Literature search services are currently unavailable. During our hosting provider's UPS upgrade we experienced a hardware failure and are currently working to resolve the issue.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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