메뉴 건너뛰기




Volumn 287, Issue 10, 2012, Pages 7495-7502

The C-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (BRCA1) is degraded by the N-end rule pathway

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC PATHWAYS; ASPARTATES; BREAST CANCER; C-TERMINAL FRAGMENTS; CASPASES; GENE PRODUCTS; N-TERMINALS; PROTEOLYTIC FRAGMENTS; WILD TYPES;

EID: 84863249152     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.301002     Document Type: Article
Times cited : (28)

References (47)
  • 6
    • 33749000596 scopus 로고    scopus 로고
    • The role of BRCA1 in transcriptional regulation and cell cycle control
    • DOI 10.1038/sj.onc.1209872, PII 1209872
    • Mullan, P. B., Quinn, J. E., and Harkin, D. P. (2006) The role of BRCA1 in transcriptional regulation and cell cycle control. Oncogene 25, 5854-5863 (Pubitemid 44453441)
    • (2006) Oncogene , vol.25 , Issue.43 , pp. 5854-5863
    • Mullan, P.B.1    Quinn, J.E.2    Harkin, D.P.3
  • 7
    • 79953134742 scopus 로고    scopus 로고
    • The role of BRCA1 in DNA damage response
    • Wu, J., Lu, L. Y., and Yu, X. (2010) The role of BRCA1 in DNA damage response. Protein Cell 1, 117-123
    • (2010) Protein Cell , vol.1 , pp. 117-123
    • Wu, J.1    Lu, L.Y.2    Yu, X.3
  • 8
    • 77953952646 scopus 로고    scopus 로고
    • BRCA1 and BRCA2. Breast/ovarian cancer susceptibility gene products and participants in DNA double-strand break repair
    • O'Donovan, P. J., and Livingston, D. M. (2010) BRCA1 and BRCA2. Breast/ovarian cancer susceptibility gene products and participants in DNA double-strand break repair. Carcinogenesis 31, 961-967
    • (2010) Carcinogenesis , vol.31 , pp. 961-967
    • O'Donovan, P.J.1    Livingston, D.M.2
  • 9
    • 75149189204 scopus 로고    scopus 로고
    • BRCA1 and its toolbox for the maintenance of genome integrity
    • Huen, M. S., Sy, S. M., and Chen, J. (2010) BRCA1 and its toolbox for the maintenance of genome integrity. Nat. Rev. Mol. Cell Biol. 11, 138-148
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 138-148
    • Huen, M.S.1    Sy, S.M.2    Chen, J.3
  • 11
    • 4043130959 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of the BRCA1 tumor suppressor is regulated during cell cycle progression
    • DOI 10.1074/jbc.M403646200
    • Choudhury, A. D., Xu, H., and Baer, R. (2004) Ubiquitination and proteasomal degradation of the BRCA1 tumor suppressor is regulated during cell cycle progression. J. Biol. Chem. 279, 33909-33918 (Pubitemid 39063041)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33909-33918
    • Choudhury, A.D.1    Xu, H.2    Baer, R.3
  • 12
    • 33847217581 scopus 로고    scopus 로고
    • Ubiquitination and proteasome-mediated degradation of BRCA1 and BARD1 during steroidogenesis in human ovarian granulosa cells
    • Lu, Y., Amleh, A., Sun, J., Jin, X., McCullough, S. D., Baer, R., Ren, D., Li, R., and Hu, Y. (2007) Ubiquitination and proteasome-mediated degradation of BRCA1 and BARD1 during steroidogenesis in human ovarian granulosa cells. Mol. Endocrinol. 21, 651-663
    • (2007) Mol. Endocrinol. , vol.21 , pp. 651-663
    • Lu, Y.1    Amleh, A.2    Sun, J.3    Jin, X.4    McCullough, S.D.5    Baer, R.6    Ren, D.7    Li, R.8    Hu, Y.9
  • 13
    • 0035491589 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of BRCA1 protein in MCF-7 human breast cancer cells
    • Choi, Y. H. (2001) Proteasome-mediated degradation of BRCA1 protein in MCF-7 human breast cancer cells. Int. J. Oncol. 19, 687-693
    • (2001) Int. J. Oncol. , vol.19 , pp. 687-693
    • Choi, Y.H.1
  • 14
    • 79251496438 scopus 로고    scopus 로고
    • Turnover of BRCA1 involves in radiation-induced apoptosis
    • Liu, W., Zong, W., Wu, G., Fujita, T., Li, W., Wu, J., and Wan, Y. (2010) Turnover of BRCA1 involves in radiation-induced apoptosis. PLoS One 5, e14484
    • (2010) PLoS One , vol.5
    • Liu, W.1    Zong, W.2    Wu, G.3    Fujita, T.4    Li, W.5    Wu, J.6    Wan, Y.7
  • 15
    • 33947359114 scopus 로고    scopus 로고
    • E2F6 negatively regulates ultraviolet-induced apoptosis via modulation of BRCA1
    • DOI 10.1038/sj.cdd.4402062, PII 4402062
    • Yang, W. W., Wang, Z. H., Zhu, Y., and Yang, H. T. (2007) E2F6 negatively regulates ultraviolet-induced apoptosis via modulation of BRCA1. Cell Death Differ. 14, 807-817 (Pubitemid 46444518)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , pp. 807-817
    • Yang, W.-W.1    Wang, Z.-H.2    Zhu, Y.3    Yang, H.-T.4
  • 16
    • 0037043778 scopus 로고    scopus 로고
    • Caspase-3 mediated cleavage of BRCA1 during UV-induced apoptosis
    • DOI 10.1038/sj.onc.1205665
    • Zhan, Q., Jin, S., Ng, B., Plisket, J., Shangary, S., Rathi, A., Brown, K. D., and Baskaran, R. (2002) Caspase-3 mediated cleavage of BRCA1 during UVinduced apoptosis. Oncogene 21, 5335-5345 (Pubitemid 34948144)
    • (2002) Oncogene , vol.21 , Issue.34 , pp. 5335-5345
    • Zhan, Q.1    Jin, S.2    Ng, B.3    Plisket, J.4    Shangary, S.5    Rathi, A.6    Brown, K.D.7    Baskaran, R.8
  • 17
    • 38649099682 scopus 로고    scopus 로고
    • Caspase-dependent BRCA1 cleavage facilitates chemotherapy-induced apoptosis
    • Dizin, E., Ray, H., Suau, F., Voeltzel, T., and Dalla Venezia, N. (2008) Caspase-dependent BRCA1 cleavage facilitates chemotherapy-induced apoptosis. Apoptosis 13, 237-246
    • (2008) Apoptosis , vol.13 , pp. 237-246
    • Dizin, E.1    Ray, H.2    Suau, F.3    Voeltzel, T.4    Dalla Venezia, N.5
  • 18
    • 79961117807 scopus 로고    scopus 로고
    • BRCT domains. Easy as one, two, three
    • Leung, C. C., and Glover, J. N. (2011) BRCT domains. Easy as one, two, three. Cell Cycle 10, 2461-2470
    • (2011) Cell Cycle , vol.10 , pp. 2461-2470
    • Leung, C.C.1    Glover, J.N.2
  • 19
    • 0031914287 scopus 로고    scopus 로고
    • Proteases, proteolysis, and apoptosis
    • DOI 10.1023/A:1007481921502
    • Solary, E., Eymin, B., Droin, N., and Haugg, M. (1998) Proteases, proteolysis, and apoptosis. Cell Biol. Toxicol. 14, 121-132 (Pubitemid 28123602)
    • (1998) Cell Biology and Toxicology , vol.14 , Issue.2 , pp. 121-132
    • Solary, E.1    Eymin, B.2    Droin, N.3    Haugg, M.4
  • 20
    • 52649141086 scopus 로고    scopus 로고
    • Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini
    • Mahrus, S., Trinidad, J. C., Barkan, D. T., Sali, A., Burlingame, A. L., and Wells, J. A. (2008) Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini. Cell 134, 866-876
    • (2008) Cell , vol.134 , pp. 866-876
    • Mahrus, S.1    Trinidad, J.C.2    Barkan, D.T.3    Sali, A.4    Burlingame, A.L.5    Wells, J.A.6
  • 22
    • 2442547741 scopus 로고    scopus 로고
    • Caspase activation - Stepping on the gas or releasing the brakes? Lessons from humans and flies
    • DOI 10.1038/sj.onc.1207522
    • Salvesen, G. S., and Abrams, J. M. (2004) Caspase activation-stepping on the gas or releasing the brakes? Lessons from humans and flies. Oncogene 23, 2774-2784 (Pubitemid 38638841)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2774-2784
    • Salvesen, G.S.1    Abrams, J.M.2
  • 23
    • 13844253728 scopus 로고    scopus 로고
    • Mathematical modeling of the regulation of caspase-3 activation and degradation
    • DOI 10.1016/j.jtbi.2004.11.011
    • Stucki, J. W., and Simon, H. U. (2005) Mathematical modeling of the regulation of caspase-3 activation and degradation. J. Theor. Biol. 234, 123-131 (Pubitemid 40249854)
    • (2005) Journal of Theoretical Biology , vol.234 , Issue.1 , pp. 123-131
    • Stucki, J.W.1    Simon, H.-U.2
  • 24
    • 33947384611 scopus 로고    scopus 로고
    • Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways
    • DOI 10.1038/sj.cdd.4402079, PII 4402079
    • Herman-Bachinsky, Y., Ryoo, H. D., Ciechanover, A., and Gonen, H. (2007) Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways. Cell Death Differ. 14, 861-871 (Pubitemid 46444523)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , pp. 861-871
    • Herman-Bachinsky, Y.1    Ryoo, H.-D.2    Ciechanover, A.3    Gonen, H.4
  • 25
    • 0037936841 scopus 로고    scopus 로고
    • Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis
    • DOI 10.1038/ncb984
    • Ditzel, M., Wilson, R., Tenev, T., Zachariou, A., Paul, A., Deas, E., and Meier, P. (2003) Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis. Nat. Cell. Biol. 5, 467-473 (Pubitemid 36592271)
    • (2003) Nature Cell Biology , vol.5 , Issue.5 , pp. 467-473
    • Ditzel, M.1    Wilson, R.2    Tenev, T.3    Zachariou, A.4    Paul, A.5    Deas, E.6    Meier, P.7
  • 26
    • 0026316101 scopus 로고
    • The N-end rule in bacteria
    • Tobias, J. W., Shrader, T. E., Rocap, G., and Varshavsky, A. (1991) The N-end rule in bacteria. Science 254, 1374-1377 (Pubitemid 21917472)
    • (1991) Science , vol.254 , Issue.5036 , pp. 1374-1377
    • Tobias, J.W.1    Shrader, T.E.2    Rocap, G.3    Varshavsky, A.4
  • 27
    • 0024562943 scopus 로고
    • The degradation signal in a shortlived protein
    • Bachmair, A., and Varshavsky, A. (1989) The degradation signal in a shortlived protein. Cell 56, 1019-1032
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 29
    • 84855198546 scopus 로고    scopus 로고
    • The N-end rule pathway. From recognition by N-recognins, to destruction by AAA + proteases
    • Dougan, D. A., Micevski, D., and Truscott, K. N. (2012) The N-end rule pathway. From recognition by N-recognins, to destruction by AAA + proteases. Biochim. Biophys. Acta 1823, 83-91
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 83-91
    • Dougan, D.A.1    Micevski, D.2    Truscott, K.N.3
  • 31
    • 77955268037 scopus 로고    scopus 로고
    • The plant N-end rule pathway. Structure and functions
    • Graciet, E., and Wellmer, F. (2010) The plant N-end rule pathway. Structure and functions. Trends Plant Sci. 15, 447-453
    • (2010) Trends Plant Sci. , vol.15 , pp. 447-453
    • Graciet, E.1    Wellmer, F.2
  • 32
    • 33646573377 scopus 로고    scopus 로고
    • Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway
    • An, J. Y., Seo, J. W., Tasaki, T., Lee, M. J., Varshavsky, A., and Kwon, Y. T. (2006) Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 103, 6212-6217
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6212-6217
    • An, J.Y.1    Seo, J.W.2    Tasaki, T.3    Lee, M.J.4    Varshavsky, A.5    Kwon, Y.T.6
  • 33
    • 79960693484 scopus 로고    scopus 로고
    • Alternative ubiquitin activation/conjugation cascades interact with N-end rule ubiquitin ligases to control degradation of RGS proteins
    • Lee, P. C., Sowa, M. E., Gygi, S. P., and Harper, J. W. (2011) Alternative ubiquitin activation/conjugation cascades interact with N-end rule ubiquitin ligases to control degradation of RGS proteins. Mol. Cell 43, 392-405
    • (2011) Mol. Cell , vol.43 , pp. 392-405
    • Lee, P.C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 34
    • 0001602527 scopus 로고    scopus 로고
    • Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway
    • Kwon, Y. T., Kashina, A. S., and Varshavsky, A. (1999) Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Mol. Cell. Biol. 19, 182-193 (Pubitemid 29018421)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 182-193
    • Kwon, Y.T.1    Kashina, A.S.2    Varshavsky, A.3
  • 35
    • 79957773104 scopus 로고    scopus 로고
    • An alternative mechanism for the catalysis of peptide bond formation by L/F transferase. Substrate binding and orientation
    • Fung, A. W., Ebhardt, H. A., Abeysundara, H., Moore, J., Xu, Z., and Fahlman, R. P. (2011) An alternative mechanism for the catalysis of peptide bond formation by L/F transferase. Substrate binding and orientation. J. Mol. Biol. 409, 617-629
    • (2011) J. Mol. Biol. , vol.409 , pp. 617-629
    • Fung, A.W.1    Ebhardt, H.A.2    Abeysundara, H.3    Moore, J.4    Xu, Z.5    Fahlman, R.P.6
  • 37
    • 77956663124 scopus 로고    scopus 로고
    • Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation
    • Zhang, F., Saha, S., Shabalina, S. A., and Kashina, A. (2010) Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. Science 329, 1534-1537
    • (2010) Science , vol.329 , pp. 1534-1537
    • Zhang, F.1    Saha, S.2    Shabalina, S.A.3    Kashina, A.4
  • 38
    • 0034077939 scopus 로고    scopus 로고
    • Multiple epitope tagging of expressed proteins for enhanced detection
    • Hernan, R., Heuermann, K., and Brizzard, B. (2000) Multiple epitope tagging of expressed proteins for enhanced detection. BioTechniques 28, 789-793 (Pubitemid 30198617)
    • (2000) BioTechniques , vol.28 , Issue.4 , pp. 789-793
    • Hernan, R.1    Heuermann, K.2    Brizzard, B.3
  • 39
    • 0029991350 scopus 로고    scopus 로고
    • Transfecting mammalian cells: Optimization of critical parameters affecting calcium-phosphate precipitate formation
    • DOI 10.1093/nar/24.4.596
    • Jordan, M., Schallhorn, A., and Wurm, F. M. (1996) Transfecting mammalian cells. Optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res. 24, 596-601 (Pubitemid 26085833)
    • (1996) Nucleic Acids Research , vol.24 , Issue.4 , pp. 596-601
    • Jordan, M.1    Schallhorn, A.2    Wurm, F.M.3
  • 40
    • 28944437762 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and related methods
    • Varshavsky, A. (2005) Ubiquitin fusion technique and related methods. Methods Enzymol. 399, 777-799
    • (2005) Methods Enzymol. , vol.399 , pp. 777-799
    • Varshavsky, A.1
  • 41
    • 0033674452 scopus 로고    scopus 로고
    • A ubiquitin- based tagging system for controlled modulation of protein stability
    • Stack, J. H., Whitney, M., Rodems, S. M., and Pollok, B. A. (2000) A ubiquitin- based tagging system for controlled modulation of protein stability. Nat. Biotechnol. 18, 1298-1302
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1298-1302
    • Stack, J.H.1    Whitney, M.2    Rodems, S.M.3    Pollok, B.A.4
  • 42
    • 0037025163 scopus 로고    scopus 로고
    • An essential role of N-terminal arginylation in cardiovascular development
    • DOI 10.1126/science.1069531
    • Kwon, Y. T., Kashina, A. S., Davydov, I. V., Hu, R. G., An, J. Y., Seo, J. W., Du, F., and Varshavsky, A. (2002) An essential role of N-terminal arginylation in cardiovascular development. Science 297, 96-99 (Pubitemid 34743100)
    • (2002) Science , vol.297 , Issue.5578 , pp. 96-99
    • Kwon, Y.T.1    Kashina, A.S.2    Davydov, I.V.3    Hu, R.-G.4    An, J.Y.5    Seo, J.W.6    Du, F.7    Varshavsky, A.8
  • 44
    • 0031954631 scopus 로고    scopus 로고
    • MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis
    • Widmann, C., Gerwins, P., Johnson, N. L., Jarpe, M. B., and Johnson, G. L. (1998) MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis. Mol. Cell. Biol. 18, 2416-2429 (Pubitemid 28152687)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.4 , pp. 2416-2429
    • Widmann, C.1    Gerwins, P.2    Johnson, N.L.3    Jarpe, M.B.4    Johnson, G.L.5
  • 45
    • 43449092551 scopus 로고    scopus 로고
    • Killing of macrophages by anthrax lethal toxin: Involvement of the N-end rule pathway
    • DOI 10.1111/j.1462-5822.2008.01131.x
    • Wickliffe, K. E., Leppla, S. H., and Moayeri, M. (2008) Killing of macrophages by anthrax lethal toxin. Involvement of the N-end rule pathway. Cell. Microbiol. 10, 1352-1362 (Pubitemid 351663925)
    • (2008) Cellular Microbiology , vol.10 , Issue.6 , pp. 1352-1362
    • Wickliffe, K.E.1    Leppla, S.H.2    Moayeri, M.3
  • 46
    • 0037719729 scopus 로고    scopus 로고
    • The N-end rule and regulation of apoptosis
    • Varshavsky, A. (2003) The N-end rule and regulation of apoptosis. Nat. Cell Biol. 5, 373-376
    • (2003) Nat. Cell Biol. , vol.5 , pp. 373-376
    • Varshavsky, A.1
  • 47
    • 33646264815 scopus 로고    scopus 로고
    • Post-translational myristoylation of caspaseactivated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events
    • Vilas, G. L., Corvi, M. M., Plummer, G. J., Seime, A. M., Lambkin, G. R., and Berthiaume, L. G. (2006) Post-translational myristoylation of caspaseactivated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. Proc. Natl. Acad. Sci. U.S.A. 103, 6542-6547
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6542-6547
    • Vilas, G.L.1    Corvi, M.M.2    Plummer, G.J.3    Seime, A.M.4    Lambkin, G.R.5    Berthiaume, L.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.