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Volumn 22, Issue 3, 2006, Pages 317-327

Interaction between c-Abl and Arg Tyrosine Kinases and Proteasome Subunit PSMA7 Regulates Proteasome Degradation

Author keywords

CELLCYCLE; PROTEINS

Indexed keywords

ABELSON KINASE; ARGININE; PROTEASOME; PROTEIN HYDROLYSATE; PROTEIN SUBUNIT; PROTEIN TYROSINE KINASE;

EID: 33646145066     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.04.007     Document Type: Article
Times cited : (53)

References (39)
  • 1
    • 0033600240 scopus 로고    scopus 로고
    • Interaction of c-Abl and p73α and their collaboration to induce apoptosis
    • Agami R., Blandino G., Oren M., and Shaul Y. Interaction of c-Abl and p73α and their collaboration to induce apoptosis. Nature 399 (1999) 809-813
    • (1999) Nature , vol.399 , pp. 809-813
    • Agami, R.1    Blandino, G.2    Oren, M.3    Shaul, Y.4
  • 3
    • 21444435325 scopus 로고    scopus 로고
    • Abl-kinase-sensitive levels of ERK5 and its intrinsic basal activity contribute to leukaemia cell survival
    • Buschbeck M., Hofbauer S., Croce L., Keri G., and Ullrich A. Abl-kinase-sensitive levels of ERK5 and its intrinsic basal activity contribute to leukaemia cell survival. EMBO Rep. 6 (2005) 63-69
    • (2005) EMBO Rep. , vol.6 , pp. 63-69
    • Buschbeck, M.1    Hofbauer, S.2    Croce, L.3    Keri, G.4    Ullrich, A.5
  • 4
    • 0042819604 scopus 로고    scopus 로고
    • Catalse is regulated by ubiquitination and proteosomal degradation. Role of the c-Abl and Arg tyrosine kinases
    • Cao C., Leng Y., Liu X., Yi Y., Li P., and Kufe D. Catalse is regulated by ubiquitination and proteosomal degradation. Role of the c-Abl and Arg tyrosine kinases. Biochemistry 42 (2003) 10348-10353
    • (2003) Biochemistry , vol.42 , pp. 10348-10353
    • Cao, C.1    Leng, Y.2    Liu, X.3    Yi, Y.4    Li, P.5    Kufe, D.6
  • 5
    • 0037630403 scopus 로고    scopus 로고
    • Functional interaction between the c-Abl and Arg protein-tyrosinekinase in the oxidative stress response
    • Cao C., Leng Y., Li C., and Kufe D. Functional interaction between the c-Abl and Arg protein-tyrosinekinase in the oxidative stress response. J. Biol. Chem. 278 (2003) 12961-12967
    • (2003) J. Biol. Chem. , vol.278 , pp. 12961-12967
    • Cao, C.1    Leng, Y.2    Li, C.3    Kufe, D.4
  • 6
    • 0035370123 scopus 로고    scopus 로고
    • Binding and regulation of HIF-1α by a subunit of the proteasome complex, PSMA7
    • Cho S., Choi Y., Kim J., Jeong S., Kim J., Kim S., and Ryu S. Binding and regulation of HIF-1α by a subunit of the proteasome complex, PSMA7. FEBS Lett. 498 (2001) 62-66
    • (2001) FEBS Lett. , vol.498 , pp. 62-66
    • Cho, S.1    Choi, Y.2    Kim, J.3    Jeong, S.4    Kim, J.5    Kim, S.6    Ryu, S.7
  • 7
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., and Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65 (1996) 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 8
    • 0035856481 scopus 로고    scopus 로고
    • Activated c-Abl is degraded by the ubiquitin-dependent proteasome pathway
    • Echarri A., and Pendergast A.M. Activated c-Abl is degraded by the ubiquitin-dependent proteasome pathway. Curr. Biol. 11 (2001) 1759-1765
    • (2001) Curr. Biol. , vol.11 , pp. 1759-1765
    • Echarri, A.1    Pendergast, A.M.2
  • 9
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 10
    • 0019127191 scopus 로고
    • Structure of the Abelson murine leukemia virus genome and the homologous cellular gene Studies with cloned viral DNA
    • Goff S., Gilboa E., Witte O., and Baltimore D. Structure of the Abelson murine leukemia virus genome and the homologous cellular gene Studies with cloned viral DNA. Cell 22 (1980) 777-785
    • (1980) Cell , vol.22 , pp. 777-785
    • Goff, S.1    Gilboa, E.2    Witte, O.3    Baltimore, D.4
  • 13
    • 0033600234 scopus 로고    scopus 로고
    • The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage
    • Gong J., Costanzo A., Yang H., Melino G., Kaelin Jr. W., Levrero M., and Wang J.Y.J. The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage. Nature 399 (1999) 806-809
    • (1999) Nature , vol.399 , pp. 806-809
    • Gong, J.1    Costanzo, A.2    Yang, H.3    Melino, G.4    Kaelin Jr., W.5    Levrero, M.6    Wang, J.Y.J.7
  • 14
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome
    • Grune T., Reinheckel T., Joshi M., and Davis K.J. Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome. J. Biol. Chem. 270 (1995) 2344-2351
    • (1995) J. Biol. Chem. , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davis, K.J.4
  • 15
    • 0030724422 scopus 로고    scopus 로고
    • Role of ubiquitin-mediated proteolysis in cel cycle control
    • Hershko A. Role of ubiquitin-mediated proteolysis in cel cycle control. Curr. Opin. Cell Biol. 9 (1997) 788-799
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 788-799
    • Hershko, A.1
  • 16
    • 5644266525 scopus 로고    scopus 로고
    • Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes
    • Horiguchi R., Yoshikuni M., Tokumoto M., Nagahama Y., and Tokumoto T. Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes. Cell. Signal. 17 (2005) 205-215
    • (2005) Cell. Signal. , vol.17 , pp. 205-215
    • Horiguchi, R.1    Yoshikuni, M.2    Tokumoto, M.3    Nagahama, Y.4    Tokumoto, T.5
  • 17
    • 0032816238 scopus 로고    scopus 로고
    • Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome comoplex
    • Hu Z., Zhang Z., Doo E., Coux O., Goldberg A.L., and Liang T.J. Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome comoplex. J. Virol. 73 (1999) 7231-7240
    • (1999) J. Virol. , vol.73 , pp. 7231-7240
    • Hu, Z.1    Zhang, Z.2    Doo, E.3    Coux, O.4    Goldberg, A.L.5    Liang, T.J.6
  • 18
    • 0029986179 scopus 로고    scopus 로고
    • Proteasome complex as a potential cellular target of hepatitis B virus X protein
    • Huang J., Kwong J., Sun E.C.-Y., and Liang T.J. Proteasome complex as a potential cellular target of hepatitis B virus X protein. J. Virol. 70 (1996) 5582-5591
    • (1996) J. Virol. , vol.70 , pp. 5582-5591
    • Huang, J.1    Kwong, J.2    Sun, E.C.-Y.3    Liang, T.J.4
  • 19
    • 0036177305 scopus 로고    scopus 로고
    • Electrpohoretic analysis of phosphorylation of the yeast 20S proteasome
    • Iwafune Y., Kawasaki H., and Hirano H. Electrpohoretic analysis of phosphorylation of the yeast 20S proteasome. Electrophoresis 23 (2002) 329-338
    • (2002) Electrophoresis , vol.23 , pp. 329-338
    • Iwafune, Y.1    Kawasaki, H.2    Hirano, H.3
  • 20
    • 0035984188 scopus 로고    scopus 로고
    • Inactivation of NF-kappaB-dependent cell survival, a novel mechanism for the proapoptotic function of c-Abl
    • Kawai H., Nie L., and Yuan Z.M. Inactivation of NF-kappaB-dependent cell survival, a novel mechanism for the proapoptotic function of c-Abl. Mol. Cell. Biol. 22 (2002) 6079-6088
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6079-6088
    • Kawai, H.1    Nie, L.2    Yuan, Z.M.3
  • 21
    • 0026551960 scopus 로고
    • Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA
    • Kipreos E.T., and Wang J.Y.J. Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA. Science 256 (1992) 382-385
    • (1992) Science , vol.256 , pp. 382-385
    • Kipreos, E.T.1    Wang, J.Y.J.2
  • 22
    • 3242771511 scopus 로고    scopus 로고
    • Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII
    • Kloetzel P.M. Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII. Nat. Immunol. 5 (2004) 661-669
    • (2004) Nat. Immunol. , vol.5 , pp. 661-669
    • Kloetzel, P.M.1
  • 24
    • 0025328751 scopus 로고
    • The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases
    • Kruh G.D., Perego R., Miki T., and Aaronson S.S. The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases. Proc. Natl. Acad. Sci. USA 87 (1990) 5802-5806
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5802-5806
    • Kruh, G.D.1    Perego, R.2    Miki, T.3    Aaronson, S.S.4
  • 25
    • 0032567339 scopus 로고    scopus 로고
    • Generation of destabilized green fluorescent protein as a transcription reporter
    • Li X., Zhao X., Fang Y., Jiang X., Duong T., Fan C., Huang C.C., and Kain S.R. Generation of destabilized green fluorescent protein as a transcription reporter. J. Biol. Chem. 273 (1998) 34970-34975
    • (1998) J. Biol. Chem. , vol.273 , pp. 34970-34975
    • Li, X.1    Zhao, X.2    Fang, Y.3    Jiang, X.4    Duong, T.5    Fan, C.6    Huang, C.C.7    Kain, S.R.8
  • 26
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: mechanisms of regulation and signaling
    • Pendergast A.M. The Abl family kinases: mechanisms of regulation and signaling. Adv. Cancer Res. 85 (2002) 51-100
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 27
    • 0033568349 scopus 로고    scopus 로고
    • c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
    • Plattner R., Kadlec L., DeMali K.A., Kazlauskas A., and Pendergast A.M. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13 (1999) 2400-2411
    • (1999) Genes Dev. , vol.13 , pp. 2400-2411
    • Plattner, R.1    Kadlec, L.2    DeMali, K.A.3    Kazlauskas, A.4    Pendergast, A.M.5
  • 29
    • 0029952689 scopus 로고    scopus 로고
    • Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure
    • Strack P.R., Waxman L., and Fagan J.M. Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure. Biochemistry 35 (1996) 7142-7149
    • (1996) Biochemistry , vol.35 , pp. 7142-7149
    • Strack, P.R.1    Waxman, L.2    Fagan, J.M.3
  • 30
    • 0034677930 scopus 로고    scopus 로고
    • Interaction between protein kinase C δ and the c-Abl tyrosine kinase in the cellular response to oxidative stress
    • Sun X., Wu F., Datta R., Kharbanda S., and Kufe D. Interaction between protein kinase C δ and the c-Abl tyrosine kinase in the cellular response to oxidative stress. J. Biol. Chem. 275 (2000) 7470-7473
    • (2000) J. Biol. Chem. , vol.275 , pp. 7470-7473
    • Sun, X.1    Wu, F.2    Datta, R.3    Kharbanda, S.4    Kufe, D.5
  • 31
    • 0038745373 scopus 로고    scopus 로고
    • c-Abl stabilizes p73 by a phosphorylation-augmented interaction
    • Tsai K.K., and Yuan Z.M. c-Abl stabilizes p73 by a phosphorylation-augmented interaction. Cancer Res. 63 (2003) 3418-3424
    • (2003) Cancer Res. , vol.63 , pp. 3418-3424
    • Tsai, K.K.1    Yuan, Z.M.2
  • 32
    • 0025780879 scopus 로고
    • Neuonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz V.L.J., Crawford C.E., Jackson P.K., Bronson R.T., and Mulligan R.C. Neuonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell 65 (1991) 1153-1163
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.J.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 33
    • 0032937828 scopus 로고    scopus 로고
    • Cycling, stressed out and nervous: Cellular functions of c-Abl
    • Van Etten R.A. Cycling, stressed out and nervous: Cellular functions of c-Abl. Trends Cell Biol. 9 (1999) 179-186
    • (1999) Trends Cell Biol. , vol.9 , pp. 179-186
    • Van Etten, R.A.1
  • 34
    • 0028084328 scopus 로고
    • The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-Actin binding domains with bundling activity
    • Van Etten R.A., Jackson P.K., Baltimore D., Standers M.C., Matsuddaira P.T., and Janmey P.A. The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-Actin binding domains with bundling activity. J. Cell Biol. 124 (1994) 325-340
    • (1994) J. Cell Biol. , vol.124 , pp. 325-340
    • Van Etten, R.A.1    Jackson, P.K.2    Baltimore, D.3    Standers, M.C.4    Matsuddaira, P.T.5    Janmey, P.A.6
  • 35
    • 0037719729 scopus 로고    scopus 로고
    • The N-end rule and regulation of apoptosis
    • Varshavsky A. The N-end rule and regulation of apoptosis. Nat. Cell Biol. 5 (2003) 373-376
    • (2003) Nat. Cell Biol. , vol.5 , pp. 373-376
    • Varshavsky, A.1
  • 36
    • 20444404618 scopus 로고    scopus 로고
    • Regulated protein degradation
    • Varshavsky A. Regulated protein degradation. Trends Biochem. Sci. 30 (2005) 283-286
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 283-286
    • Varshavsky, A.1
  • 37
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., and Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68 (1999) 1051-1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1051-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3


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