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Related Experiment Video

Updated: May 3, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

CHIP/Stub1 interacts with eIF5A and mediates its degradation.

Yu Shang¹, Xinghui Zhao², Bo Tian³

¹The Key Laboratory for Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing 100875, China; State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Medicine, Tsinghua University, Beijing 100084, China.

Cellular Signalling

|February 11, 2014

Summary

The carboxyl terminus of Hsc70-interacting protein (CHIP) targets eukaryotic initiation factor 5A (eIF5A) for degradation. This E3 ligase regulates eIF5A protein stability, offering new insights into cellular processes.

Keywords:

CHIP/Stub1 Colorectal cancer E3 ligase Protein–protein interaction eIF5A degradation

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Area of Science:

Molecular and Cellular Biology
Protein Regulation
Cancer Biology

Background:

eIF5A is essential for eukaryotic cell proliferation and its activity is regulated by hypusine modification, phosphorylation, and acetylation.
Regulation of eIF5A protein stability remained largely uncharacterized.

Purpose of the Study:

To investigate the mechanisms regulating eIF5A protein stability.
To identify proteins that interact with and modify eIF5A.

Main Methods:

Proteomics analysis to identify eIF5A interacting partners.
Co-immunoprecipitation assays to confirm protein interactions.
Western blotting to assess protein levels in wild-type and knockout cells.
Analysis of patient tumor data for expression correlation.

Main Results:

CHIP, an E3 ligase, was identified as a novel interactor of eIF5A.
CHIP directly binds to eIF5A, promoting its ubiquitination and subsequent degradation.
CHIP expression inversely correlates with eIF5A levels in colorectal cancers.
eIF5A protein levels are elevated in CHIP-knockout cells.

Conclusions:

CHIP regulates eIF5A protein stability through a ubiquitin-proteasome degradation pathway.
This study reveals a new mechanism for controlling eIF5A levels, impacting eukaryotic cell proliferation and potentially cancer development.