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000599937 1001_ $$aReichelt, Julia$$b0
000599937 245__ $$aNon-functional ubiquitin C-terminal hydrolase L1 drives podocyte injury through impairing proteasomes in autoimmune glomerulonephritis
000599937 260__ $$aLondon$$bNature Publishing Group UK$$c2023
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000599937 500__ $$aThe authors would like to thank Antonio Virgillio Failla from the UMIF,UKE and Roland Thuenauer from the ALFM, CSSB, DESY for technicalassistance in super resolution microscopy.
000599937 520__ $$aLittle is known about the mechanistic significance of the ubiquitin proteasome system (UPS) in a kidney autoimmune environment. In membranous nephropathy (MN), autoantibodies target podocytes of the glomerular filter resulting in proteinuria. Converging biochemical, structural, mouse pathomechanistic, and clinical information we report that the deubiquitinase Ubiquitin C-terminal hydrolase L1 (UCH-L1) is induced by oxidative stress in podocytes and is directly involved in proteasome substrate accumulation. Mechanistically, this toxic gain-of-function is mediated by non-functional UCH-L1, which interacts with and thereby impairs proteasomes. In experimental MN, UCH-L1 becomes non-functional and MN patients with poor outcome exhibit autoantibodies with preferential reactivity to non-functional UCH-L1. Podocyte-specific deletion of UCH-L1 protects from experimental MN, whereas overexpression of non-functional UCH-L1 impairs podocyte proteostasis and drives injury in mice. In conclusion, the UPS is pathomechanistically linked to podocyte disease by aberrant proteasomal interactions of non-functional UCH-L1.
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000599937 7001_ $$aSachs, Wiebke$$b1
000599937 7001_ $$aFrömbling, Sarah$$b2
000599937 7001_ $$aFehlert, Julia$$b3
000599937 7001_ $$aStudencka-Turski, Maja$$b4
000599937 7001_ $$aBetz, Anna$$b5
000599937 7001_ $$00000-0003-0827-149X$$aLoreth, Desiree$$b6
000599937 7001_ $$00000-0003-1889-0470$$aBlume, Lukas$$b7
000599937 7001_ $$0P:(DE-H253)PIP1085705$$aWitt, Susanne$$b8
000599937 7001_ $$aPohl, Sandra$$b9
000599937 7001_ $$aBrand, Johannes$$b10
000599937 7001_ $$aCzesla, Maire$$b11
000599937 7001_ $$0P:(DE-H253)PIP1032213$$aKnop, Jan$$b12
000599937 7001_ $$aFlorea, Bogdan I.$$b13
000599937 7001_ $$aZielinski, Stephanie$$b14
000599937 7001_ $$aSachs, Marlies$$b15
000599937 7001_ $$aHoxha, Elion$$b16
000599937 7001_ $$aHermans-Borgmeyer, Irm$$b17
000599937 7001_ $$aZahner, Gunther$$b18
000599937 7001_ $$00000-0003-4053-1474$$aWiech, Thorsten$$b19
000599937 7001_ $$00000-0002-2551-242X$$aKrüger, Elke$$b20
000599937 7001_ $$0P:(DE-HGF)0$$aMeyer-Schwesinger, Catherine$$b21$$eCorresponding author
000599937 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-023-37836-8$$gVol. 14, no. 1, p. 2114$$n1$$p2114$$tNature Communications$$v14$$x2041-1723$$y2023
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