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Updated: Apr 29, 2026
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In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
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The E3 ligase CHIP: insights into its structure and regulation
Indranil Paul1, Mrinal K Ghosh1
1Cancer Biology and Inflammatory Disorder Division, Council of Scientific and Industrial Research-Indian Institute of Chemical Biology (CSIR-IICB), 4 Raja S.C. Mullick Road, Kolkata 700032, India.
Biomed Research International
|May 29, 2014
Summary
The carboxy-terminus of Hsc70 interacting protein (CHIP) is a key E3 ligase regulating cellular processes. This review details CHIP
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- The carboxy-terminus of Hsc70 interacting protein (CHIP) is a crucial cochaperone E3 ligase.
- CHIP contains tetratricopeptide (TPR) motifs and a U-box domain, mediating protein quality control.
- CHIP regulates numerous proteins vital for physiological and pathological processes.
Purpose of the Study:
- To provide a concise review of the current understanding of CHIP biochemistry.
- To summarize the regulatory mechanisms influencing CHIP activity.
- To highlight CHIP's role in maintaining cellular homeostasis.
Main Methods:
- Literature review of recent studies on CHIP.
- Analysis of CHIP's structural and functional domains.
- Synthesis of information on CHIP's regulatory pathways.
Main Results:
- CHIP functions as a central E3 ligase in cellular quality control.
- Its activity is modulated by various regulatory mechanisms.
- Understanding CHIP regulation is essential for cellular homeostasis.
Conclusions:
- CHIP is a critical regulator of cellular processes through its E3 ligase activity.
- Varied mechanisms control CHIP activity, impacting cellular health.
- This review consolidates current knowledge on CHIP biochemistry and regulation.
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