iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human

We have previously shown that ASPP1 and ASPP2 are specific activators of p53; one mechanism by which wild-type p53 is tolerated in human breast carcinomas is through loss of ASPP activity. We have further shown that 53BP2, which corresponds to a C-terminal fragment of ASPP2, acts as a dominant negative inhibitor of p53 (ref. 1). Hence, an inhibitory form of ASPP resembling 53BP2 could allow cells to bypass the tumor-suppressor functions of p53 and the ASPP proteins. Here, we characterize such a protein, iASPP (inhibitory member of the ASPP family), encoded by PPP1R13L in humans and ape-1 in Caenorhabditis elegans. iASPP is an evolutionarily conserved inhibitor of p53; inhibition of iASPP by RNA-mediated interference or antisense RNA in C. elegans or human cells, respectively, induces p53-dependent apoptosis. Moreover, iASPP is an oncoprotein that cooperates with Ras, E1A and E7, but not mutant p53, to transform cells in vitro. Increased expression of iASPP also confers resistance to ultraviolet radiation and to cisplatin-induced apoptosis. iASPP expression is upregulated in human breast carcinomas expressing wild-type p53 and normal levels of ASPP. Inhibition of iASPP could provide an important new strategy for treating tumors expressing wild-type p53.

[1]  G. Rubin,et al.  Drosophila p53 Binds a Damage Response Element at the reaper Locus , 2000, Cell.

[2]  D. Holdstock Past, present--and future? , 2005, Medicine, conflict, and survival.

[3]  Xin Lu,et al.  E2F1-induced apoptosis requires DNA binding but not transactivation and is inhibited by the retinoblastoma protein through direct interaction. , 1997, Genes & development.

[4]  K. Vousden,et al.  Transcriptional activation by p53 correlates with suppression of growth but not transformation , 1994, Cell.

[5]  E. Harlow,et al.  Antibodies: A Laboratory Manual , 1988 .

[6]  A. Fire,et al.  Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans , 1998, Nature.

[7]  K. Hofmann,et al.  The C. elegans homolog of the p53 tumor suppressor is required for DNA damage-induced apoptosis , 2001, Current Biology.

[8]  H. Horvitz,et al.  Genetics of programmed cell death in C. elegans: past, present and future. , 1998, Trends in genetics : TIG.

[9]  Xin Lu,et al.  ASPP proteins specifically stimulate the apoptotic function of p53. , 2001, Molecular cell.

[10]  M. Belvin,et al.  Drosophila p53 Is a Structural and Functional Homolog of the Tumor Suppressor p53 , 2000, Cell.

[11]  T. Okamoto,et al.  Identification of a Novel Inhibitor of Nuclear Factor-κB, RelA-associated Inhibitor* , 1999, The Journal of Biological Chemistry.

[12]  N. Pavletich,et al.  Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2 , 1996, Science.

[13]  W. B. Derry,et al.  Caenorhabditis elegans p53: Role in Apoptosis, Meiosis, and Stress Resistance , 2001, Science.