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RACK1, A multifaceted scaffolding protein: Structure and function

David R Adams1, Dorit Ron2 and Patrick A Kiely3*

Author Affiliations

1 Department of Chemistry, Heriot-Watt University, Riccarton Campus, Edinburgh EH14AS, UK

2 Ernest Gallo Research Center, Department of Neurology, University of California, San Francisco, Emeryville, CA, USA 94608

3 Department of Life Sciences, and Materials and Surface Science Institute, University of Limerick, Limerick, Ireland

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Cell Communication and Signaling 2011, 9:22  doi:10.1186/1478-811X-9-22

Published: 6 October 2011


The Receptor for Activated C Kinase 1 (RACK1) is a member of the tryptophan-aspartate repeat (WD-repeat) family of proteins and shares significant homology to the β subunit of G-proteins (Gβ). RACK1 adopts a seven-bladed β-propeller structure which facilitates protein binding. RACK1 has a significant role to play in shuttling proteins around the cell, anchoring proteins at particular locations and in stabilising protein activity. It interacts with the ribosomal machinery, with several cell surface receptors and with proteins in the nucleus. As a result, RACK1 is a key mediator of various pathways and contributes to numerous aspects of cellular function. Here, we discuss RACK1 gene and structure and its role in specific signaling pathways, and address how posttranslational modifications facilitate subcellular location and translocation of RACK1. This review condenses several recent studies suggesting a role for RACK1 in physiological processes such as development, cell migration, central nervous system (CN) function and circadian rhythm as well as reviewing the role of RACK1 in disease.

RACK1; WD-repeat; guanine nucleotide binding protein 2-like 1; (Gβ); heterotrimeric G-proteins; PKCβII; scaffolding protein