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Biochem Biophys Res Commun. 2002 Apr 26;293(1):617-21.

Up-regulation of PDCD4 in senescent human diploid fibroblasts.

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  • 1Department of Biochemistry and Molecular Biology and Ilchun Molecular Medicine Institute, Seoul National University College of Medicine, 28 Yongondong, Chongnogu, Seoul 110-799, Republic of Korea.

Abstract

Programmed cell death 4 (PDCD4) has a common MI domain sharing with death associated protein 5 (DAP5) and a component of eukaryotic translation initiation factor (eIF4G) complex and it might also work as a tumor suppressor. We could find that the message and product of Pdcd4 gene were up-regulated in senescent human diploid fibroblasts. In yeast two hybrid analysis, the C-terminal region of PDCD4 interacted with ribosomal protein S13 (RPS13), ribosomal protein L5 (RPL5), and TI-227H. In in vitro binding assay, RPS13, a component of 40S ribosome was stably bound to PDCD4. We also found that PDCD4 was localized to polysome fractions. We could pull out eIF4G with GST-PDCD4, but eIF4E did not interact with PDCD4. From these results, we could assume that PDCD4 might regulate the eIF4G-dependent translation through direct interactions with eIF4G and RPS13 in senescent fibroblasts.

PMID:
12054647
[PubMed - indexed for MEDLINE]
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