Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly

Marcello Ceci, Cristina Gaviraghi, Chiara Gorrini, Leonardo A. Sala, Nina Offenhäuser, Pier Carlo Marchisio and Stefano Biffo ()
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Marcello Ceci: DIBIT-HSR
Cristina Gaviraghi: DIBIT-HSR
Chiara Gorrini: DIBIT-HSR
Leonardo A. Sala: DIBIT-HSR
Nina Offenhäuser: Firc Institute for Molecular Oncology
Pier Carlo Marchisio: DIBIT-HSR
Stefano Biffo: DIBIT-HSR

Nature, 2003, vol. 426, issue 6966, 579-584

Abstract: Abstract The assembly of 80S ribosomes requires joining of the 40S and 60S subunits, which is triggered by the formation of an initiation complex on the 40S subunit1. This event is rate-limiting for translation2, and depends on external stimuli3 and the status of the cell4. Here we show that 60S subunits are activated by release of eIF6 (also termed p27BBP)5,6. In the cytoplasm, eIF6 is bound to free 60S but not to 80S. Furthermore, eIF6 interacts in the cytoplasm with RACK17, a receptor for activated protein kinase C (PKC). RACK1 is a major component of translating ribosomes, which harbour significant amounts of PKC. Loading 60S subunits with eIF6 caused a dose-dependent translational block and impairment of 80S formation, which were reversed by expression of RACK1 and stimulation of PKC in vivo and in vitro. PKC stimulation led to eIF6 phosphorylation, and mutation of a serine residue in the carboxy terminus of eIF6 impaired RACK1/PKC-mediated translational rescue. We propose that eIF6 release regulates subunit joining, and that RACK1 provides a physical and functional link between PKC signalling and ribosome activation.

Date: 2003
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DOI: 10.1038/nature02160

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