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Volumn 10, Issue 4, 2015, Pages 484-496

c-Abl regulates proteasome abundance by controlling the ubiquitin-proteasomal degradation of PSMA7 subunit

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; BRCA1 PROTEIN; CELL PROTEIN; PROTEASOME; PSMA7 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; PSMA7 PROTEIN, HUMAN;

EID: 84922789202     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.12.044     Document Type: Article
Times cited : (31)

References (47)
  • 1
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • Aiken C.T., Kaake R.M., Wang X., Huang L. Oxidative stress-mediated regulation of proteasome complexes. Mol. Cell. Proteomics 2011, 10:006924.
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 006924
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 3
    • 0042905738 scopus 로고    scopus 로고
    • Catalase activity is regulated by c-Abl and Arg in the oxidative stress response
    • Cao C., Leng Y., Kufe D. Catalase activity is regulated by c-Abl and Arg in the oxidative stress response. J.Biol. Chem. 2003, 278:29667-29675.
    • (2003) J.Biol. Chem. , vol.278 , pp. 29667-29675
    • Cao, C.1    Leng, Y.2    Kufe, D.3
  • 5
    • 0035370123 scopus 로고    scopus 로고
    • Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7
    • Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E. Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7. FEBS Lett. 2001, 498:62-66.
    • (2001) FEBS Lett. , vol.498 , pp. 62-66
    • Cho, S.1    Choi, Y.J.2    Kim, J.M.3    Jeong, S.T.4    Kim, J.H.5    Kim, S.H.6    Ryu, S.E.7
  • 7
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma N.P., Lindsten K., Glas R., Jellne M., Masucci M.G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 2000, 18:538-543.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 9
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 2009, 78:477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 12
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • Grune T., Catalgol B., Licht A., Ermak G., Pickering A.M., Ngo J.K., Davies K.J. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress. Free Radic. Biol. Med. 2011, 51:1355-1364.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1355-1364
    • Grune, T.1    Catalgol, B.2    Licht, A.3    Ermak, G.4    Pickering, A.M.5    Ngo, J.K.6    Davies, K.J.7
  • 14
    • 21544475903 scopus 로고    scopus 로고
    • IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink S., Ludwig D., Kloetzel P.M., Krüger E. IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Natl. Acad. Sci. USA 2005, 102:9241-9246.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Krüger, E.4
  • 16
    • 84857313367 scopus 로고    scopus 로고
    • Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity
    • Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M. Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell 2012, 148:727-738.
    • (2012) Cell , vol.148 , pp. 727-738
    • Huber, E.M.1    Basler, M.2    Schwab, R.3    Heinemeyer, W.4    Kirk, C.J.5    Groettrup, M.6    Groll, M.7
  • 17
    • 0033118399 scopus 로고    scopus 로고
    • Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer
    • Jørgensen L., Hendil K.B. Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer. Mol. Biol. Rep. 1999, 26:119-123.
    • (1999) Mol. Biol. Rep. , vol.26 , pp. 119-123
    • Jørgensen, L.1    Hendil, K.B.2
  • 25
    • 77955503621 scopus 로고    scopus 로고
    • Ecm29 fulfils quality control functions in proteasome assembly
    • Lehmann A., Niewienda A., Jechow K., Janek K., Enenkel C. Ecm29 fulfils quality control functions in proteasome assembly. Mol. Cell 2010, 38:879-888.
    • (2010) Mol. Cell , vol.38 , pp. 879-888
    • Lehmann, A.1    Niewienda, A.2    Jechow, K.3    Janek, K.4    Enenkel, C.5
  • 26
    • 77954660827 scopus 로고    scopus 로고
    • C-Abl and Arg tyrosine kinases regulate lysosomal degradation of the oncoprotein Galectin-3
    • Li X., Ma Q., Wang J., Liu X., Yang Y., Zhao H., Wang Y., Jin Y., Zeng J., Li J., et al. c-Abl and Arg tyrosine kinases regulate lysosomal degradation of the oncoprotein Galectin-3. Cell Death Differ. 2010, 17:1277-1287.
    • (2010) Cell Death Differ. , vol.17 , pp. 1277-1287
    • Li, X.1    Ma, Q.2    Wang, J.3    Liu, X.4    Yang, Y.5    Zhao, H.6    Wang, Y.7    Jin, Y.8    Zeng, J.9    Li, J.10
  • 27
    • 33646145066 scopus 로고    scopus 로고
    • Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation
    • Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C. Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation. Mol. Cell 2006, 22:317-327.
    • (2006) Mol. Cell , vol.22 , pp. 317-327
    • Liu, X.1    Huang, W.2    Li, C.3    Li, P.4    Yuan, J.5    Li, X.6    Qiu, X.B.7    Ma, Q.8    Cao, C.9
  • 29
    • 10444224552 scopus 로고    scopus 로고
    • Proteasome proteolytic activity in hematopoietic cells from patients with chronic myeloid leukemia and multiple myeloma
    • Magill L., Lynas J., Morris T.C., Walker B., Irvine A.E. Proteasome proteolytic activity in hematopoietic cells from patients with chronic myeloid leukemia and multiple myeloma. Haematologica 2004, 89:1428-1433.
    • (2004) Haematologica , vol.89 , pp. 1428-1433
    • Magill, L.1    Lynas, J.2    Morris, T.C.3    Walker, B.4    Irvine, A.E.5
  • 31
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon A., Goldberg A.L. Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 2001, 8:1339-1349.
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 32
    • 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. 2002, 85:51-100.
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 33
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: proteases in the machine age
    • Pickart C.M., Cohen R.E. Proteasomes and their kin: proteases in the machine age. Nat. Rev. Mol. Cell Biol. 2004, 5:177-187.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 34
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress
    • Pickering A.M., Linder R.A., Zhang H., Forman H.J., Davies K.J. Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress. J.Biol. Chem. 2012, 287:10021-10031.
    • (2012) J.Biol. Chem. , vol.287 , pp. 10021-10031
    • Pickering, A.M.1    Linder, R.A.2    Zhang, H.3    Forman, H.J.4    Davies, K.J.5
  • 35
    • 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., 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. 1999, 13:2400-2411.
    • (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
  • 36
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • Radhakrishnan S.K., Lee C.S., Young P., Beskow A., Chan J.Y., Deshaies R.J. Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol. Cell 2010, 38:17-28.
    • (2010) Mol. Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 38
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren R., Mayer B.J., Cicchetti P., Baltimore D. Identification of a ten-amino acid proline-rich SH3 binding site. Science 1993, 259:1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 42
    • 66349096607 scopus 로고    scopus 로고
    • PALB2 is an integral component of the BRCA complex required for homologous recombination repair
    • Sy S.M., Huen M.S., Chen J. PALB2 is an integral component of the BRCA complex required for homologous recombination repair. Proc. Natl. Acad. Sci. USA 2009, 106:7155-7160.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7155-7160
    • Sy, S.M.1    Huen, M.S.2    Chen, J.3
  • 43
    • 1442264792 scopus 로고    scopus 로고
    • Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast
    • Velichutina I., Connerly P.L., Arendt C.S., Li X., Hochstrasser M. Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. EMBO J. 2004, 23:500-510.
    • (2004) EMBO J. , vol.23 , pp. 500-510
    • Velichutina, I.1    Connerly, P.L.2    Arendt, C.S.3    Li, X.4    Hochstrasser, M.5
  • 45
    • 0037155196 scopus 로고    scopus 로고
    • Analysis of Drosophila 26S proteasome using RNA interference
    • Wójcik C., DeMartino G.N. Analysis of Drosophila 26S proteasome using RNA interference. J.Biol. Chem. 2002, 277:6188-6197.
    • (2002) J.Biol. Chem. , vol.277 , pp. 6188-6197
    • Wójcik, C.1    DeMartino, G.N.2
  • 46
    • 0035853037 scopus 로고    scopus 로고
    • RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit
    • Xie Y., Varshavsky A. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc. Natl. Acad. Sci. USA 2001, 98:3056-3061.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3056-3061
    • Xie, Y.1    Varshavsky, A.2
  • 47
    • 84922814898 scopus 로고    scopus 로고
    • Inhibition of proteasome by bortezomib increase chemosensitivity of bcr/abl positive human k562 chronic myleoid leukemia cells to imatinib
    • Yusuf B., Oztekin C., Yonca B. Inhibition of proteasome by bortezomib increase chemosensitivity of bcr/abl positive human k562 chronic myleoid leukemia cells to imatinib. Health 2009, 1:320-324.
    • (2009) Health , vol.1 , pp. 320-324
    • Yusuf, B.1    Oztekin, C.2    Yonca, B.3


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