biostudies-literatureKumar SScience and Engineering Research BoardCouncil of Scientific and Industrial Research, IndiaDepartment of Science and Technology, Ministry of Science and Technology, India1521-1555https://www.ebi.ac.uk/biostudies/studies/S-EPMC9485218biostudies-literatureUnknown9(6)The carboxy-terminus of Hsp70-interacting protein (CHIP) is a ubiquitin ligase and co-chaperone belonging to Ubox family that plays a crucial role in the maintenance of cellular homeostasis by switching the equilibrium of the folding-refolding mechanism towards the proteasomal or lysosomal degradation pathway. It links molecular chaperones <i>viz</i>. HSC70, HSP70 and HSP90 with ubiquitin proteasome system (UPS), acting as a quality control system. CHIP contains charged domain in between N-terminal tetratricopeptide repeat (TPR) and C-terminal Ubox domain. TPR domain interacts with the aberrant client proteins <i>via</i> chaperones while Ubox domain facilitates the ubiquitin transfer to the client proteins for ubiquitination. Thus, CHIP is a classic molecule that executes ubiquitination foGenes & diseasesChaperone-assisted E3 ligase CHIP: A double agent in cancer.PMC9485218DST/NM/NT/2018/105Basu MGhosh MKKumar SfalseChaperone-assisted E3 ligase CHIP: A double agent in cancer.The carboxy-terminus of Hsp70-interacting protein (CHIP) is a ubiquitin ligase and co-chaperone belonging to Ubox family that plays a crucial role in the maintenance of cellular homeostasis by switching the equilibrium of the folding-refolding mechanism towards the proteasomal or lysosomal degradation pathway. It links molecular chaperones <i>viz</i>. HSC70, HSP70 and HSP90 with ubiquitin proteasome system (UPS), acting as a quality control system. CHIP contains charged domain in between N-terminal tetratricopeptide repeat (TPR) and C-terminal Ubox domain. TPR domain interacts with the aberrant client proteins <i>via</i> chaperones while Ubox domain facilitates the ubiquitin transfer to the client proteins for ubiquitination. Thus, CHIP is a classic molecule that executes ubiquitination fo2022-01-01T00:00:00Z2022 Nov2026-07-14T15:50:07.882Z2025-04-05T12:10:51.208ZS-EPMC94852183615749810.1016/j.gendis.2021.08.003