The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
CHIP: a quality-control E3 ligase collaborating with molecular chaperones
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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“However, molecular chaperones Hsp70 and Hsp90 can also recruit the co-chaperone E3 ligase CHIP (C-terminus of Hsp70 interacting protein), which leads to ubiquitination and degradation of the chaperone-bound client proteins [56–59].”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [58]
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Metadata
- Authors
- Murata, S., Chiba, T., & Tanaka, K.
- Affiliations
- Tokyo Metropolitan Institute of Medical Science (JP)
- Corresponding author
- Murata, Shigeo
- 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)
- 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
- 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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