Journal
SCIENCE
Volume 314, Issue 5798, Pages 467-471Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1130276
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Funding
- NCI NIH HHS [R01-CA76584] Funding Source: Medline
- NIGMS NIH HHS [R01-GM57587] Funding Source: Medline
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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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