The promyelocytic (PML) nuclear compartment and transcription control

Biochemical Pharmacology

Volumn 60, Issue 8, 2000, Pages 1197-1201

  Doucas, Vassilis ^a  

^a UNIVERSITY OF GENEVA MEDICAL SCHOOL   (Switzerland)

Author keywords

Cancer; CBP; Nuclear compartmentalization; PML; Signal transduction; Transcription control; Viral propagation

Indexed keywords

CELL NUCLEUS RECEPTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HORMONE RECEPTOR; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR AP 1;

ANIMAL CELL; CELL COMPARTMENTALIZATION; CELL NUCLEUS; CELL NUCLEUS INCLUSION BODY; GENE DISRUPTION; GENETIC TRANSCRIPTION; NONHUMAN; PRIORITY JOURNAL; PROMYELOCYTIC LEUKEMIA; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN LOCALIZATION; REVIEW; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION;

EID: 0034668190     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(00)00413-5     Document Type: Article

References (41)

1. Doucas V., Brockes J.P., Yaniv M., de The H., Dejean A. The PML-retinoic acid receptor alpha translocation converts the receptor from an inhibitor to a retinoic acid-dependent activator of transcription factor AP-1. Proc Natl Acad Sci USA. 90:1993;9345-9349.
2. Doucas V., Evans R.M. Human T-cell leukemia retrovirus-Tax protein is a repressor of nuclear receptor signaling. Proc Natl Acad Sci USA. 96:1999;2633-2638.
3. Doucas V., Tini M., Egan D.A., Evans R.M. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci USA. 96:1999;2627-2632.
4. Weber A.F., Frommes S.P. Nuclear bodies Their prevalence, location and ultrastructure in the calf . Science. 141:1963;912-913.
5. Brasch K., Ochs R.L. Nuclear bodies (NBs) A newly "rediscovered" organelle . Exp Cell Res. 202:1992;211-223.
6. Spector D.L. Macromolecular domains within the cell nucleus. Annu Rev Cell Biol. 9:1993;265-315.
7. Doucas V., Evans R.M. The PML nuclear compartment and cancer. Biochim Biophys Acta. 1288:1996;M25-M29.
8. Kakizuka A., Miller W. Jr, Umesono K., Warrell R. Jr, Frankel S.R., Murty V.V., Dmitrovsky E., Evans R.M. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell. 66:1991;663-674.
9. de The F., Lavau C., Marchio A., Chomienne C., Degos L., Dejean A. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell. 66:1991;675-684.
10. Pandolfi P.P., Grignani F., Alcalay M., Mencarelli A., Biondi A., LoCoco F., Grignani F., Pelicci P.G. Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene. 6:1991;1285-1292.
11. Goddard A.D., Borrow J., Solomon E. A previously uncharacterized gene, PML, is fused to the retinoic acid receptor alpha gene in acute promyelocytic leukaemia. Leukemia. 6:1992;117S-119S.
12. Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B., Lanotte M., Berger R., Chambon P. Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL) Structural similarities with a new family of oncoproteins . EMBO J. 11:1992;629-642.
13. Chang K.S., Stass S.A., Chu D.T., Deaven L.L., Trujillo J.M., Freireich E.J. Characterization of a fusion cDNA (RARA/myl) transcribed from the t(15;17) translocation breakpoint in acute promyelocytic leukemia. Mol Cell Biol. 12:1992;800-810.
14. Freemont P.S., Hanson I.M., Trowsdale J. A novel cysteine-rich sequence motif. Cell. 64:1991;483-484.
15. Huang M.E., Ye Y.C., Chen S.R., Chai J.R., Lu J.X., Zhoa L., Gu L.J., Wang Z.Y. Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia. Blood. 72:1988;567-572.
16. Grignani F., Ferrucci P.F., Testa U., Talamo G., Fagioli M., Alcalay M., Mencarelli A., Peschle C., Nicoletti I., et al. The acute promyelocytic leukemia-specific PML-RAR alpha fusion protein inhibits differentiation and promotes survival of myeloid precursor cells. Cell. 74:1993;423-431.
17. Dyck J.A., Maul G.G., Miller W. Jr, Chen J.D., Kakizuka A., Evans R.M. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell. 76:1994;333-343.
18. Weis K., Rambaud S., Lavau C., Jansen J., Carvalho T., Carmo-Fonseca M., Lamond A., Dejean A. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell. 76:1994;345-356.
19. Doucas V., Ishov A.M., Romo A., Juguilon H., Weitzman M.D., Evans R.M., Maul G.G. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10:1996;196-207.
20. Day P.M., Roden R.B., Lowy D.R., Schiller J.T. The papillomavirus minor capsid protein, L2, induces localization of the major capsid protein, L1 and the viral transcription/replication protein, E2, to PML oncogenic domains. J Virol. 72:1998;142-150.
21. Desbois C., Rousset R., Bantignies F., Jalinot P. Exclusion of the Int-6 from PML nuclear bodies by binding to the HTLV-1 Tax oncoprotein. Science. 273:1996;951-953.
22. Doucas V and Evans RM, Patent, US. Serial No. 08/975,272, 1997.
23. Skinner P.J., Koshy B.T., Cummings C.J., Klement I.A., Helin K., Servadio A., Zoghbi H.Y., Orr H.T. Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures. Nature. 389:1997;971-974.
24. Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y. The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Nature. 389:1997;974-978.
25. Mangelsdorf D.J., Kliewer S.A., Kakizuka A., Umesono K., Evans R.M. Retinoid receptors. Recent Prog Horm Res. 48:1993;99-121.
26. Beato M., Herrlich P., Schutz G. Steroid hormone receptors Many actors in search of a plot . Cell. 83:1995;851-857.
27. Schule R., Rangarajan P., Yang N., Kliewer S., Ransone L.J., Bolado J., Verma I.M., Evans R.M. Retinoic acid is a negative regulator of AP-1-responsive genes. Proc Natl Acad Sci USA. 88:1991;6092-6096.
28. Karin M., Hunter T. Transcriptional control by protein phosphorylation Signal transmission from the cell surface to the nucleus . Curr Biol. 5:1995;747-757.
29. Roeder R.G. The role of general initiation factors in transcription by RNA polymerase II. Trends Biochem Sci. 21:1996;327-335.
30. Chrivia J.C., Kwok R.P., Lamb N., Hagiwara M., Montminy M.R., Goodman R.H. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature. 365:1993;855-859.
31. Janknecht R., Hunter T. Versatile molecular glue. Transcriptional control. Curr Biol. 6:1996;951-954.
32. Goldman P.S., DeMaggio A.J., Hoekstra M.F., Goodman R.H. The beta-adrenergic receptor kinase interacts with the amino terminus of the G protein beta subunit. Biochem Biophys Res Commun. 240:1997;425-429.
33. Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell. 85:1996;403-414.
34. Heery D.M., Kalkhoven E., Hoare S., Parker M.G. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature. 387:1997;733-736.
35. Nakajima T., Uchida C., Anderson S.F., Lee C.G., Hurwitz J., Parvin J.D., Montminy M. RNA helicase A mediates association of CBP with RNA polymerase II. Cell. 90:1997;1107-1112.
36. Avantaggiati M.L., Ogryzko V., Gardner K., Giordano A., Levine A.S., Kelly K. Recruitment of p300/CBP in p53-dependent signal pathways. Cell. 89:1997;1175-1184.
37. Gu W., Shi X.L., Roeder R.G. Synergistic activation of transcription by CBP and p53. Nature. 387:1997;819-823.
38. Lill N.L., Grossman S.R., Ginsberg D., DeCaprio J., Livingston D.M. Binding and modulation of p53 by p300/CBP coactivators. Nature. 387:1997;823-827.
39. Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 87:1996;953-959.
40. Bannister A.J., Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature. 384:1996;641-643.
41. Janknecht R., Wells N.J., Hunter T. TGF-beta-stimulated cooperation of smad proteins with the coactivators CBP/p300. Genes Dev. 12:1998;2114-2119.