@article {168,
	title = {An HDAC1-binding domain within FATS bridges p21 turnover to radiation-induced tumorigenesis.},
	journal = {Oncogene},
	volume = {29},
	year = {2010},
	month = {2010 May 6},
	pages = {2659-71},
	abstract = {<p>There is a gap between the initial formation of cells carrying radiation-induced genetic damage and their contribution to cancer development. Herein, we reveal a previously uncharacterized gene FATS through a genome-wide approach and demonstrate its essential role in regulating the abundance of p21 in surveillance of genome integrity. A large exon coding the NH2-terminal domain of FATS, deleted in spontaneous mouse lymphomas, is much more frequently deleted in radiation-induced mouse lymphomas. Its human counterpart is a fragile site gene at a previously identified loss of heterozygosity site. FATS is essential for maintaining steady-state level of p21 protein and sustaining DNA damage checkpoint. Furthermore, the NH2-terminal FATS physically interacts with histone deacetylase 1 (HDAC1) to enhance the acetylation of endogenous p21, leading to the stabilization of p21. Our results reveal a molecular linkage between p21 abundance and radiation-induced carcinogenesis.</p>},
	keywords = {Acetylation, Animals, Binding Sites, Cell Division, Chromosome Fragile Sites, Cyclin-Dependent Kinase Inhibitor p21, DNA Damage, G2 Phase, Histone Deacetylase 1, Humans, Mice, Neoplasms, Radiation-Induced, NIH 3T3 Cells, Tumor Suppressor Proteins, Ubiquitination},
	issn = {1476-5594},
	doi = {10.1038/onc.2010.19},
	author = {Li, Z and Zhang, Q and Jiang-Hua Mao and Weise, A and Mrasek, K and Fan, X and Zhang, X and Liehr, T and Lu, K H and Balmain, A and Cai, W-W}
}
