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| http://dx.doi.org/10.1080/15384101.2017.1355179 | DOI Listing |
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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.
Mol Cell Oncol
July 2017
Department of Pediatrics, Division of Hematology-Oncology, Baylor College of Medicine, Houston, TX, USA.
Despite being frequently mutated or deregulated in acute myeloid leukemia (AML) and many other cancers, the mechanisms by which nucleophosmin (NPM1) regulates oncogenesis remain elusive. We found that NPM1 plays a direct and conserved role in DNA damage-induced assembly of the PIDDosome complex, the activating platform for caspase-2. This function is carried in the nucleolus and is essential for caspase-2-mediated apoptosis in response to a variety of DNA injuries.
View Article and Find Full Text PDFThe nucleolus: A new home for the PIDDosome.
Cell Cycle
May 2019
c Department of Medicine, Division of Hematology/Oncology , Tisch Cancer Institute, Icahn School of Medicine at Mount Sinai, New York , NY , USA.
Nucleolar caspase-2: Protecting us from DNA damage.
J Cell Biol
June 2017
School of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba QLD 4102, Australia
Caspase-2 triggers apoptosis, but how it is activated by different stimuli is unclear. In this issue, Ando et al. (2017.
View Article and Find Full Text PDFNPM1 directs PIDDosome-dependent caspase-2 activation in the nucleolus.
J Cell Biol
June 2017
Department of Pediatrics, Division of Hematology-Oncology, Baylor College of Medicine, Houston, TX 77030
The PIDDosome (PIDD-RAIDD-caspase-2 complex) is considered to be the primary signaling platform for caspase-2 activation in response to genotoxic stress. Yet studies of PIDD-deficient mice show that caspase-2 activation can proceed in the absence of PIDD. Here we show that DNA damage induces the assembly of at least two distinct activation platforms for caspase-2: a cytoplasmic platform that is RAIDD dependent but PIDD independent, and a nucleolar platform that requires both PIDD and RAIDD.
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