Cited by 218Heat shock proteins researchUbiquitin and proteasome pathwaysAutophagy in Disease and Therapy

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CHIP: a quality-control E3 ligase collaborating with molecular chaperones

Murata, Shigeo, Chiba, Tomoki, Tanaka, Keiji·2003·The International Journal of Biochemistry & Cell Biology

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Abstract

It is notable that both the chaperone and ubiquitin-proteasome systems are required for removal of aberrant cellular proteins to ensure protein homeostasis in cells. However, the entity that links the two systems had remained elusive. Carboxyl-terminus of Hsc70 interacting protein (CHIP), originally identified as a co-chaperone of Hsc70, has both a tetratricopeptide repeat (TPR) motif and a U-box domain. The TPR motif associates with Hsc70 and Hsp90, while the U-box domain executes a ubiquitin ligase activity. Thus, CHIP is an ideal molecule acting as a protein quality-control ubiquitin ligase that selectively leads abnormal proteins recognized by molecular chaperones to degradation by the proteasome. Accumulating evidence from in vitro studies indicates that this is apparently the case. Here, we present and discuss several unresolved but critical issues related to the molecular mechanism and in vivo roles of CHIP.

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Authors: Murata, S., Chiba, T., & Tanaka, K.
Affiliations: Tokyo Metropolitan Institute of Medical Science (JP)
Corresponding author: Murata, Shigeo
ORCID: Murata, Shigeo
Chiba, Tomoki
Tanaka, Keiji
Venue: The International Journal of Biochemistry & Cell Biology
Publisher: Elsevier BV
Published: 2003-05
Volume: 35
Issue: 5
Pages: 572-578
ISSN: 1357-2725 (ISSN-L)
DOI: 10.1016/s1357-2725(02)00394-1
OpenAlex: W2069183580
Cited by: 218
References: 33
Citations by year: 2026: 3 · 2025: 2 · 2024: 5 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 6 · 2019: 7 · 2018: 8 · 2017: 15 · 2016: 7 · 2015: 6 · 2014: 10 · 2013: 9 · 2012: 22
FWCI: 0.88
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: The International Journal of Biochemistry & Cell Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: CHIP, E3 ubiquitin ligase, molecular chaperones, protein quality control, proteostasis, ubiquitin-proteasome system, HSP90, U-box domain, protein degradation
MeSH terms: Animals, Cysteine Endopeptidases, Humans, Multienzyme Complexes, Protein Denaturation, Protein Folding, Molecular Chaperones, HSP70 Heat-Shock Proteins, Neurodegenerative Diseases, Ubiquitin, Proteasome Endopeptidase Complex, HSC70 Heat-Shock Proteins, Mice

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CHIP: a quality-control E3 ligase collaborating with molecular chaperones

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