REFERENCES
- Bernardi, R., and P. P. Pandolfi. 2003. Role of PML and the PML-nuclear body in the control of programmed cell death. Oncogene 22:9048–9057.
- Borden, K. L. 2002. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell. Biol. 22:5259–5269.
- Buschbeck, M., I. Uribesalgo, A. Ledl, A. Gutierrez, S. Minucci, S. Muller, and L. Di Croce. 2007. PML4 induces differentiation by Myc destabilization. Oncogene 26:3415–3422.
- Chelbi-Alix, M. K., L. Pelicano, F. Quignon, M. H. Koken, L. Venturini, M. Stadler, J. Pavlovic, L. Degos, and H. de The. 1995. Induction of the PML protein by interferons in normal and APL cells. Leukemia 9:2027–2033.
- Ching, R. W., G. Dellaire, C. H. Eskiw, and D. P. Bazett-Jones. 2005. PML bodies: a meeting place for genomic loci? J. Cell Sci. 118:847–854.
- De Nicola, F., T. Bruno, S. Iezzi, M. Di Padova, A. Floridi, C. Passananti, G. Del Sal, and M. Fanciulli. 2007. The prolyl isomerase Pin1 affects Che-1 stability in response to apoptotic DNA damage. J. Biol. Chem. 282:19685–19691.
- de Stanchina, E., E. Querido, M. Narita, R. V. Davuluri, P. P. Pandolfi, G. Ferbeyre, and S. W. Lowe. 2004. PML is a direct p53 target that modulates p53 effector functions. Mol. Cell 13:523–535.
- de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos, and A. Dejean. 1991. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66:675–684.
- Doucas, V., and R. M. Evans. 1996. The PML nuclear compartment and cancer. Biochim. Biophys. Acta 1288:M25-M29.
- Dyck, J. A., G. G. Maul, W. H. Miller, Jr., J. D. Chen, A. Kakizuka, and R. M. Evans. 1994. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76:333–343.
- Everett, R. D., P. Lomonte, T. Sternsdorf, R. van Driel, and A. Orr. 1999. Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112:4581–4588.
- Ferbeyre, G., E. de Stanchina, E. Querido, N. Baptiste, C. Prives, and S. W. Lowe. 2000. PML is induced by oncogenic ras and promotes premature senescence. Genes Dev. 14:2015–2027.
- Galat, A. 2003. Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity—targets—functions. Curr. Top. Med. Chem. 3:1315–1347.
- Gurrieri, C., P. Capodieci, R. Bernardi, P. P. Scaglioni, K. Nafa, L. J. Rush, D. A. Verbel, C. Cordon-Cardo, and P. P. Pandolfi. 2004. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J. Natl. Cancer Inst. 96:269–279.
- Hamdane, M., C. Smet, A. V. Sambo, A. Leroy, J. M. Wieruszeski, P. Delobel, C. A. Maurage, A. Ghestem, R. Wintjens, S. Begard, N. Sergeant, A. Delacourte, D. Horvath, I. Landrieu, G. Lippens, and L. Buee. 2002. Pin1: a therapeutic target in Alzheimer neurodegeneration. J. Mol. Neurosci. 19:275–287.
- Hayakawa, F., and M. L. Privalsky. 2004. Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. Cancer Cell 5:389–401.
- Hofmann, T. G., and H. Will. 2003. Body language: the function of PML nuclear bodies in apoptosis regulation. Cell Death Differ. 10:1290–1299.
- Ishov, A. M., A. G. Sotnikov, D. Negorev, O. V. Vladimirova, N. Neff, T. Kamitani, E. T. Yeh, J. F. Strauss, 3rd, and G. G. Maul. 1999. PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147:221–234.
- Jensen, K., C. Shiels, and P. S. Freemont. 2001. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20:7223–7233.
- Joseph, J. D., E. S. Yeh, K. I. Swenson, A. R. Means, and Winkler. 2003. The peptidyl-prolyl isomerase Pin1. Prog. Cell Cycle Res. 5:477–487.
- Kakizuka, A., W. H. Miller, Jr., K. Umesono, R. P. Warrell, Jr., S. R. Frankel, V. V. Murty, E. Dmitrovsky, and R. M. Evans. 1991. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 66:663–674.
- Kawai, T., S. Akira, and J. C. Reed. 2003. ZIP kinase triggers apoptosis from nuclear PML oncogenic domains. Mol. Cell. Biol. 23:6174–6186.
- Lallemand-Breitenbach, V., J. Zhu, F. Puvion, M. Koken, N. Honore, A. Doubeikovsky, E. Duprez, P. P. Pandolfi, E. Puvion, P. Freemont, and H. de The. 2001. Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J. Exp. Med. 193:1361–1371.
- Lavau, C., A. Marchio, M. Fagioli, J. Jansen, B. Falini, P. Lebon, F. Grosveld, P. P. Pandolfi, P. G. Pelicci, and A. Dejean. 1995. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 11:871–876.
- Lavoie, S. B., A. L. Albert, and M. Vincent. 2003. Unexpected roles of the peptidyl-prolyl cis/trans isomerase Pin1. Med. Sci. (Paris) 19:1251-1258. [In French.]
- Le, X. F., S. Vallian, Z. M. Mu, M. C. Hung, and K. S. Chang. 1998. Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene 16:1839–1849.
- Lu, P. J., X. Z. Zhou, M. Shen, and K. P. Lu. 1999. Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283:1325–1328.
- Mann, K. K., and W. H. Miller, Jr. 2004. Death by arsenic: implications of PML sumoylation. Cancer Cell 5:307–309.
- Maul, G. G., D. Negorev, P. Bell, and A. M. Ishov. 2000. Review: properties and assembly mechanisms of ND10, PML bodies, or PODs. J. Struct. Biol. 129:278–287.
- Melnick, A., and J. D. Licht. 1999. Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93:3167–3215.
- Muller, S., W. H. Miller, Jr., and A. Dejean. 1998. Trivalent antimonials induce degradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells. Blood 92:4308–4316.
- Ranganathan, R., and E. M. Ross. 1997. PDZ domain proteins: scaffolds for signaling complexes. Curr. Biol. 7:R770-R773.
- Reineke, E. L., H. Liu, M. Lam, Y. Liu, and H. Y. Kao. 2007. Aberrant association of promyelocytic leukemia protein-retinoic acid receptor-alpha with coactivators contributes to its ability to regulate gene expression. J. Biol. Chem. 282:18584–18596.
- Ryo, A., Y. C. Liou, G. Wulf, M. Nakamura, S. W. Lee, and K. P. Lu. 2002. PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell. Biol. 22:5281–5295.
- Ryo, A., M. Nakamura, G. Wulf, Y. C. Liou, and K. P. Lu. 2001. Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 3:793–801.
- Ryo, A., F. Suizu, Y. Yoshida, K. Perrem, Y. C. Liou, G. Wulf, R. Rottapel, S. Yamaoka, and K. P. Lu. 2003. Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell 12:1413–1426.
- Scaglioni, P. P., T. M. Yung, L. F. Cai, H. Erdjument-Bromage, A. J. Kaufman, B. Singh, J. Teruya-Feldstein, P. Tempst, and P. P. Pandolfi. 2006. A CK2-dependent mechanism for degradation of the PML tumor suppressor. Cell 126:269–283.
- Schmid, F. X. 1995. Protein folding. Prolyl isomerases join the fold. Curr. Biol. 5:993–994.
- Shen, M., P. T. Stukenberg, M. W. Kirschner, and K. P. Lu. 1998. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12:706–720.
- Stadler, M., M. K. Chelbi-Alix, M. H. Koken, L. Venturini, C. Lee, A. Saib, F. Quignon, L. Pelicano, M. C. Guillemin, C. Schindler, et al. 1995. Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 11:2565–2573.
- Strohmaier, H., C. H. Spruck, P. Kaiser, K. A. Won, O. Sangfelt, and S. I. Reed. 2001. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413:316–322.
- Takahashi, Y., V. Lallemand-Breitenbach, J. Zhu, and H. de The. 2004. PML nuclear bodies and apoptosis. Oncogene 23:2819–2824.
- Urist, M., and C. Prives. 2004. The linchpin? Pin1 meets p73. Cancer Cell 5:515–517.
- van Drogen, F., O. Sangfelt, A. Malyukova, L. Matskova, E. Yeh, A. R. Means, and S. I. Reed. 2006. Ubiquitylation of cyclin E requires the sequential function of SCF complexes containing distinct hCdc4 isoforms. Mol. Cell 23:37–48.
- Wang, Z. G., L. Delva, M. Gaboli, R. Rivi, M. Giorgio, C. Cordon-Cardo, F. Grosveld, and P. P. Pandolfi. 1998. Role of PML in cell growth and the retinoic acid pathway. Science 279:1547–1551.
- Winkler, K. E., K. I. Swenson, S. Kornbluth, and A. R. Means. 2000. Requirement of the prolyl isomerase Pin1 for the replication checkpoint. Science 287:1644–1647.
- Wu, R. C., Q. Feng, D. M. Lonard, and B. W. O'Malley. 2007. SRC-3 coactivator functional lifetime is regulated by a phospho-dependent ubiquitin time clock. Cell 129:1125–1140.
- Wu, W. S., S. Vallian, E. Seto, W. M. Yang, D. Edmondson, S. Roth, and K. S. Chang. 2001. The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol. Cell. Biol. 21:2259–2268.
- Wulf, G., G. Finn, F. Suizu, and K. P. Lu. 2005. Phosphorylation-specific prolyl isomerization: is there an underlying theme? Nat. Cell Biol. 7:435–441.
- Wulf, G., P. Garg, Y. C. Liou, D. Iglehart, and K. P. Lu. 2004. Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis. EMBO J. 23:3397–3407.
- Wulf, G., A. Ryo, Y. C. Liou, and K. P. Lu. 2003. The prolyl isomerase Pin1 in breast development and cancer. Breast Cancer Res. 5:76–82.
- Xu, Z. X., R. X. Zhao, T. Ding, T. T. Tran, W. Zhang, P. P. Pandolfi, and K. S. Chang. 2004. Promyelocytic leukemia protein 4 induces apoptosis by inhibition of survivin expression. J. Biol. Chem. 279:1838–1844.
- Yaffe, M. B., M. Schutkowski, M. Shen, X. Z. Zhou, P. T. Stukenberg, J. U. Rahfeld, J. Xu, J. Kuang, M. W. Kirschner, G. Fischer, L. C. Cantley, and K. P. Lu. 1997. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 278:1957–1960.
- Yeh, E., M. Cunningham, H. Arnold, D. Chasse, T. Monteith, G. Ivaldi, W. C. Hahn, P. T. Stukenberg, S. Shenolikar, T. Uchida, C. M. Counter, J. R. Nevins, A. R. Means, and R. Sears. 2004. A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells. Nat. Cell Biol. 6:308–318.
- Yi, P., R. C. Wu, J. Sandquist, J. Wong, S. Y. Tsai, M. J. Tsai, A. R. Means, and B. W. O'Malley. 2005. Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1). Mol. Cell. Biol. 25:9687–9699.
- Zhong, S., S. Muller, S. Ronchetti, P. S. Freemont, A. Dejean, and P. P. Pandolfi. 2000. Role of SUMO-1-modified PML in nuclear body formation. Blood 95:2748–2752.