Functional importance and structure of small ribosomal protein RACK1

Abstract

The Receptor for Activated C Kinase 1 (RACK1) protein is one of the ribosomal proteins that is located in the small subunit which is maintained across most of the eukaryotes and functions as a flexible scaffold protein involved in multiple signaling pathways. It is considered as a highly conserved protein that found in a wide range of tryptophan-aspartate (WD40) repeat proteins of eukaryotic organisms, from Chlamydomonas to plants and mammals. RACK1 adopts a propeller structure with seven blades structures, enabling the binding capability of the protein. RACK1 participates in shuttling and anchoring of proteins around the cells at certain positions and it stabilizes protein production during translation. RACK1 is a member of the protein family WD repeat that consists of seven-bladed βpropeller structure which shares important homology to the G-proteins (Gb) β-subunit. It interacts with the ribosomal machinery, multiple receptors of the cell surface and the nuclear proteins. RACK1 is a key mediator of different pathways and contributes to a variety of cellular functional aspects. This review discusses the main function of RACK1 protein in eukaryotes including animals and plants. Furthermore, we will show the recent study on RACK1 function in different organisms. © 2022 Production by the University of Garmian. This is an open access article under the LICENSE https://creativecommons.org/licenses/by-nc/4.0/