RAB40C regulates RACK1 stability via the ubiquitin-proteasome system

Jon P. Day; Ellanor Whiteley; Michael Freeley; Aideen Long; Beatrice Malacrida; Patrick Kiely; George S. Baillie

doi:10.4155/fsoa-2018-0022

RAB40C regulates RACK1 stability via the ubiquitin-proteasome system

Jon P. Day, Ellanor Whiteley, Michael Freeley, Aideen Long, Beatrice Malacrida, Patrick Kiely, George S. Baillie

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Article number	FSO317
Pages (from-to)	FSO317
Journal	Future Science OA
Volume	4
Issue number	7
DOIs	https://doi.org/10.4155/fsoa-2018-0022
Publication status	Published - 2018

Keywords

RAB40C
RACK1
Ubiquitin-proteasome system

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.4155/fsoa-2018-0022

Cite this

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title = "RAB40C regulates RACK1 stability via the ubiquitin-proteasome system",

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.",

keywords = "RAB40C, RACK1, Ubiquitin-proteasome system",

author = "Day, {Jon P.} and Ellanor Whiteley and Michael Freeley and Aideen Long and Beatrice Malacrida and Patrick Kiely and Baillie, {George S.}",

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doi = "10.4155/fsoa-2018-0022",

language = "English",

volume = "4",

pages = "FSO317",

journal = "Future Science OA",

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T1 - RAB40C regulates RACK1 stability via the ubiquitin-proteasome system

AU - Day, Jon P.

AU - Whiteley, Ellanor

AU - Freeley, Michael

AU - Long, Aideen

AU - Malacrida, Beatrice

AU - Kiely, Patrick

AU - Baillie, George S.

PY - 2018

Y1 - 2018

N2 - 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.

AB - 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.

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RAB40C regulates RACK1 stability via the ubiquitin-proteasome system

Abstract

Keywords

UN SDGs

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