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Science 29 November 1991:
Vol. 254. no. 5036, pp. 1371 - 1374
DOI: 10.1126/science.1720570

Articles

Science, Vol 254, Issue 5036, 1371-1374
Copyright © 1991 by American Association for the Advancement of Science


articles

Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia

AD Goddard, J Borrow, PS Freemont, and E Solomon

Somatic Cell Genetics Laboratory, Imperial Cancer Research Fund, London, United Kingdom.

The translocation t(15;17) associated with acute promyelocytic leukemia results in the fusion of the retinoic acid receptor alpha (RARA) gene to the PML gene. Characterization of PML revealed that it is a putative zinc finger protein and potential transcription factor that is commonly expressed, with at least three major transcription products. PML breakpoints cluster in two regions on either side of an alternatively spliced exon. Although leukemic cells with translocations characteristically express only one fusion product, both PML/RARA (on the 15q+ derivative chromosome) and RARA/PML (on the 17q- derivative) are transcribed.


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SUMO-1 Modification of Human Cytomegalovirus IE1/IE72.
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PAX8-PPARgamma 1 Fusion in Oncogene Human Thyroid Carcinoma.
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J. Cell Biol. 147, 221-234
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Underdeveloped uterus and reduced estrogen responsiveness in mice with disruption of the estrogen-responsive finger protein gene, which is a direct target of estrogen receptor alpha.
A. Orimo, S. Inoue, O. Minowa, N. Tominaga, Y. Tomioka, M. Sato, J. Kuno, H. Hiroi, Y. Shimizu, M. Suzuki, et al. (1999)
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   Abstract »    Full Text »    PDF »
Complete Remission of t(11;17) Positive Acute Promyelocytic Leukemia Induced by All-trans Retinoic Acid and Granulocyte Colony-Stimulating Factor.
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S. Müller and A. Dejean (1999)
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H. Guldner, C Szostecki, P Schroder, U Matschl, K Jensen, C Luders, H Will, and T Sternsdorf (1999)
J. Cell Sci. 112, 733-747
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SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation.
E Duprez, A. Saurin, J. Desterro, V Lallemand-Breitenbach, K Howe, M. Boddy, E Solomon, H de The, R. Hay, and P. Freemont (1999)
J. Cell Sci. 112, 381-393
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S. Vallian, K.-V. Chin, and K.-S. Chang (1998)
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Trivalent Antimonials Induce Degradation of the PML-RARalpha Oncoprotein and Reorganization of the Promyelocytic Leukemia Nuclear Bodies in Acute Promyelocytic Leukemia NB4 Cells.
S. Muller, W. H. Miller Jr, and A. Dejean (1998)
Blood 92, 4308-4316
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H.-L. C. Liu, E. Golder-Novoselsky, M. H. Seto, L. Webster, J. McClary, and D. A. Zajchowski (1998)
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Identification of Three Major Sentrinization Sites in PML.
T. Kamitani, K. Kito, H. P. Nguyen, H. Wada, T. Fukuda-Kamitani, and E. T. H. Yeh (1998)
J. Biol. Chem. 273, 26675-26682
   Abstract »    Full Text »    PDF »
Coactivator TIF1beta Interacts with Transcription Factor C/EBPbeta and Glucocorticoid Receptor To Induce alpha 1-Acid Glycoprotein Gene Expression.
C.-J. Chang, Y.-L. Chen, and S.-C. Lee (1998)
Mol. Cell. Biol. 18, 5880-5887
   Abstract »    Full Text »    PDF »
The Promyelocytic Leukemia Zinc Finger Protein Affects Myeloid Cell Growth, Differentiation, and Apoptosis.
R. Shaknovich, P. L. Yeyati, S. Ivins, A. Melnick, C. Lempert, S. Waxman, A. Zelent, and J. D. Licht (1998)
Mol. Cell. Biol. 18, 5533-5545
   Abstract »    Full Text »    PDF »
The Disruption of ND10 during Herpes Simplex Virus Infection Correlates with the Vmw110- and Proteasome-Dependent Loss of Several PML Isoforms.
R. D. Everett, P. Freemont, H. Saitoh, M. Dasso, A. Orr, M. Kathoria, and J. Parkinson (1998)
J. Virol. 72, 6581-6591
   Abstract »    Full Text »    PDF »
Disruption of PML Subnuclear Domains by the Acidic IE1 Protein of Human Cytomegalovirus Is Mediated through Interaction with PML and May Modulate a RING Finger-Dependent Cryptic Transactivator Function of PML.
J.-H. Ahn, E. J. Brignole III, and G. S. Hayward (1998)
Mol. Cell. Biol. 18, 4899-4913
   Abstract »    Full Text »    PDF »
Two RING Finger Proteins, the Oncoprotein PML and the Arenavirus Z Protein, Colocalize with the Nuclear Fraction of the Ribosomal P Proteins.
K. L. B. Borden, E. J. CampbellDwyer, G. W. Carlile, M. Djavani, and M. S. Salvato (1998)
J. Virol. 72, 3819-3826
   Abstract »    Full Text »    PDF »
Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body.
V. J. LaMorte, J. A. Dyck, R. L. Ochs, and R. M. Evans (1998)
PNAS 95, 4991-4996
   Abstract »    Full Text »    PDF »
Structure and Function in the Nucleus.
A. I. Lamond and W. C. Earnshaw (1998)
Science 280, 547-553
   Abstract »    Full Text »
Reduced Retinoic Acid-Sensitivities of Nuclear Receptor Corepressor Binding to PML- and PLZF-RARalpha Underlie Molecular Pathogenesis and Treatment of Acute Promyelocytic Leukemia.
F. Guidez, S. Ivins, J. Zhu, M. Soderstrom, S. Waxman, and A. Zelent (1998)
Blood 91, 2634-2642
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Role of PML in Cell Growth and the Retinoic Acid Pathway.
Z. Gang Wang, L. Delva, M. Gaboli, R. Rivi, M. Giorgio, C. Cordon-Cardo, F. Grosveld, and P. Paolo Pandolfi (1998)
Science 279, 1547-1551
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An Arenavirus RING (Zinc-Binding) Protein Binds the Oncoprotein Promyelocyte Leukemia Protein (PML) and Relocates PML Nuclear Bodies to the Cytoplasm.
K. L. B. Borden, E. J. Campbell Dwyer, and M. S. Salvato (1998)
J. Virol. 72, 758-766
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Evidence for Covalent Modification of the Nuclear Dot-associated Proteins PML and Sp100 by PIC1/SUMO-1.
T. Sternsdorf, K. Jensen, and H. Will (1997)
J. Cell Biol. 139, 1621-1634
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Characterization of Cryptic Rearrangements and Variant Translocations in Acute Promyelocytic Leukemia.
D. Grimwade, P. Gorman, E. Duprez, K. Howe, S. Langabeer, F. Oliver, H. Walker, D. Culligan, J. Waters, M. Pomfret, et al. (1997)
Blood 90, 4876-4885
   Abstract »    Full Text »    PDF »
Leukemia-associated retinoic acid receptor alpha  fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies.
M. H. M. Koken, A. Reid, F. Quignon, M. K. Chelbi-Alix, J. M. Davies, J. H. S. Kabarowski, J. Zhu, S. Dong, S.-J. Chen, Z. Chen, et al. (1997)
PNAS 94, 10255-10260
   Abstract »    Full Text »    PDF »
Characterization of the Retinoid Binding Properties of the Major Fusion Products Present in Acute Promyelocytic Leukemia Cells.
L. Benedetti, A. A. Levin, B. M. Scicchitano, F. Grignani, G. Allenby, D. Diverio, F. Lo Coco, G. Avvisati, M. Ruthardt, S. Adamo, et al. (1997)
Blood 90, 1175-1185
   Abstract »    Full Text »    PDF »
Transcription Factors, Normal Myeloid Development, and Leukemia.
D. G. Tenen, R. Hromas, J. D. Licht, and D.-E. Zhang (1997)
Blood 90, 489-519
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Use of Arsenic Trioxide (As2O3 ) in the Treatment of Acute Promyelocytic Leukemia (APL): I. As2O3 Exerts Dose-Dependent Dual Effects on APL Cells.
G.-Q. Chen, X.-G. Shi, W. Tang, S.-M. Xiong, J. Zhu, X. Cai, Z.-G. Han, J.-H. Ni, G.-Y. Shi, P.-M. Jia, et al. (1997)
Blood 89, 3345-3353
   Abstract »    Full Text »    PDF »
Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia.
J. Zhu, M. H. M. Koken, F. Quignon, M. K. Chelbi-Alix, L. Degos, Z. Y. Wang, Z. Chen, and H. de The (1997)
PNAS 94, 3978-3983
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Altered Myeloid Development and Acute Leukemia in Transgenic Mice Expressing PML-RARalpha Under Control of Cathepsin G Regulatory Sequences.
J. L. Grisolano, R. L. Wesselschmidt, P. G. Pelicci, and T. J. Ley (1997)
Blood 89, 376-387
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All-Trans-Retinoic Acid Pharmacology and Its Impact on the Treatment of Acute Promyelocytic Leukemia.
P. C. Adamson (1996)
Oncologist 1, 305-314
   Abstract »    Full Text »    PDF »
Analysis of the Growth and Transformation Suppressor Domains of Promyelocytic Leukemia Gene, PML.
X.-F. Le, P. Yang, and K.-S. Chang (1996)
J. Biol. Chem. 271, 130-135
   Abstract »    Full Text »    PDF »
Molecular Cloning, Structure, and Expression of Mouse Estrogen-responsive Finger Protein Efp.
A. Orimo, S. Inoue, K. Ikeda, S. Noji, and M. Muramatsu (1995)
J. Biol. Chem. 270, 24406-24413
   Abstract »    Full Text »    PDF »
Acute Promyelocytic Leukemia.
R. P. Warrell, H. de The, Z.-Y. Wang, and L. Degos (1993)
N. Engl. J. Med. 329, 177-189
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LYAR, a novel nucleolar protein with zinc finger DNA-binding motifs, is involved in cell growth regulation..
L Su, R J Hershberger, and I L Weissman (1993)
Genes & Dev. 7, 735-748
   Abstract »    PDF »
Xenopus nuclear factor 7 (xnf7) possesses an NLS that functions efficiently in both oocytes and embryos.
X Li and L. Etkin (1993)
J. Cell Sci. 105, 389-395
   Abstract »    PDF »
Cloning and Characterization of LUN, a Novel RING Finger Protein That Is Highly Expressed in Lung and Specifically Binds to a Palindromic Sequence.
D. Chu, N. Kakazu, M. J. Gorrin-Rivas, H.-P. Lu, M. Kawata, T. Abe, K. Ueda, and Y. Adachi (2001)
J. Biol. Chem. 276, 14004-14013
   Abstract »    Full Text »    PDF »
PRAM-1 Is a Novel Adaptor Protein Regulated by Retinoic Acid (RA) and Promyelocytic Leukemia (PML)-RA Receptor alpha in Acute Promyelocytic Leukemia Cells.
C. Moog-Lutz, E. J. Peterson, P. G. Lutz, S. Eliason, F. Cave-Riant, A. Singer, Y. Di Gioia, S. Dmowski, J. Kamens, Y. E. Cayre, et al. (2001)
J. Biol. Chem. 276, 22375-22381
   Abstract »    Full Text »    PDF »



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