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Volumn 121, Issue 7, 2005, Pages 1085-1095

Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; BH3 PROTEIN; CELL EXTRACT; PROTEASOME INHIBITOR; PROTEIN BCL 2; PROTEIN MCL 1; UBIQUITIN PROTEIN LIGASE;

EID: 21244472965     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.06.009     Document Type: Article
Times cited : (716)

References (40)
  • 1
    • 0035338814 scopus 로고    scopus 로고
    • The WWE domain: A common interaction module in protein ubiquitination and ADP ribosylation
    • L. Aravind The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation Trends Biochem. Sci. 26 2001 273 275
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 273-275
    • Aravind, L.1
  • 2
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • A.C. Carrano, E. Eytan, A. Hershko, and M. Pagano SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27 Nat. Cell Biol. 1 1999 193 199
    • (1999) Nat. Cell Biol. , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 4
    • 2942517678 scopus 로고    scopus 로고
    • Characterisation of Mcl-1 cleavage during apoptosis of haematopoietic cells
    • J.G. Clohessy, J. Zhuang, and H.J. Brady Characterisation of Mcl-1 cleavage during apoptosis of haematopoietic cells Br. J. Haematol. 125 2004 655 665
    • (2004) Br. J. Haematol. , vol.125 , pp. 655-665
    • Clohessy, J.G.1    Zhuang, J.2    Brady, H.J.3
  • 5
    • 0348014686 scopus 로고    scopus 로고
    • DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells
    • A. Cuconati, C. Mukherjee, D. Perez, and E. White DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells Genes Dev. 17 2003 2922 2932
    • (2003) Genes Dev. , vol.17 , pp. 2922-2932
    • Cuconati, A.1    Mukherjee, C.2    Perez, D.3    White, E.4
  • 6
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • N.N. Danial, and S.J. Korsmeyer Cell death: Critical control points Cell 116 2004 205 219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 7
    • 3042686666 scopus 로고    scopus 로고
    • Granulocyte macrophage colony-stimulating factor signaling and proteasome inhibition delay neutrophil apoptosis by increasing the stability of Mcl-1
    • M. Derouet, L. Thomas, A. Cross, R.J. Moots, and S.W. Edwards Granulocyte macrophage colony-stimulating factor signaling and proteasome inhibition delay neutrophil apoptosis by increasing the stability of Mcl-1 J. Biol. Chem. 279 2004 26915 26921
    • (2004) J. Biol. Chem. , vol.279 , pp. 26915-26921
    • Derouet, M.1    Thomas, L.2    Cross, A.3    Moots, R.J.4    Edwards, S.W.5
  • 8
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • C. Du, M. Fang, Y. Li, L. Li, and X. Wang Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition Cell 102 2000 33 42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 9
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • A. Gross, J.M. McDonnell, and S.J. Korsmeyer BCL-2 family members and the mitochondria in apoptosis Genes Dev. 13 1999 1899 1911
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 10
    • 0028225081 scopus 로고
    • Cloning of a DNA binding protein that is a tyrosine kinase substrate and recognizes an upstream initiator-like sequence in the promoter of the preprodynorphin gene
    • J. Gu, K. Ren, R. Dubner, and M.J. Iadarola Cloning of a DNA binding protein that is a tyrosine kinase substrate and recognizes an upstream initiator-like sequence in the promoter of the preprodynorphin gene Brain Res. Mol. Brain Res. 24 1994 77 88
    • (1994) Brain Res. Mol. Brain Res. , vol.24 , pp. 77-88
    • Gu, J.1    Ren, K.2    Dubner, R.3    Iadarola, M.J.4
  • 11
    • 7444243152 scopus 로고    scopus 로고
    • Survival factor-induced extracellylar signal-regulated kinase phosphorylate Bim, inhibiting its association with Bax and proapoptotic activity
    • H. Harada, B. Quearry, A. Ruiz-Vela, and S.J. Korsmeyer Survival factor-induced extracellylar signal-regulated kinase phosphorylate Bim, inhibiting its association with Bax and proapoptotic activity Proc. Natl. Acad. Sci. USA 101 2004 15313 15317
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15313-15317
    • Harada, H.1    Quearry, B.2    Ruiz-Vela, A.3    Korsmeyer, S.J.4
  • 14
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • A. Hershko, H. Heller, S. Elias, and A. Ciechanover Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown J. Biol. Chem. 258 1983 8206 8214
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 15
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • K. Hofmann, and P. Bucher The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway Trends Biochem. Sci. 21 1996 172 173
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 16
    • 0034284309 scopus 로고    scopus 로고
    • Mcl-1 is a common target of stem cell factor and interleukin-5 for apoptosis prevention activity via MEK/MAPK and PI-3K/Akt pathways
    • H.M. Huang, C.J. Huang, and J.J. Yen Mcl-1 is a common target of stem cell factor and interleukin-5 for apoptosis prevention activity via MEK/MAPK and PI-3K/Akt pathways Blood 96 2000 1764 1771
    • (2000) Blood , vol.96 , pp. 1764-1771
    • Huang, H.M.1    Huang, C.J.2    Yen, J.J.3
  • 17
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • J.M. Huibregtse, M. Scheffner, S. Beaudenon, and P.M. Howley A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase Proc. Natl. Acad. Sci. USA 92 1995 2563 2567
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 18
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: The role of the BH3 domain in apoptosis
    • A. Kelekar, and C.B. Thompson Bcl-2-family proteins: the role of the BH3 domain in apoptosis Trends Cell Biol. 8 1998 324 330
    • (1998) Trends Cell Biol. , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 19
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • J.F. Kerr, A.H. Wyllie, and A.R. Currie Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer 26 1972 239 257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 20
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2
    • K.M. Kozopas, T. Yang, H.L. Buchan, P. Zhou, and R.W. Craig MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2 Proc. Natl. Acad. Sci. USA 90 1993 3516 3520
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 22
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • X. Liu, C.N. Kim, J. Yang, R. Jemmerson, and X. Wang Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c Cell 86 1996 147 157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 24
  • 25
    • 0038046166 scopus 로고    scopus 로고
    • Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation
    • D. Nijhawan, M. Fang, E. Traer, Q. Zhong, W. Gao, F. Du, and X. Wang Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation Genes Dev. 17 2003 1475 1486
    • (2003) Genes Dev. , vol.17 , pp. 1475-1486
    • Nijhawan, D.1    Fang, M.2    Traer, E.3    Zhong, Q.4    Gao, W.5    Du, F.6    Wang, X.7
  • 26
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: A novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 27
    • 0348148880 scopus 로고    scopus 로고
    • Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1
    • J.T. Opferman, A. Letai, C. Beard, M.D. Sorcinelli, C.C. Ong, and S.J. Korsmeyer Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1 Nature 426 2003 671 676
    • (2003) Nature , vol.426 , pp. 671-676
    • Opferman, J.T.1    Letai, A.2    Beard, C.3    Sorcinelli, M.D.4    Ong, C.C.5    Korsmeyer, S.J.6
  • 28
  • 29
    • 15744369062 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1-dependent overexpression of myeloid cell factor-1 protects hypoxic cells against tert-butyl hydroperoxide-induced apoptosis
    • 10.1074/jbc.M411858200
    • J.P. Piret, E. Minet, J.P. Cosse, N. Ninane, C. Debacq, M. Raes, and C. Michiels Hypoxia-inducible factor-1-dependent overexpression of myeloid cell factor-1 protects hypoxic cells against tert-butyl hydroperoxide-induced apoptosis J. Biol. Chem. 280 2004 9336 9344 10.1074/jbc.M411858200 Published online December 17, 2004
    • (2004) J. Biol. Chem. , vol.280 , pp. 9336-9344
    • Piret, J.P.1    Minet, E.2    Cosse, J.P.3    Ninane, N.4    Debacq, C.5    Raes, M.6    Michiels, C.7
  • 30
    • 0031464448 scopus 로고    scopus 로고
    • Bcl-2 family proteins: Regulators of apoptosis and chemoresistance in hematologic malignancies
    • J.C. Reed Bcl-2 family proteins: regulators of apoptosis and chemoresistance in hematologic malignancies Semin. Hematol. 34 1997 9 19
    • (1997) Semin. Hematol. , vol.34 , pp. 9-19
    • Reed, J.C.1
  • 32
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • M. Scheffner, U. Nuber, and J.M. Huibregtse Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade Nature 373 1995 81 83
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 33
    • 0034456911 scopus 로고    scopus 로고
    • Recent studies of the ubiquitin system and the N-end rule pathway
    • A. Varshavsky Recent studies of the ubiquitin system and the N-end rule pathway Harvey Lect. 96 2000 93 116
    • (2000) Harvey Lect. , vol.96 , pp. 93-116
    • Varshavsky, A.1
  • 35
    • 15444373128 scopus 로고    scopus 로고
    • Specific cleavage of MCL-1 by caspase-3 in trail-induced apoptosis in Jurkat leukemia T cells
    • C. Weng, Y. Li, D. Xu, Y. Shi, and H. Tang Specific cleavage of MCL-1 by caspase-3 in trail-induced apoptosis in Jurkat leukemia T cells J. Biol. Chem. 280 2005 10491 10500
    • (2005) J. Biol. Chem. , vol.280 , pp. 10491-10500
    • Weng, C.1    Li, Y.2    Xu, D.3    Shi, Y.4    Tang, H.5
  • 37
    • 0028965578 scopus 로고
    • The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2
    • T. Yang, K.M. Kozopas, and R.W. Craig The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2 J. Cell Biol. 128 1995 1173 1184
    • (1995) J. Cell Biol. , vol.128 , pp. 1173-1184
    • Yang, T.1    Kozopas, K.M.2    Craig, R.W.3
  • 38
    • 0029915856 scopus 로고    scopus 로고
    • MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation
    • T. Yang, H.L. Buchan, K.J. Townsend, and R.W. Craig MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation J. Cell. Physiol. 166 1996 523 536
    • (1996) J. Cell. Physiol. , vol.166 , pp. 523-536
    • Yang, T.1    Buchan, H.L.2    Townsend, K.J.3    Craig, R.W.4
  • 39
    • 0037085778 scopus 로고    scopus 로고
    • Myeloid cell factor-1 is a critical survival factor for multiple myeloma
    • B. Zhang, I. Gojo, and R.G. Fenton Myeloid cell factor-1 is a critical survival factor for multiple myeloma Blood 99 2002 1885 1893
    • (2002) Blood , vol.99 , pp. 1885-1893
    • Zhang, B.1    Gojo, I.2    Fenton, R.G.3
  • 40
    • 0031034078 scopus 로고    scopus 로고
    • Mcl-1, a Bcl-2 family member, delays the death of hematopoietic under a variety of apoptosis-inducing conditions
    • P. Zhou, L. Qian, K.M. Kozopas, and R.W. Craig Mcl-1, a Bcl-2 family member, delays the death of hematopoietic under a variety of apoptosis-inducing conditions Blood 89 1997 630 643
    • (1997) Blood , vol.89 , pp. 630-643
    • Zhou, P.1    Qian, L.2    Kozopas, K.M.3    Craig, R.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.