Scopus - Trends in Biochemical Sciences: Are promyelocytic leukaemia protein nuclear bodies a scaffold for caspase-2 programmed cell death?


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Trends in Biochemical Sciences
Volume 32, Issue 9, September 2007, Pages 400-406

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Salomoni, P. , Ferguson, B.J. , Wyllie, A.H.
New insights into the role of PML in tumour suppression
(2008) Cell Research

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DOI: 10.1016/j.tibs.2007.08.001
Document Type: Article

View references (51)

Are promyelocytic leukaemia protein nuclear bodies a scaffold for caspase-2 programmed cell death?

Sanchez-Pulido, L.^a , Valencia, A.^b , Rojas, A.M.^b

^aNational Center for Biotechnology, Consejo Superior de Investigaciones Cientificas., C/Darwin n3, 28049 Madrid, Spain
^bStructural Computational Biology Group, Spanish National Cancer Research Center, C/Melchor Fernandez Almagro, n3, 28029 Madrid, Spain

Abstract

Promyelocytic leukaemia protein nuclear bodies (PML-NBs) are nuclear structures whose function is still poorly understood. They are implicated in various biological functions, such as viral infection, cellular transformation, innate immunity and growth control, and they might be dynamic hubs sensing stress and DNA damage. Data from PML^-/- mice suggest that PML-NBs are involved in apoptosis via caspase-independent mechanisms, probably involving p53-dependent and independent pathways. However, the recently demonstrated co-localization of caspase-2 within the PML-NB nuclear structures presents a new paradigm for nuclear cell death. Here, we show that these nuclear structures have a protein known as SP100 that could contain a caspase recruitment domain (CARD). If verified experimentally, this discovery will suggest a mechanism by which caspase-2 could be recruited into the complex and ultimately lead to apoptosis. © 2007 Elsevier Ltd. All rights reserved.

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