This Article Full Text Full Text (PDF) Supplementary Data Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Condemine, W. Articles by de Thé, H. Search for Related Content PubMed PubMed Citation Articles by Condemine, W. Articles by de Thé, H.

Characterization of Endogenous Human Promyelocytic Leukemia Isoforms

¹ Centre National de la Recherche Scientifique UMR7151, Équipe Labellisée par La Ligne Contre le Cancer, ² Institut National de la Sante et de la Recherche Medicale U728, Université de Paris VII, Hôpital St. Louis, Paris Cedex; and ³ Centre National de la Recherche Scientifique UPR1983, Institut A. Lwoff, Villejuif Cedex, France

Requests for reprints: Hugues de Thé, Centre National de la Recherche Scientifique UMR7151, Équipe Labellisée par La Ligne Contre le Cancer, Paris Cedex 75475, France. Phone: 33-1-5372-2191; Fax: 33-1-5372-2190; E-mail: dethe{at}paris7.jussieu.fr.

Promyelocytic leukemia (PML) has been implicated in a variety of functions, including control of TP53 function and modulation of cellular senescence. Sumolated PML is the organizer of mature PML bodies, recruiting a variety of proteins onto these nuclear domains. The PML gene is predicted to encode a variety of protein isoforms. Overexpression of only one of them, PML-IV, promotes senescence in human diploid fibroblasts, whereas PML-III was proposed to specifically interact with the centrosome. We show that all PML isoform proteins are expressed in cell lines or primary cells. Unexpectedly, we found that PML-III, PML-IV, and PML-V are quantitatively minor isoforms compared with PML-I/II and could not confirm the centrosomal targeting of PML-III. Stable expression of each isoform, in a pml-null background, yields distinct subcellular localization patterns, suggesting that, like in other RBCC/TRIM proteins, the COOH-terminal domains of PML are involved in interactions with specific cellular components. Only the isoform-specific sequences of PML-I and PML-V are highly conserved between man and mouse. That PML-I contains all conserved exons and is more abundantly expressed than PML-IV suggests that it is a critical contributor to PML function(s). (Cancer Res 2006; 66(12): 6192-8)

This article has been cited by other articles:

				T. Nojima, T. Oshiro-Ideue, H. Nakanoya, H. Kawamura, T. Morimoto, Y. Kawaguchi, N. Kataoka, and M. Hagiwara Herpesvirus protein ICP27 switches PML isoform by altering mRNA splicing Nucleic Acids Res., October 1, 2009; 37(19): 6515 - 6527. [Abstract] [Full Text] [PDF]

				K. N. Leppard, E. Emmott, M. S. Cortese, and T. Rich Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukaemia (PML) protein nuclear domains for disruption via a sequence in PML isoform II that is predicted as a protein interaction site by bioinformatic analysis J. Gen. Virol., January 1, 2009; 90(1): 95 - 104. [Abstract] [Full Text] [PDF]

				A. Viens, F. Harper, E. Pichard, M. Comisso, G. Pierron, and V. Ogryzko Use of Protein Biotinylation In Vivo for Immunoelectron Microscopic Localization of a Specific Protein Isoform J. Histochem. Cytochem., October 1, 2008; 56(10): 911 - 919. [Abstract] [Full Text] [PDF]

				S. Weidtkamp-Peters, T. Lenser, D. Negorev, N. Gerstner, T. G. Hofmann, G. Schwanitz, C. Hoischen, G. Maul, P. Dittrich, and P. Hemmerich Dynamics of component exchange at PML nuclear bodies J. Cell Sci., August 15, 2008; 121(16): 2731 - 2743. [Abstract] [Full Text] [PDF]

				Y.-C. M. Chen, C. Kappel, J. Beaudouin, R. Eils, and D. L. Spector Live Cell Dynamics of Promyelocytic Leukemia Nuclear Bodies upon Entry into and Exit from Mitosis Mol. Biol. Cell, July 1, 2008; 19(7): 3147 - 3162. [Abstract] [Full Text] [PDF]

				W. Condemine, Y. Takahashi, M. Le Bras, and H. de The A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells J. Cell Sci., September 15, 2007; 120(18): 3219 - 3227. [Abstract] [Full Text] [PDF]

				N. Dror, N. Rave-Harel, A. Burchert, A. Azriel, T. Tamura, P. Tailor, A. Neubauer, K. Ozato, and B.-Z. Levi Interferon Regulatory Factor-8 Is Indispensable for the Expression of Promyelocytic Leukemia and the Formation of Nuclear Bodies in Myeloid Cells J. Biol. Chem., February 23, 2007; 282(8): 5633 - 5640. [Abstract] [Full Text] [PDF]

				G. J. Block, C. H. Eskiw, G. Dellaire, and D. P. Bazett-Jones Transcriptional Regulation Is Affected by Subnuclear Targeting of Reporter Plasmids to PML Nuclear Bodies Mol. Cell. Biol., December 1, 2006; 26(23): 8814 - 8825. [Abstract] [Full Text] [PDF]