2003
DOI: 10.1038/nature02160
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Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly

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 subunit. This event is rate-limiting for translation, and depends on external stimuli and the status of the cell. Here we show that 60S subunits are activated by release of eIF6 (also termed p27BBP). In the cytoplasm, eIF6 is bound to free 60S but not to 80S. Furthermore, eIF6 interacts in the cytoplasm with RACK1, a receptor for activated protein kinase C (PKC). R… Show more

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Cited by 406 publications
(463 citation statements)
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“…RACK1 is a newly discovered ribosomal protein, present in all eukaryotic genomes and has so far been demonstrated to be present in the small subunit of yeast and human ribosomes (Link et al, 1999;Ceci et al, 2003; reviewed by Nilsson et al, 2004). RACK1 has been shown to interact with a number of different signalling molecules, such as Src, intergrin-b and PKC, and through this interaction is thought to mediate translation regulation.…”
Section: Discussionmentioning
confidence: 99%
“…RACK1 is a newly discovered ribosomal protein, present in all eukaryotic genomes and has so far been demonstrated to be present in the small subunit of yeast and human ribosomes (Link et al, 1999;Ceci et al, 2003; reviewed by Nilsson et al, 2004). RACK1 has been shown to interact with a number of different signalling molecules, such as Src, intergrin-b and PKC, and through this interaction is thought to mediate translation regulation.…”
Section: Discussionmentioning
confidence: 99%
“…The polyclonal antibody against the C terminus of eIF6 detects a specific 27 kDa band in immunoblot, which matches the predicted size of eIF6 (Biffo et al, 1997). However this antibody only recognizes eIF6 in the nucleolus ( Figure 3a) when used in immunocytochemistry, whereas immunoblot analysis demonstrates that the major fraction of eIF6 is actually in the cytoplasm (Ceci et al, 2003). We reasoned that the epitopes detected by the eIF6 antibody were masked in the cytoplasm when detected by immunocytochemistry, but were available in the denatured protein detected by western blot.…”
Section: Eif6 Selectively Regulates B-catenin Protein Levelsmentioning
confidence: 99%
“…eIF6 is essential for biogenesis of the 60S ribosome and must be released before proper assembly of 40S and 60S subunits can take place (Sanvito et al, 1999;Wood et al, 1999;Basu et al, 2001). In the cytoplasm, eIF6 is phosphorylated through the RACK1-PKCbII pathway and released from the 60S subunit, thus allowing the assembly of 40S and 60S subunits into the 80S ribosome (Ceci et al, 2003). In addition, casein kinase 1 (CK1) phosphorylation of eIF6 regulates its nucleocytoplasmic localization and mutant inactive eIF6 is constitutively nuclear suggesting that it has an important role in the cytoplasm (Basu et al, 2003).…”
Section: Introductionmentioning
confidence: 99%
“…For example, in transformed cultured cancer cells, RACK1 was shown to form a scaffolding complex that includes the IGF-1R, ␤1 integrin, and focal adhesion kinase (6,9,10,12). In addition, RACK1 is also found at the 40 S ribosomal subunit (3,13,14) and was shown to bridge protein kinase C-mediated signaling to the ribosomal translation machinery (15). RACK1 plays an important role in the central nervous system (16).…”
mentioning
confidence: 99%