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Science 6 March 1998:
Vol. 279. no. 5356, pp. 1547 - 1551
DOI: 10.1126/science.279.5356.1547
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Reports

Role of PML in Cell Growth and the Retinoic Acid Pathway

Zhu Gang Wang, * Laurent Delva, * Mirella Gaboli, Roberta Rivi, Marco Giorgio, Carlos Cordon-Cardo, Frank Grosveld, Pier Paolo Pandolfi dagger

The PML gene is fused to the retinoic acid receptor alpha  (RARalpha ) gene in chromosomal translocations associated with acute promyelocytic leukemia (APL). Ablation of murine PML protein by homologous recombination revealed that PML regulates hemopoietic differentiation and controls cell growth and tumorigenesis. PML function was essential for the tumor-growth-suppressive activity of retinoic acid (RA) and for its ability to induce terminal myeloid differentiation of precursor cells. PML was needed for the RA-dependent transactivation of the p21WAF1/CIP1 gene, which regulates cell cycle progression and cellular differentiation. These results indicate that PML is a critical component of the RA pathway and that disruption of its activity by the PML-RARalpha fusion protein may be important in APL pathogenesis.

Z. G. Wang, L. Delva, M. Gaboli, R. Rivi, M. Giorgio, P. P. Pandolfi, Department of Human Genetics and Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Division, Graduate School of Medical Sciences, Cornell University, 1275 York Avenue, New York, NY 10021, USA.
C. Cordon-Cardo, Department of Pathology, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.
F. Grosveld, Department of Cell Biology and Genetics, Faculty of Medicine, Erasmus University, Post Office Box 1738, 3000 DR, Rotterdam, Netherlands.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: p-pandolfi{at}ski.mskcc.org

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   Abstract »    Full Text »    PDF »
Role of SUMO-1-modified PML in nuclear body formation.
S. Zhong, S. Muller, S. Ronchetti, P. S. Freemont, A. Dejean, and P. P. Pandolfi (2000)
Blood 95, 2748-2752
   Abstract »    Full Text »    PDF »
Sequestration and Inhibition of Daxx-Mediated Transcriptional Repression by PML.
H. Li, C. Leo, J. Zhu, X. Wu, J. O'Neil, E.-J. Park, and J. D. Chen (2000)
Mol. Cell. Biol. 20, 1784-1796
   Abstract »    Full Text »
Leukemia initiated by PMLRARalpha : the PML domain plays a critical role while retinoic acid-mediated transactivation is dispensable.
S. C. Kogan, S.-h. Hong, D. B. Shultz, M. L. Privalsky, and J. M. Bishop (2000)
Blood 95, 1541-1550
   Abstract »    Full Text »    PDF »
Promyelocytic Leukemia Protein (PML) and Daxx Participate in a Novel Nuclear Pathway for Apoptosis.
S. Zhong, P. Salomoni, S. Ronchetti, A. Guo, D. Ruggero, and P. P. Pandolfi (2000)
J. Exp. Med. 191, 631-640
   Abstract »    Full Text »    PDF »
ALT-associated PML bodies are present in viable cells and are enriched in cells in the G(2)/M phase of the cell cycle.
J. Grobelny, A. Godwin, and D Broccoli (2000)
J. Cell Sci. 113, 4577-4585
   Abstract »    PDF »
Roles of RecQ Family Helicases in the Maintenance of Genome Stability.
L. WU, S.L. DAVIES, and I.D. HICKSON (2000)
Cold Spring Harb Symp Quant Biol 65, 573-582
   Abstract »    PDF »
A bcr-3 isoform of RARalpha -PML potentiates the development of PML-RARalpha -driven acute promyelocytic leukemia.
J. L. Pollock, P. Westervelt, A. K. Kurichety, P. G. Pelicci, J. L. Grisolano, and T. J. Ley (1999)
PNAS 96, 15103-15108
   Abstract »    Full Text »    PDF »
Physical and Functional Interactions between Cellular Retinoic Acid Binding Protein II and the Retinoic Acid-Dependent Nuclear Complex.
L. Delva, J.-N. Bastie, C. Rochette-Egly, R. Kraiba, N. Balitrand, G. Despouy, P. Chambon, and C. Chomienne (1999)
Mol. Cell. Biol. 19, 7158-7167
   Abstract »    Full Text »    PDF »
Overexpression of Wild-Type Retinoic Acid Receptor alpha (RARalpha ) Recapitulates Retinoic Acid-Sensitive Transformation of Primary Myeloid Progenitors by Acute Promyelocytic Leukemia RARalpha -Fusion Genes.
C. Du, R. L. Redner, M. P. Cooke, and C. Lavau (1999)
Blood 94, 793-802
   Abstract »    Full Text »    PDF »
Genetic Diagnosis and Molecular Monitoring in the Management of Acute Promyelocytic Leukemia.
F. L. Coco, D. Diverio, B. Falini, A. Biondi, C. Nervi, and P. G. Pelicci (1999)
Blood 94, 12-22
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Viral Immediate-Early Proteins Abrogate the Modification by SUMO-1 of PML and Sp100 Proteins, Correlating with Nuclear Body Disruption.
S. Müller and A. Dejean (1999)
J. Virol. 73, 5137-5143
   Abstract »    Full Text »
Structural and Functional Heterogeneity of Nuclear Bodies.
D. B. Bloch, J.-D. Chiche, D. Orth, S. M. de la Monte, A. Rosenzweig, and K. D. Bloch (1999)
Mol. Cell. Biol. 19, 4423-4430
   Abstract »    Full Text »    PDF »
Deconstructing a Disease: RAR{alpha}, Its Fusion Partners, and Their Roles in the Pathogenesis of Acute Promyelocytic Leukemia.
A. Melnick and J. D. Licht (1999)
Blood 93, 3167-3215
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HERF1, a Novel Hematopoiesis-Specific RING Finger Protein, Is Required for Terminal Differentiation of Erythroid Cells.
H. Harada, Y. Harada, D. P. O'Brien, D. S. Rice, C. W. Naeve, and J. R. Downing (1999)
Mol. Cell. Biol. 19, 3808-3815
   Abstract »    Full Text »    PDF »
Retinoic Acid and Arsenic Synergize to Eradicate Leukemic Cells in a Mouse Model of Acute Promyelocytic Leukemia.
V. Lallemand-Breitenbach, M.-C. Guillemin, A. Janin, M.-T. Daniel, L. Degos, S. C. Kogan, J. Michael Bishop, and H. de The (1999)
J. Exp. Med. 189, 1043-1052
   Abstract »    Full Text »    PDF »
Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling.
V. Doucas, M. Tini, D. A. Egan, and R. M. Evans (1999)
PNAS 96, 2627-2632
   Abstract »    Full Text »    PDF »
Cell cycle regulation of PML modification and ND10 composition.
R. Everett, P Lomonte, T Sternsdorf, R van Driel, and A Orr (1999)
J. Cell Sci. 112, 4581-4588
   Abstract »    PDF »
Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies.
C Morris-Desbois, V Bochard, C Reynaud, and P Jalinot (1999)
J. Cell Sci. 112, 3331-3342
   Abstract »    PDF »


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