메뉴 건너뛰기




Volumn 11, Issue 11, 2004, Pages 1114-1121

PML bodies control the nuclear dynamics and function of the CHFR mitotic checkpoint protein

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN;

EID: 7544227866     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb837     Document Type: Article
Times cited : (28)

References (29)
  • 1
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • Melnick, A. & Licht, J.D. Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93, 3167-3215 (1999)
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 3
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen, K., Shiels, C. & Freemont, P.S. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20, 7223-7233 (2001).
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 4
    • 0000237552 scopus 로고    scopus 로고
    • Role of PML in cell growth and the retinoic acid pathway
    • Wang, Z.G. et al. Role of PML in cell growth and the retinoic acid pathway. Science 279, 1547-1551 (1998).
    • (1998) Science , vol.279 , pp. 1547-1551
    • Wang, Z.G.1
  • 5
    • 1342291118 scopus 로고    scopus 로고
    • Loss of the tumor suppressor PML in human cancers of multiple histologic origins
    • Gurrieri, C. et al. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J. Natl. Cancer Inst. 96, 269-279 (2004).
    • (2004) J. Natl. Cancer Inst. , vol.96 , pp. 269-279
    • Gurrieri, C.1
  • 6
    • 0343776952 scopus 로고    scopus 로고
    • Role of SUMO-1-modified PML in nuclear body formation
    • Zhong, S., Muller, S., Freemont, P.S., Dejean, A. & Pandolfi, P.P. Role of SUMO-1-modified PML in nuclear body formation. Blood 95, 2748-2753 (2000).
    • (2000) Blood , vol.95 , pp. 2748-2753
    • Zhong, S.1    Muller, S.2    Freemont, P.S.3    Dejean, A.4    Pandolfi, P.P.5
  • 7
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni, P. & Pandolfi, P.P. The role of PML in tumor suppression. Cell 108, 165-170 (2002).
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 8
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P. & Pandolfi P.P. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2, E85-E90 (2000).
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 9
    • 0034721154 scopus 로고    scopus 로고
    • Chfr defines a mitotic stress checkpoint that delays entry into metaphase
    • Scolnick, D.M. & Halazonetis, T.D. Chfr defines a mitotic stress checkpoint that delays entry into metaphase. Nature 406, 430-435 (2000).
    • (2000) Nature , vol.406 , pp. 430-435
    • Scolnick, D.M.1    Halazonetis, T.D.2
  • 10
    • 0037086283 scopus 로고    scopus 로고
    • Chfr regulates a mitotic stress pathway through its RING-finger domain with ubiquitin ligase activity
    • Chaturvedi, P, et al. Chfr regulates a mitotic stress pathway through its RING-finger domain with ubiquitin ligase activity. Cancer Res. 62, 1797-1801 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 1797-1801
    • Chaturvedi, P.1
  • 11
    • 0034851781 scopus 로고    scopus 로고
    • Nuclear domains
    • Spector, D.L. Nuclear domains. J. Cell Sci. 114, 2891-2893 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 2891-2893
    • Spector, D.L.1
  • 12
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S., Matunis, M.J. & Dejean, A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70 (1998).
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 14
    • 0034618664 scopus 로고    scopus 로고
    • Microtubule disassembly delays the G2-M transition in vertebrates
    • Rieder, C.L. & Cole, R. Microtubule disassembly delays the G2-M transition in vertebrates. Curr. Biol. 10, 1067-1070 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 1067-1070
    • Rieder, C.L.1    Cole, R.2
  • 15
    • 0242551691 scopus 로고    scopus 로고
    • The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains
    • Bothos, J., Summers, M.K., Venere, M., Scolnick, D.M. & Halazonetis, T.D. The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains. Oncogene 22, 7101-7107 (2003).
    • (2003) Oncogene , vol.22 , pp. 7101-7107
    • Bothos, J.1    Summers, M.K.2    Venere, M.3    Scolnick, D.M.4    Halazonetis, T.D.5
  • 16
    • 0029010740 scopus 로고
    • The PML gene encodes a phosphoprotein associated with the nuclear matrix
    • Chang, K.S., Fan, Y.H., Andreeff, M., Liu, J. & Mu, Z.M. The PML gene encodes a phosphoprotein associated with the nuclear matrix. Blood 85, 3646-3653 (1995).
    • (1995) Blood , vol.85 , pp. 3646-3653
    • Chang, K.S.1    Fan, Y.H.2    Andreeff, M.3    Liu, J.4    Mu, Z.M.5
  • 17
    • 0037148527 scopus 로고    scopus 로고
    • The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition
    • Kang, D., Chen, J., Wong, J. & Fang, G. The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition. J. Cell Biol. 156, 249-259 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 249-259
    • Kang, D.1    Chen, J.2    Wong, J.3    Fang, G.4
  • 18
    • 0037972167 scopus 로고    scopus 로고
    • Scores of RINGS but no PHDs in ubiquitin signaling
    • Aravind, L., Iyer, L.M. & Koonin, E.V. Scores of RINGS but no PHDs in ubiquitin signaling. Cell Cycle 2, 123-126 (2003).
    • (2003) Cell Cycle , vol.2 , pp. 123-126
    • Aravind, L.1    Iyer, L.M.2    Koonin, E.V.3
  • 19
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert, F-M., Hendzel, M. & Bazlett-Jones, D.P. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148, 283-292 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 283-292
    • Boisvert, F.-M.1    Hendzel, M.2    Bazlett-Jones, D.P.3
  • 20
    • 0037275750 scopus 로고    scopus 로고
    • Frequent hypermethylation of the 5′ CpG island of the mitotic stress checkpoint gene Chfr in colorectal and non-small cell lung cancer
    • Corn, P.G. et al. Frequent hypermethylation of the 5′ CpG island of the mitotic stress checkpoint gene Chfr in colorectal and non-small cell lung cancer. Carcinogenesis, 24, 47-51 (2003).
    • (2003) Carcinogenesis , vol.24 , pp. 47-51
    • Corn, P.G.1
  • 21
    • 0037934421 scopus 로고    scopus 로고
    • Epigenetic inactivation of CHFR in human tumors
    • Toyota, M. et al. Epigenetic inactivation of CHFR in human tumors. Proc. Natl. Acad. Sci. USA 100, 7818-7823 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7818-7823
    • Toyota, M.1
  • 22
    • 0242442559 scopus 로고    scopus 로고
    • Inactivating mutations targeting the chfr mitotic checkpoint gene in human lung cancer
    • Mariatos, G. et al. Inactivating mutations targeting the chfr mitotic checkpoint gene in human lung cancer. Cancer Res. 63, 7185-7189 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 7185-7189
    • Mariatos, G.1
  • 23
    • 9144239265 scopus 로고    scopus 로고
    • Epigenetic inactivation of CHFR and sensitivity to microtubule inhibitors in gastric cancer
    • Satoh, A. et al. Epigenetic inactivation of CHFR and sensitivity to microtubule inhibitors in gastric cancer. Cancer Res. 63, 8606-8613 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 8606-8613
    • Satoh, A.1
  • 24
    • 0024147427 scopus 로고
    • A glial cell line promotes the outgrowth of neuritis from embryonic Xenopus retina
    • Sakaguchi, D.S., Coffman, C.R., Gallenson, N. & Harris, W.A. A glial cell line promotes the outgrowth of neuritis from embryonic Xenopus retina. Acta Biol. Hung. 39, 201-209 (1988).
    • (1988) Acta Biol. Hung. , vol.39 , pp. 201-209
    • Sakaguchi, D.S.1    Coffman, C.R.2    Gallenson, N.3    Harris, W.A.4
  • 25
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders, E.M., Stap, J., Brakenhoff, G., van Driel, R. & Aten, J.A. Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J. Cell Sci. 103, 857-862 (1992).
    • (1992) J. Cell Sci. , vol.103 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.3    Van Driel, R.4    Aten, J.A.5
  • 26
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens, P.I., Majoul, I.V., Verveer, P.J., Soling, H.D. & Jovin, T.M. Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J. 15, 4246-4253 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4246-4253
    • Bastiaens, P.I.1    Majoul, I.V.2    Verveer, P.J.3    Soling, H.D.4    Jovin, T.M.5
  • 27
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg, J. et al. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138, 1193-1206 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1
  • 28
    • 0242298319 scopus 로고    scopus 로고
    • Dynamic control of Rad51 recombinase by self-association and interaction with BRCA2
    • Yu, D.S. et al. Dynamic control of Rad51 recombinase by self-association and interaction with BRCA2. Mol. Cell 12, 1029-1041 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1029-1041
    • Yu, D.S.1
  • 29
    • 0024115313 scopus 로고
    • Mitotic chromosome structure
    • Earnshaw, W.C. Mitotic chromosome structure. Bioessays 9, 147-150 (1988).
    • (1988) Bioessays , vol.9 , pp. 147-150
    • Earnshaw, W.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.