SSRP1 functions as a co-activator of the transcriptional activator p63

Shelya X. Zeng, Mu Shui Dai, David M. Keller, Hua Lu

Research output: Contribution to journalArticlepeer-review

75 Scopus citations


The p53 homolog p63 is a transcriptional activator. Here, we describe the identification of an HMG1-like protein SSRP1 as a co-activator of p63. Over-expression of wild-type, but not deletion mutant, SSRP1 remarkably enhanced p63γ-dependent luciferase activity, G1 arrest, apoptosis and expression of endogenous PIG3, p21Waf1/cip1 and MDM2 in human p53-deficient lung carcinoma H1299 cells and mouse embryonic fibroblasts. Also, SSRP1 interacted to p63γ in vitro and in cells, and resided with p63γ at the p53-responsive DNA element sites of the cellular endogenous MDM2 and p21Waf1/cip1 promoters. Moreover, N-terminus-deleted p63 (ΔN-p63) bound to neither SSRP1 nor its central domain in vitro. Accordingly, SSRP1 was unable to stimulate ΔN-p63-mediated residual luciferase activity and apoptosis in cells. Finally, the ectopic expression of the central p63-binding domain of SSRP1 inhibited p63-dependent transcription in cells. Thus, these results suggest that SSRP1 stimulates p63 activity by associating with this activator at the promoter.

Original languageEnglish (US)
Pages (from-to)5487-5497
Number of pages11
JournalEMBO Journal
Issue number20
StatePublished - Oct 15 2002


  • Apoptosis and cell cycle
  • Co-activator
  • SSRP1
  • Transcription
  • p63

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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