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Blood, 1 October 2004, Vol. 104, No. 7, pp. 2035-2043. Prepublished online as a Blood First Edition Paper on June 8, 2004; DOI 10.1182/blood-2004-01-0065. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-01-0065v1 104/7/2035    most recent 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 Plenchette, S. Articles by Solary, E. Search for Related Content PubMed PubMed Citation Articles by Plenchette, S. Articles by Solary, E. Related Collections Hematopoiesis and Stem Cells Neoplasia Phagocytes Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMATOPOIESIS Translocation of the inhibitor of apoptosis protein c-IAP1 from the nucleus to the Golgi in hematopoietic cells undergoing differentiation: a nuclear export signal-mediated event Stéphanie Plenchette, Séverine Cathelin, Cédric Rébé, Sophie Launay, Sylvain Ladoire, Olivier Sordet, Tibor Ponnelle, Najet Debili, Thi-Hai Phan, Rose-Ann Padua, Laurence Dubrez-Daloz, and Eric Solary From the Institut National de la Santé et de la Recherche Médicale (INSERM) U517, INSERM EPI 106, IFR100, Dijon, France; INSERM U362, Institut Gustave Roussy, Villejuif, France; INSERM EMI00-03, Institut Universitaire d'Hematologie, Hopital St Louis, Paris, France; The Rayne Institute, King's College Hospital, London, United Kingdom. The caspase inhibitor and RING finger-containing protein cellular inhibitor of apoptosis protein 1 (c-IAP1) has been shown to be involved in both apoptosis inhibition and signaling by members of the tumor necrosis factor (TNF) receptor family. The protein is regulated transcriptionally (eg, is a target for nuclear factor-B [NF-B]) and can be inhibited by mitochondrial proteins released in the cytoplasm upon apoptotic stimuli. The present study indicates that an additional level of regulation of c-IAP1 may be cell compartmentalization. The protein is present in the nucleus of undifferentiated U937 and THP1 monocytic cell lines. When these cells undergo differentiation under phorbol ester exposure, c-IAP1 translocates to the cytoplasmic side of the Golgi apparatus. This redistribution involves a nuclear export signal (NES)-mediated, leptomycin B-sensitive mechanism. Using site-directed mutagenesis, we localized the functional NES motif in the caspase recruitment domain (CARD) of c-IAP1. A nucleocytoplasmic redistribution of the protein was also observed in human monocytes as well as in tumor cells from epithelial origin when undergoing differentiation. c-IAP1 does not translocate from the nucleus of cells whose differentiation is blocked (ie, in cell lines and monocytes from transgenic mice overexpressing B-cell lymphoma 2 [Bcl-2] and in monocytes from patients with chronic myelomonocytic leukemia). Altogether, these observations associate c-IAP1 cellular location with cell differentiation, which opens new perspectives on the functions of the protein. (Blood. 2004;104:2035-2043) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: N. C. Healy and R. O'Connor Sequestration of PDLIM2 in the cytoplasm of monocytic/macrophage cells is associated with adhesion and increased nuclear activity of NF-{kappa}B J. Leukoc. Biol., March 1, 2009; 85(3): 481 - 490. [Abstract] [Full Text] [PDF] H.-S. Jin, D.-H. Lee, D.-H. Kim, J.-H. Chung, S.-J. Lee, and T. H. Lee cIAP1, cIAP2, and XIAP Act Cooperatively via Nonredundant Pathways to Regulate Genotoxic Stress-Induced Nuclear Factor-{kappa}B Activation Cancer Res., March 1, 2009; 69(5): 1782 - 1791. [Abstract] [Full Text] [PDF] A. Dupoux, J. Cartier, S. Cathelin, R. Filomenko, E. Solary, and L. Dubrez-Daloz cIAP1-dependent TRAF2 degradation regulates the differentiation of monocytes into macrophages and their response to CD40 ligand Blood, January 1, 2009; 113(1): 175 - 185. [Abstract] [Full Text] [PDF] N. Omidvar, S. Kogan, S. Beurlet, C. le Pogam, A. Janin, R. West, M.-E. Noguera, M. Reboul, A. Soulie, C. Leboeuf, et al. BCL-2 and Mutant NRAS Interact Physically and Functionally in a Mouse Model of Progressive Myelodysplasia Cancer Res., December 15, 2007; 67(24): 11657 - 11667. [Abstract] [Full Text] [PDF] P. Fernando and L. A. Megeney Is caspase-dependent apoptosis only cell differentiation taken to the extreme? FASEB J, January 1, 2007; 21(1): 8 - 17. [Abstract] [Full Text] [PDF] E. Tirro, M. L. Consoli, M. Massimino, L. Manzella, F. Frasca, L. Sciacca, L. Vicari, G. Stassi, L. Messina, A. Messina, et al. Altered Expression of c-IAP1, Survivin, and Smac Contributes to Chemotherapy Resistance in Thyroid Cancer Cells. Cancer Res., April 15, 2006; 66(8): 4263 - 4272. [Abstract] [Full Text] [PDF] T. Samuel, K. Okada, M. Hyer, K. Welsh, J. M. Zapata, and J. C. Reed cIAP1 Localizes to the Nuclear Compartment and Modulates the Cell Cycle Cancer Res., January 1, 2005; 65(1): 210 - 218. [Abstract] [Full Text] [PDF]

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