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

  1. Author:
    Dorrello, N. V.
    Peschiaroli, A.
    Guardavaccaro, D.
    Colburn, N. H.
    Sherman, N. E.
    Pagano, M.

  2. Author Address

    NYU, Sch Med, Inst Canc, Dept Pathol, New York, NY 10016 USA. NCI, Lab Canc Prevent, Frederick, MD 21702 USA. Univ Virginia, WM Keck Biomed Mass Spectrometry Lab, Charlottesville, VA 22908 USA.;Pagano, M, NYU, Sch Med, Inst Canc, Dept Pathol, 550 1st Ave,MSB 599, New York, NY 10016 USA.;michele.pagano@med.nyu.edu
    1. Year: 2006
    2. Date: Oct
  2. Journal: Science
    1. 314
    2. 5798
    3. Pages: 467-471
  4. Type of Article: Article
  5. ISSN: 0036-8075
  1. 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 Ser(67) by the protein kinase S6K1 and subsequently degraded via the ubiquitin ligase SCF beta TRCP. Expression in cultured cells of a stable PDCD4 mutant that is unable to bind beta TRCP 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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External Sources

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  2. DOI: 10.1126/science.1130276
  3. View record in Web of Science®
  4. WOS: 000241382500043

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