S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth - PubMed (original) (raw)

. 2006 Oct 20;314(5798):467-71.

doi: 10.1126/science.1130276.

Affiliations

• PMID: 17053147
• DOI: 10.1126/science.1130276

S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth

N Valerio Dorrello et al. Science. 2006.

Abstract

The tumor suppressor programmed cell death protein 4 (PDCD4) inhibits the translation initiation factor eIF4A, an RNA helicase that catalyzes the unwinding of secondary structure at the 5' untranslated region (5'UTR) of messenger RNAs (mRNAs). In response to mitogens, PDCD4 was rapidly phosphorylated on Ser67 by the protein kinase S6K1 and subsequently degraded via the ubiquitin ligase SCF(betaTRCP). Expression in cultured cells of a stable PDCD4 mutant that is unable to bind betaTRCP inhibited translation of an mRNA with a structured 5'UTR, resulted in smaller cell size, and slowed down cell cycle progression. We propose that regulated degradation of PDCD4 in response to mitogens allows efficient protein synthesis and consequently cell growth.

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Comment in

• Signal transduction. Protein synthesis and oncogenesis meet again.
  Sonenberg N, Pause A. Sonenberg N, et al. Science. 2006 Oct 20;314(5798):428-9. doi: 10.1126/science.1134031. Science. 2006. PMID: 17053135 No abstract available.

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