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RACK1 Specifically Regulates Translation through its Binding to Ribosomes.

The translational capability of ribosomes deprived of specific non-fundamental ribosomal proteins may be altered. Physiological mechanisms are scanty and it is unclear whether free ribosomal proteins can crosstalk with the signaling machinery. RACK1 (Receptor for Activated C Kinase 1) is a highly conserved scaffold protein, located on the 40S subunit near the mRNA exit channel. RACK1 is involved in a variety of intracellular contexts, both on and off the ribosomes, acting as a receptor for proteins in signaling like PKCs. Here we show that binding of RACK1 to ribosomes is essential for full translation of capped mRNAs and efficient recruitment of eIF4E (eukaryotic Initiation Factor 4E). In vitro , supplementing the ribosome machinery with wild-type RACK1 restores the translational capability, whereas addition of a RACK1 mutant unable to bind ribosomes does not. Out of the ribosome, RACK1 has a reduced half-life. By accumulating in living cells, free RACK1 exerts an inhibitory phenotype by impairing cell cycle progression and repressing global translation. Here we present RACK1 binding to ribosomes as a crucial way to regulate translation, possibly by interacting with known signaling-involved partners on or out of the ribosome.

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