메뉴 건너뛰기




Volumn 584, Issue 14, 2010, Pages 3021-3027

REGγ proteasome mediates degradation of the ubiquitin ligase Smurf1

Author keywords

Proteasome; Protein degradation; REG ; Smad ubiquitination regulatory factor 1; Ubiquitin

Indexed keywords

GLUTATHIONE; PROTEASOME; PROTEIN REGGAMMA; PROTEIN SMURF1; PROTEIN SMURF2; SMAD UBIQUITINATION REGULATORY FACTOR 1; SMAD UBIQUITINATION REGULATORY FACTOR 2; SMAD UBIQUITINATION REGULATORY FACTOR 5; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; AUTOANTIGEN; KI ANTIGEN; LIGASE; UBIQUITIN;

EID: 77954176625     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.05.034     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 1996, 65:801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 2
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 3
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • Orlowski M., Wilk S. Ubiquitin-independent proteolytic functions of the proteasome. Arch. Biochem. Biophys. 2003, 415:1-5.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 5
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain)
    • Ma C.P., Slaughter C.A., DeMartino G.N. Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain). J. Biol. Chem. 1992, 267:10515-10523.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Ma, C.P.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 6
    • 0026498493 scopus 로고
    • Purification of an 11 S regulator of the multicatalytic protease
    • Dubiel W., Pratt G., Ferrell K., Rechsteiner M. Purification of an 11 S regulator of the multicatalytic protease. J. Biol. Chem. 1992, 267:22369-22377.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 7
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
    • Kloetzel P.M., Ossendorp F. Proteasome and peptidase function in MHC-class-I-mediated antigen presentation. Curr. Opin. Immunol. 2004, 16:76-81.
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 9
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 2005, 15:27-33.
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 10
    • 31044449824 scopus 로고    scopus 로고
    • The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome
    • Li X., Lonard D.M., Jung S.Y., Malovannaya A., Feng Q., Qin J., Tsai S.Y., Tsai M.J., O'Malley B.W. The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome. Cell 2006, 124:381-392.
    • (2006) Cell , vol.124 , pp. 381-392
    • Li, X.1    Lonard, D.M.2    Jung, S.Y.3    Malovannaya, A.4    Feng, Q.5    Qin, J.6    Tsai, S.Y.7    Tsai, M.J.8    O'Malley, B.W.9
  • 11
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of cell-cycle inhibitors by the REGγ proteasome
    • Chen X., Barton L.F., Chi Y., Clurman B.E., Roberts J.M. Ubiquitin-independent degradation of cell-cycle inhibitors by the REGγ proteasome. Mol. Cell 2007, 26:843-852.
    • (2007) Mol. Cell , vol.26 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 12
    • 34250339984 scopus 로고    scopus 로고
    • Ubiquitin- and ATP- independent proteolytic turnover of p21 by the REGγ-proteasome pathway
    • Li X., Amazit L., Long W., Lonard D.M., Monaco J.J., O'Malley B.W. Ubiquitin- and ATP- independent proteolytic turnover of p21 by the REGγ-proteasome pathway. Mol. Cell 2007, 26:831-842.
    • (2007) Mol. Cell , vol.26 , pp. 831-842
    • Li, X.1    Amazit, L.2    Long, W.3    Lonard, D.M.4    Monaco, J.J.5    O'Malley, B.W.6
  • 15
    • 40949117250 scopus 로고    scopus 로고
    • Proteasome activator PA28 regulates p53 by enhancing its MDM2-mediated degradation
    • Zhang Z., Zhang R. Proteasome activator PA28 regulates p53 by enhancing its MDM2-mediated degradation. EMBO J. 2008, 27:852-864.
    • (2008) EMBO J. , vol.27 , pp. 852-864
    • Zhang, Z.1    Zhang, R.2
  • 21
    • 33750592404 scopus 로고    scopus 로고
    • Aberrant accumulation of PTTG1 induced by a mutated thyroid hormone beta receptor inhibits mitotic progression
    • Ying H., Furuya F., Zhao L., Araki O., West B.L., Hanover J.A., Willingham M.C., Cheng S.Y. Aberrant accumulation of PTTG1 induced by a mutated thyroid hormone beta receptor inhibits mitotic progression. J. Clin. Invest. 2006, 116:2972-2984.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2972-2984
    • Ying, H.1    Furuya, F.2    Zhao, L.3    Araki, O.4    West, B.L.5    Hanover, J.A.6    Willingham, M.C.7    Cheng, S.Y.8
  • 22
    • 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
  • 23
    • 17044414102 scopus 로고    scopus 로고
    • Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation
    • Yamashita M., Ying S.X., Zhang G.M., Li C., Cheng S.Y., Deng C.X., Zhang Y.E. Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 2005, 121:101-113.
    • (2005) Cell , vol.121 , pp. 101-113
    • Yamashita, M.1    Ying, S.X.2    Zhang, G.M.3    Li, C.4    Cheng, S.Y.5    Deng, C.X.6    Zhang, Y.E.7
  • 28
  • 29
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner M., Nuber U., Huibregtse J.M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 1995, 373:81-83.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 30
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2009, 10:398-409.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 31
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture
    • Ingham R.J., Gish G., Pawson T. The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture. Oncogene 2004, 23:1972-1984.
    • (2004) Oncogene , vol.23 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 32
    • 1842477311 scopus 로고    scopus 로고
    • Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo
    • Zhao M., Qiao M., Harris S.E., Oyajobi B.O., Mundy G.R., Chen D. Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo. J. Biol. Chem. 2004, 279:12854-12859.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12854-12859
    • Zhao, M.1    Qiao, M.2    Harris, S.E.3    Oyajobi, B.O.4    Mundy, G.R.5    Chen, D.6
  • 33
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • Bloom J., Amador V., Bartolini F., DeMartino G., Pagano M. Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 2003, 115:71-82.
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    DeMartino, G.4    Pagano, M.5
  • 34
    • 3042796205 scopus 로고    scopus 로고
    • N-terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome
    • Coulombe P., Rodier G., Bonneil E., Thibault P., Meloche S. N-terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome. Mol. Cell. Biol. 2004, 24:6140-6150.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6140-6150
    • Coulombe, P.1    Rodier, G.2    Bonneil, E.3    Thibault, P.4    Meloche, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.