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eLife

eLife

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Clearance of protein aggregates during cell division

Published:6 June 2025 DOI: 10.7554/eLife.96675 PMID: 40476343
Shoukang Du,?Yuhan Wang,?Bowen Chen,?Shuangshuang Xie,?Kuan Yoow Chan,?David C Hay,?Ting Gang Chew

Abstract

Protein aggregates are spatially organized and regulated in cells to prevent the deleterious effects of proteostatic stress. Misfolding of proteins in the endoplasmic reticulum (ER) results in aggregate formation, but how the aggregates are processed, especially during cell division is not well understood. Here, we induced proteostatic stress and protein aggregation using a proteostasis reporter, which is prone to misfolding and aggregation in the ER. Unexpectedly, we detected solid-like protein aggregates deposited mainly in the nucleus and surrounded by the ER membrane. The membrane-bound aggregates were then cleared as cells progressed through mitosis and cytokinesis. Aggregate clearance depended on Hsp70 family chaperones in the ER, particularly BiP, and proteasomal activity. The clearance culminated at mitotic exit and required cyclin-dependent kinase 1 (Cdk1) inactivation but was independent of the anaphase-promoting complex (APC/C). The ER reorganization that is active during mitosis and cytokinesis was required for the aggregate clearance. Thus, dividing cells reorganize the ER networks to allow BiP to clear the protein aggregates to maintain proteostasis in the newly divided cells.

Substances (4)

Materials
Procduct Name CAS Molecular Formula Supplier Price
MLN-8237 1028486-01-2 C27H20ClFN4O4 226 suppliers $17.00-$2691.10
MLN-8237 1028486-01-2 C27H20ClFN4O4 226 suppliers $17.00-$2691.10
MLN-8237 1028486-01-2 C27H20ClFN4O4 226 suppliers $17.00-$2691.10
MLN-8237 1028486-01-2 C27H20ClFN4O4 226 suppliers $17.00-$2691.10

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