Daly, J. P., Whiteley, E., Freeley, M., Long, A., Malacrida, B., Kiely, P. and Baillie, G. S. (2018) RAB40C regulates RACK1 stability via the ubiquitin-proteasome system. Future Science OA, 4(7), FSO317. (doi: 10.4155/fsoa-2018-0022) (PMID:30112187) (PMCID:PMC6088270)
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Abstract
Aim: RACK1 is a multifunctional scaffolding protein that is expressed in many cellular compartments, orchestrating a number of signaling processes. RACK1 acts as a signaling hub to localize active enzymes to discrete locations; therefore tight control of RACK1 is vital to cellular homeostasis. Our aim was to identify the mechanisms responsible for RACK1 turnover and show that degradation is directed by the ubiquitin proteasome system. Results: Using siRNA screening, we identified RAB40C as the ubiquitin E3 ligase responsible for ubiquitination of RACK1, and that the action of RAB40C in controlling RACK1 levels is crucial to both cancer cell growth and migration of T cells. Conclusion: Our data suggest that manipulation of RACK1 levels in this way may provide a novel strategy to explore RACK1 function.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Baillie, Professor George and WHITELEY, Ellanor |
| Authors: | Daly, J. P., Whiteley, E., Freeley, M., Long, A., Malacrida, B., Kiely, P., and Baillie, G. S. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Cardiovascular & Metabolic Health |
| Journal Name: | Future Science OA |
| Publisher: | Future Science |
| ISSN: | 2056-5623 |
| ISSN (Online): | 2056-5623 |
| Published Online: | 02 July 2018 |
| Copyright Holders: | Copyright © 2018 Glasgow University |
| First Published: | First published in Future Science OA 4(7): FSO317 |
| Publisher Policy: | Reproduced under a Creative Commons License |
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