Dysfunctional uch-l1 inhibits proteostasis

Dysfunctional uch-l1 inhibits proteostasis

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Access through your institution Buy or subscribe Podocyte injury in membranous nephritis (MN) is associated with induction of the ubiquitin proteasome system. Meyer-Schwesinger and


colleagues previously reported de novo expression of ubiquitin C-terminal hydrolase-L1 (UCH-L1) in MN and now show a link between dysfunctional UCH-L1 and impaired podocyte proteostasis. The


researchers also showed that UCH-L1 binds to the proteasome and that the modified, but not the wild-type, protein inhibits proteasome activity, potentially by interfering with substrate


access. The detection of antibodies that preferentially bind variant UCH-L1 in patients with MN suggests that inhibition of the proteasome mediated by non-functional UCH-L1 might contribute


to podocyte injury in MN. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Access Nature and 54 other Nature Portfolio


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during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support REFERENCES ORIGINAL ARTICLE * Reichelt, J. et al.


Non-functional ubiquitin C-terminal hydrolase L1 drives podocyte injury through impairing proteasomes in autoimmune glomerulonephritis. _Nat. Commun._ 14, 2114 (2023) Article  CAS  PubMed 


PubMed Central  Google Scholar  Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Nature Reviews Nephrology http://www.nature.com/nrneph Monica Wang Authors * Monica Wang


View author publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence to Monica Wang. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT


THIS ARTICLE CITE THIS ARTICLE Wang, M. Dysfunctional UCH-L1 inhibits proteostasis. _Nat Rev Nephrol_ 19, 424 (2023). https://doi.org/10.1038/s41581-023-00730-z Download citation *


Published: 31 May 2023 * Issue Date: July 2023 * DOI: https://doi.org/10.1038/s41581-023-00730-z SHARE THIS ARTICLE Anyone you share the following link with will be able to read this


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