RACK1, A multifaceted scaffolding protein: Structure and function

David R. Adams, Dorit Ron, Patrick A. Kiely

Research output: Contribution to journalLiterature review

233 Citations (Scopus)

Abstract

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 beta subunit of G-proteins (G beta). RACK1 adopts a seven-bladed beta-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.

Original languageEnglish
Article number22
Number of pages24
JournalCell Communication and Signaling
Volume9
DOIs
Publication statusPublished - 6 Oct 2011

Keywords

  • RACK1
  • WD-repeat
  • guanine nucleotide binding protein 2-like 1
  • (G beta)
  • heterotrimeric G-proteins
  • PKC beta II
  • scaffolding protein
  • ACTIVATED-C-KINASE
  • WD-REPEAT PROTEINS
  • G-BETA-GAMMA
  • HETEROTRIMERIC G-PROTEINS
  • RECEPTOR-INTERACTING PROTEIN
  • ANCHORAGE-INDEPENDENT GROWTH
  • PRO-APOPTOTIC FUNCTION
  • CRYSTAL-STRUCTURE
  • CELL-MIGRATION
  • FOCAL ADHESIONS

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