Article abstract
Nature Cell Biology 10, 1051 - 1061 (2008)
Published online: 1 August 2008 | doi:10.1038/ncb1764
A ribosomal protein L23-nucleophosmin circuit coordinates Miz1 function with cell growth
Michael Wanzel1, Annika C. Russ1, Daniela Kleine-Kohlbrecher2, Emanuela Colombo3, Pier-Guiseppe Pelicci3 & Martin Eilers1
Abstract
The Myc-associated zinc-finger protein, Miz1, is a negative regulator of cell proliferation and induces expression of the cell-cycle inhibitors p15Ink4b and p21Cip1. Here we identify the ribosomal protein L23 as a negative regulator of Miz1-dependent transactivation. L23 exerts this function by retaining nucleophosmin, an essential co-activator of Miz1 required for Miz1-induced cell-cycle arrest, in the nucleolus. Mutant forms of nucleophosmin found in acute myeloid leukaemia fail to co-activate Miz1 and re-localize it to the cytosol. As L23 is encoded by a direct target gene of Myc, this regulatory circuit may provide a feedback mechanism that links translation of Myc target genes and cell growth to Miz1-dependent cell-cycle arrest.
- Institute for Molecular Biology and Tumor Research (IMT), Emil-Mannkopff-Str.2, 35033 Marburg; Germany.
- Biotech Research and Innovation Centre (BRIC), Copenhagen Biocenter; Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.
- Department of Experimental Oncology, Instituto Europeo di Oncologia, Via Ripamonti 435; 20141 Milan, Italy.
Correspondence to: Martin Eilers1 e-mail: eilers@imt.uni-marburg.de
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