RACK1 story

The receptor for activated C-kinase 1 (RACK1) is a protein evolutionarily conserved from yeast to mammals. RACK1 is a member of the WD40 repeat protein family, an abundant group of proteins with a conserved structure. A canonical WD40 protein comprises seven repeats, each of which contains 40–60 residues with a WD motif (tryptophan and aspartic acid or their equivalent). Each repeat typically folds into a four-stranded anti-parallel β-sheet (blade). These blades together form a β-propeller structure that enables molecular interactions and the assembly of protein complexes.

RACK1 is the focus of contemporary research due to its engagement in many fundamental yet unrelated processes, including translation, cell polarization and motility or apoptosis. RACK1 importance is manifested by its essentiality, and its malfunction leads to immune defects, neuronal diseases or enhanced invasiveness of cancer cells.

RACK1 is also a known component of stress granules (SGs). These ribonucleoprotein assemblies shape translation responses upon stress conditions and possess cytoprotective functions. On the other hand, a malfunction of SGs is linked to several human disorders.

We are heading toward a better understanding of RACK1 involvement in translation, stress response, apoptosis and its implications in related disorders.