4.5 Article

TIP30 Directly Binds p53 Tumor Suppressor Protein In Vitro

Journal

MOLECULES AND CELLS
Volume 34, Issue 5, Pages 495-500

Publisher

KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
DOI: 10.1007/s10059-012-0232-x

Keywords

GST pull-down assay; p53; protein-protein interaction; surface plasmon resonance; TIP30

Funding

  1. National R&D Program for Cancer Control
  2. Ministry for Health and Welfare, Republic of Korea [0920240]
  3. Korean-Hungarian Joint Laboratory Program grant [UGM0021011]
  4. Korea Health Promotion Institute [0920240] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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TIP30 (30 kDa HIV-1 TAT-interacting protein), also called HTATIP2 or CC3, is a tumor suppressor protein that acts as an angiogenesis inhibitor. TIP30 blocks nuclear import of the mRNA-binding protein HuR, and thereby promotes the cytoplasmic accumulation of HuR by binding to importin-beta, which is known to facilitate the cytoplasm-tonuclear transport of HuR. Accumulation of HuR in the cytoplasm, in turn, enhances the expression of the transcription factor p53, a tumor suppressor that plays an essential role in preserving genome stability and inhibiting cancer growth. In addition to such a post-transcriptional mechanism via which TIP30 increases the p53 level, it has been proposed that TIP30 may regulate p53 protein at the protein level by directly binding to it. In order to investigate the possibility of direct interaction between p53 and TIP30, we have used on three functional regions in p53 and examined their interactions with TIP30 using GST pull-down assay and surface plasmon resonance technique. The results show that that TIP30 binds to the DNA-binding domain and the C-terminal domain of p53.

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