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Zhejian Ji

As seen in: Nature, Science Magazine, BioRxiv, Cell Press
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Articles

ATP-independent unfolding of ubiquitin by Ufd1 initiates Cdc48/p97-mediated substrate processing

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By Yanzhu Wang, Zhimin Zhang, Pengyu Wang, Jiang Du, Jinheng Pan, Shan Feng, Jing Huang, Zhejian Ji
| Nature Verified
Abstract The Cdc48 ATPase (p97 or VCP in mammals) cooperates with its cofactors Ufd1 and Npl4 to extract polyubiquitinated proteins from membranes or multisubunit complexes, promoting their proteasomal degradation. A ubiquitin molecule in the chain is unfolded in an ATP-independent manner and initiates substrate translocation through the central pore of the ATPase. How ubiquitin is unfolded remains unclear.
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Torsins organize CLCC1 assembly to safeguard ER bilayer and lipid homeostasis

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By Yonglun Wang, Renqian Wang, Yuanhang Yao, Rongxian Hou, Lu Yan, Yiechang Lin, Yating Hu, Youlei Li, Lingzhi Wu, Yuangang Zhu, Ning Gao, Chen Song, Xiao Wang, Zhejian Ji, Xiao-Wei Chen
| Cell Press Verified
Keywords lipid metabolism ER membrane homeostasis AAA+ ATPase torsins Get full text access Log in, subscribe or purchase for full access. References 1. Mathiowetz, A.J. ∙ Olzmann, J.A. Lipid droplets and cellular lipid flux Nat. Cell Biol. 2024; 26:331-345 2. Feingold, K.R. Lipid and Lipoprotein Metabolism Endocrinol. Metab. Clin. N. Am. 2022; 51:437-458 3. Roth, G.A. ∙ Abate, D. ∙ Abate, K.H. ...
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Bidirectional substrate shuttling between the 26S proteasome and the Cdc48 ATPase promotes protein degradation

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By Zhejian Ji, João Paulo, Steven Gygi, Tom A. Rapoport
| Cell Press Verified
Highlights • Cdc48 ATPase-dependent proteasomal protein degradation reconstituted in vitro • Substrate shuttling between the proteasome and Cdc48 is mediated by Rad23 and Ubx5 • Shp1 stimulates protein unfolding by Cdc48, rather than substrate recruitment • Bidirectional substrate shuttling between the molecular machines occurs in yeast Summary Most eukaryotic proteins are degraded by the 26S proteasome after modification with a polyubiquitin chain.
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