J. Biol. Chem. 2001, 276:6897-6900.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6897-6900
    • Sun, R.1    Chen, X.2    Yang, V.W.3
  • 52
    • 0033104158 scopus 로고    scopus 로고
    • A gene encoding an intestinal-enriched member of the Krüppel-like factor family expressed in intestinal epithelial cells
    • Conkright M.D., Wani M.A., Anderson K.P., Lingrel J.B. A gene encoding an intestinal-enriched member of the Krüppel-like factor family expressed in intestinal epithelial cells. Nucleic Acids Res. 1999, 27:1263-1270.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1263-1270
    • Conkright, M.D.1    Wani, M.A.2    Anderson, K.P.3    Lingrel, J.B.4
  • 53
    • 85027945007 scopus 로고    scopus 로고
    • Krüppel-like factors: three fingers in control
    • Swamynathan S.K. Krüppel-like factors: three fingers in control. Hum. Genom. 2010, 4:263-270.
    • (2010) Hum. Genom. , vol.4 , pp. 263-270
    • Swamynathan, S.K.1
  • 54
    • 65449148205 scopus 로고    scopus 로고
    • Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration
    • Huang C., Rajfur Z., Yousefi N., Chen Z., Jacobson K., Ginsberg M.H. Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration. Nat. Cell Biol. 2009, 11:624-630.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 624-630
    • Huang, C.1    Rajfur, Z.2    Yousefi, N.3    Chen, Z.4    Jacobson, K.5    Ginsberg, M.H.6
  • 55
    • 33947116450 scopus 로고    scopus 로고
    • Ubiquitination of the GTPase Rap1B by the ubiquitin ligase Smurf2 is required for the establishment of neuronal polarity
    • Schwamborn J.C., Müller M., Becker A.H.M., Püschel A.W. Ubiquitination of the GTPase Rap1B by the ubiquitin ligase Smurf2 is required for the establishment of neuronal polarity. EMBO J. 2007, 26:1410-1422.
    • (2007) EMBO J. , vol.26 , pp. 1410-1422
    • Schwamborn, J.C.1    Müller, M.2    Becker, A.H.M.3    Püschel, A.W.4
  • 56
    • 44649151131 scopus 로고    scopus 로고
    • Smurf1 directly targets hPEM-2, a GEF for Cdc42, via a novel combination of protein interaction modules in the ubiquitin-proteasome pathway
    • Yamaguchi K., Ohara O., Ando A., Nagase T. Smurf1 directly targets hPEM-2, a GEF for Cdc42, via a novel combination of protein interaction modules in the ubiquitin-proteasome pathway. Biol. Chem. 2008, 389:405-413.
    • (2008) Biol. Chem. , vol.389 , pp. 405-413
    • Yamaguchi, K.1    Ohara, O.2    Ando, A.3    Nagase, T.4
  • 57
    • 67649210240 scopus 로고    scopus 로고
    • Smurf2 participates in human trophoblast cell invasion by inhibiting TGF-β Type I receptor
    • Yang Q., Chen S.P., Zhang X.P., Wang H., Zhu C., Lin H.Y. Smurf2 participates in human trophoblast cell invasion by inhibiting TGF-β Type I receptor. J. Histochem. Cytochem. 2009, 57:605.
    • (2009) J. Histochem. Cytochem. , vol.57 , pp. 605
    • Yang, Q.1    Chen, S.P.2    Zhang, X.P.3    Wang, H.4    Zhu, C.5    Lin, H.Y.6
  • 58
    • 67649397771 scopus 로고    scopus 로고
    • Cerebral cavernous malformation 2 protein promotes smad ubiquitin regulatory factor 1-mediated RhoA degradation in endothelial cells
    • Crose L.E.S., Hilder T.L., Sciaky N., Johnson G.L. Cerebral cavernous malformation 2 protein promotes smad ubiquitin regulatory factor 1-mediated RhoA degradation in endothelial cells. J. Biol. Chem. 2009, 284:13301-13305.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13301-13305
    • Crose, L.E.S.1    Hilder, T.L.2    Sciaky, N.3    Johnson, G.L.4
  • 60
    • 33744969296 scopus 로고    scopus 로고
    • Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling
    • Asanuma K., Yanagida-Asanuma E., Faul C., Tomino Y., Kim K., Mundel P. Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling. Nat. Cell Biol. 2006, 8:485-491.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 485-491
    • Asanuma, K.1    Yanagida-Asanuma, E.2    Faul, C.3    Tomino, Y.4    Kim, K.5    Mundel, P.6
  • 61
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane D.P. Cancer. p53, guardian of the genome. Nature 1992, 358:15.
    • (1992) Nature , vol.358 , pp. 15
    • Lane, D.P.1
  • 62
    • 77954174209 scopus 로고    scopus 로고
    • HECT ubiquitin ligase Smurf1 targets the tumor suppressor ING2 for ubiquitination and degradation
    • Nie J., Liu L., Wu M., Xing G., He S., Yin Y., Tian C., He F., Zhang L. HECT ubiquitin ligase Smurf1 targets the tumor suppressor ING2 for ubiquitination and degradation. FEBS Lett. 2010, 584:3005-3012.
    • (2010) FEBS Lett. , vol.584 , pp. 3005-3012
    • Nie, J.1    Liu, L.2    Wu, M.3    Xing, G.4    He, S.5    Yin, Y.6    Tian, C.7    He, F.8    Zhang, L.9
  • 63
    • 79955958397 scopus 로고    scopus 로고
    • The E3 ligase Smurf1 regulates Wolfram syndrome protein stability at the endoplasmic reticulum
    • Guo X., Shen S., Song S., He S., Cui Y., Xing G., Wang J., Yin Y., Fan L., He F. The E3 ligase Smurf1 regulates Wolfram syndrome protein stability at the endoplasmic reticulum. J. Biol. Chem. 2011, 286:18037.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18037
    • Guo, X.1    Shen, S.2    Song, S.3    He, S.4    Cui, Y.5    Xing, G.6    Wang, J.7    Yin, Y.8    Fan, L.9    He, F.10
  • 64
    • 1842429946 scopus 로고    scopus 로고
    • An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein
    • Li H., Seth A. An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein. Oncogene 2004, 23:1801-1808.
    • (2004) Oncogene , vol.23 , pp. 1801-1808
    • Li, H.1    Seth, A.2
  • 65
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997, 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 68
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • Chen D., Kon N., Li M., Zhang W., Qin J., Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 2005, 121:1071-1083.
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 69
    • 22844447871 scopus 로고    scopus 로고
    • The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
    • Esser C., Scheffner M., Höhfeld J. The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J. Biol. Chem. 2005, 280:27443-27448.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27443-27448
    • Esser, C.1    Scheffner, M.2    Höhfeld, J.3
  • 72
    • 80054864989 scopus 로고    scopus 로고
    • Ubiquitination of heat shock protein 27 is mediated by its interaction with Smad ubiquitination regulatory factor 2 in A549 cells
    • Sun Y., Zhou M., Fu D., Xu B., Fang T., Ma Y., Chen J., Zhang J. Ubiquitination of heat shock protein 27 is mediated by its interaction with Smad ubiquitination regulatory factor 2 in A549 cells. Exp. Lung Res. 2011, 37:568-573.
    • (2011) Exp. Lung Res. , vol.37 , pp. 568-573
    • Sun, Y.1    Zhou, M.2    Fu, D.3    Xu, B.4    Fang, T.5    Ma, Y.6    Chen, J.7    Zhang, J.8
  • 75
    • 10744231292 scopus 로고    scopus 로고
    • Proteasomal degradation of Runx2 shortens parathyroid hormone-induced anti-apoptotic signaling in osteoblasts: a putative explanation for why intermittent administration is needed for bone anabolism
    • Bellido T., Ali A.A., Plotkin L.I., Fu Q., Gubrij I., Roberson P.K., Weinstein R.S., O'Brien C.A., Manolagas S.C., Jilka R.L. Proteasomal degradation of Runx2 shortens parathyroid hormone-induced anti-apoptotic signaling in osteoblasts: a putative explanation for why intermittent administration is needed for bone anabolism. Sci. STKE 2003, 278:50259.
    • (2003) Sci. STKE , vol.278 , pp. 50259
    • Bellido, T.1    Ali, A.A.2    Plotkin, L.I.3    Fu, Q.4    Gubrij, I.5    Roberson, P.K.6    Weinstein, R.S.7    O'Brien, C.A.8    Manolagas, S.C.9    Jilka, R.L.10
  • 77
    • 49449101076 scopus 로고    scopus 로고
    • Smurf2 is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation
    • Carpentier I., Coornaert B., Beyaert R. Smurf2 is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation. Biochem. Biophys. Res. Commun. 2008, 374:752-757.
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , pp. 752-757
    • Carpentier, I.1    Coornaert, B.2    Beyaert, R.3
  • 79
    • 0025238437 scopus 로고
    • The protein Id: a negative regulator of helix-loop-helix DNA binding proteins
    • Benezra R., Davis R.L., Lockshon D., Turner D.L., Weintraub H. The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 1990, 61:49.
    • (1990) Cell , vol.61 , pp. 49
    • Benezra, R.1    Davis, R.L.2    Lockshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 80
    • 0028303223 scopus 로고
    • The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein
    • Iavarone A., Garg P., Lasorella A., Hsu J., Israel M.A. The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein. Genes Dev. 1994, 8:1270-1284.
    • (1994) Genes Dev. , vol.8 , pp. 1270-1284
    • Iavarone, A.1    Garg, P.2    Lasorella, A.3    Hsu, J.4    Israel, M.A.5
  • 83
    • 81155151472 scopus 로고    scopus 로고
    • Smurf2-mediated ubiquitination and degradation of Id1 regulates p16 expression during senescence
    • Kong Y., Cui H., Zhang H. Smurf2-mediated ubiquitination and degradation of Id1 regulates p16 expression during senescence. Aging Cell 2011, 10:1038-1046.
    • (2011) Aging Cell , vol.10 , pp. 1038-1046
    • Kong, Y.1    Cui, H.2    Zhang, H.3
  • 84
    • 27944454433 scopus 로고    scopus 로고
    • Monoubiquitination of human histone H2B: the factors involved and their roles in< i> HOX gene regulation
    • Zhu B., Zheng Y., Pham A.D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Monoubiquitination of human histone H2B: the factors involved and their roles in< i> HOX gene regulation. Mol. Cell 2005, 20:601-611.
    • (2005) Mol. Cell , vol.20 , pp. 601-611
    • Zhu, B.1    Zheng, Y.2    Pham, A.D.3    Mandal, S.S.4    Erdjument-Bromage, H.5    Tempst, P.6    Reinberg, D.7
  • 85
    • 43149122898 scopus 로고    scopus 로고
    • Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells
    • Minsky N., Shema E., Field Y., Schuster M., Segal E., Oren M. Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells. Nat. Cell Biol. 2008, 10:483-488.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 483-488
    • Minsky, N.1    Shema, E.2    Field, Y.3    Schuster, M.4    Segal, E.5    Oren, M.6
  • 91
    • 33748521536 scopus 로고    scopus 로고
    • E3 ubiquitin ligases as cancer targets and biomarkers
    • Sun Y. E3 ubiquitin ligases as cancer targets and biomarkers. Neoplasia 2006, 8:645.
    • (2006) Neoplasia , vol.8 , pp. 645
    • Sun, Y.1


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