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000646209 1001_ $$0P:(DE-HGF)0$$aLarsson, Johan N. K.$$b0
000646209 245__ $$aHeat shock protein 10 as a chaperone modulating α‐synuclein amyloid fibril formation
000646209 260__ $$aHoboken, NJ$$bWiley$$c2026
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000646209 520__ $$aHSP10 is a well-known human co-chaperone that interacts with HSP60 to comprise the HSP60/10 chaperonin complex which upholds mitochondrial proteostasis. HSP10 also demonstrates independent roles in binding to misfolded proteins and interacts with several amyloidogenic client proteins. Using a variety of biophysical and biochemical methods, we studied the interactions of HSP10 with the amyloidogenic protein α-synuclein (α-syn) associated with Parkinson's disease. HSP10 efficiently inhibited fibril formation of wild type (WT) and disease-mutant A30P α-syn at sufficient concentrations of chaperone by both binding to α-syn monomers and by blocking secondary nucleation on fibril surfaces. However, under sub-stoichiometric conditions, below 1:5 (HSP10:α-syn), the chaperone sequestered multiple A30P α-syn monomers and thereby promoted nucleation of fibril formation with a magnitude comparable to the efficacy of seeding with preformed fibrils. The fibril formation acceleration effect of the HSP10 chaperone was client-specific as it was observed for A30P but not WT α-syn. Our results broaden the scope of HSP10 chaperone activity and can have implications for disease onset in synucleinopathies.
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000646209 7001_ $$aKumar, Ranjeet$$b1
000646209 7001_ $$00009-0006-1755-1388$$aBuratti, Fiamma Ayelen$$b2
000646209 7001_ $$00000-0002-4303-4783$$aNyström, Sofie$$b3
000646209 7001_ $$00000-0003-1058-1964$$aWittung-Stafshede, Pernilla$$b4
000646209 7001_ $$0P:(DE-H253)PIP1091750$$aHammarstrom, Per$$b5$$eCorresponding author
000646209 773__ $$0PERI:(DE-600)2000025-X$$a10.1002/pro.70452$$gVol. 35, no. 2, p. e70452$$n2$$pe70452$$tProtein science$$v35$$x0961-8368$$y2026
000646209 8564_ $$uhttps://onlinelibrary.wiley.com/doi/full/10.1002/pro.70452
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