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Updated: Jul 4, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
[The multifunctionality of CHIP protein in the protein quality-control system]
Robert Lenartowski1, Krzysztof Gumowski, Anna Goc
1Instytut Biologii Ogólnej i Molekularnej, Zakład Genetyki, Uniwersytet Mikołaja Kopernika w Toruniu, Toruń. rlenart@umk.pl <rlenart@umk.pl>
Abstract:
Selective protein degradation depends on their quality being controlled by the cellular system, which includes chaperones involved in protein folding and two degradation systems, the proteasomal and lysosomal. CHIP (carboxyl terminus of Hsp70-interacting protein), an E3 ubiquitin ligase and co-chaperone, serves as a chaperone-degradation system interface. This article reviews the molecular characteristics of CHIP protein, the mechanism of its action, and its role in cellular metabolism and discusses how CHIP dysfunction may lead to neurodegenerative diseases.
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