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Regulation of eukaryotic translation by the RACK1 protein: a platform for signalling molecules on the ribosome
Author(s) -
Nilsson Jakob,
Sengupta Jayati,
Frank Joachim,
Nissen Poul
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400291
Subject(s) - microbiology and biotechnology , internal ribosome entry site , eukaryotic ribosome , eif4e , translation (biology) , ribosome , initiation factor , biology , eukaryotic initiation factor , messenger rna , chemistry , rna , biochemistry , gene
The receptor for activated C‐kinase (RACK1) is a scaffold protein that is able to interact simultaneously with several signalling molecules. It binds to protein kinases and membrane‐bound receptors in a regulated fashion. Interestingly, RACK1 is also a constituent of the eukaryotic ribosome, and a recent cryo‐electron microscopy study localized it to the head region of the 40S subunit in the vicinity of the messenger RNA (mRNA) exit channel. RACK1 recruits activated protein kinase C to the ribosome, which leads to the stimulation of translation through the phosphorylation of initiation factor 6 and, potentially, of mRNA‐associated proteins. RACK1 therefore links signal‐transduction pathways directly to the ribosome, which allows translation to be regulated in response to cell stimuli. In addition, the fact that RACK1 associates with membrane‐bound receptors indicates that it promotes the docking of ribosomes at sites where local translation is required, such as focal adhesions.