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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Zhong, S. Articles by Pandolfi, P. P. Search for Related Content PubMed PubMed Citation Articles by Zhong, S. Articles by Pandolfi, P. P. Related Collections Neoplasia Plenary Papers Oncogenes and Tumor Suppressors Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 95 No. 9 (May 1), 2000: pp. 2748-2752 PLENARY PAPER Role of SUMO-1-modified PML in nuclear body formation Sue Zhong, Stefan Müller, Simona Ronchetti, Paul S. Freemont, Anne Dejean, and Pier Paolo Pandolfi From the Department of Human Genetics and Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Division, Graduate School of Medical Sciences, Cornell University, New York, NY; Unite de Recombinaison et Expression Genetique, INSERM U 163, Institut Pasteur, Paris, France; and Molecular Structure and Function Laboratory, Imperial Cancer Research Fund, London, England. The tumor-suppressive promyelocytic leukemia (PML) protein of acute promyelocytic leukemia (APL) has served as one of the defining components of a class of distinctive nuclear bodies (NBs). PML is delocalized from NBs in APL cells and is degraded in cells infected by several viruses. In these cells, NBs are disrupted, leading to the aberrant localization of NB proteins. These results have suggested a critical role for the NB in immune response and tumor suppression and raised the question of whether PML is crucial for the formation or stability of NB. In addition, PML is, among other proteins, covalently modified by SUMO-1. However, the functional relevance of this modification is unclear. Here, we show in primary PML/ cells of various histologic origins, that in the absence of PML, several NB proteins such as Sp100, CBP, ISG20, Daxx, and SUMO-1 fail to accumulate in the NB and acquire aberrant localization patterns. Transfection of PML in PML/ cells causes the relocalization of NB proteins. By contrast, a PML mutant that can no longer be modified by SUMO-1 fails to do so and displays an aberrant nuclear localization pattern. Therefore, PML is required for the proper formation of the NB. Conjugation to SUMO-1 is a prerequisite for PML to exert this function. These data shed new light on both the mechanisms underlying the formation of the NBs and the pathogenesis of APL. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. K. Brouwer, J. Schimmel, J. C.A.G. Wiegant, A. C.O. Vertegaal, H. J. Tanke, and R. W. Dirks Telomeric DNA Mediates De Novo PML Body Formation Mol. Biol. Cell, November 15, 2009; 20(22): 4804 - 4815. [Abstract] [Full Text] [PDF] Y.-L. Chung and T.-Y. Tsai Promyelocytic Leukemia Nuclear Bodies Link the DNA Damage Repair Pathway with Hepatitis B Virus Replication: Implications for Hepatitis B Virus Exacerbation during Chemotherapy and Radiotherapy Mol. Cancer Res., October 1, 2009; 7(10): 1672 - 1685. [Abstract] [Full Text] [PDF] L. Marcos-Villar, F. Lopitz-Otsoa, P. Gallego, C. Munoz-Fontela, J. Gonzalez-Santamaria, M. Campagna, G. Shou-Jiang, M. S. Rodriguez, and C. 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