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An HDAC1-binding domain within FATS bridges p21 turnover to radiation-induced tumorigenesis.

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.

Pubmed ID: 20154723


  • Li Z
  • Zhang Q
  • Mao JH
  • Weise A
  • Mrasek K
  • Fan X
  • Zhang X
  • Liehr T
  • Lu KH
  • Balmain A
  • Cai WW



Publication Data

May 6, 2010

Associated Grants


Mesh Terms

  • Acetylation
  • Animals
  • Binding Sites
  • Cell Division
  • Chromosome Fragile Sites
  • Cyclin-Dependent Kinase Inhibitor p21
  • DNA Damage
  • G2 Phase
  • Histone Deacetylase 1
  • Humans
  • Mice
  • NIH 3T3 Cells
  • Neoplasms, Radiation-Induced
  • Tumor Suppressor Proteins
  • Ubiquitination