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024 7 _ |a 10.1002/pro.70452
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100 1 _ |a Larsson, Johan N. K.
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245 _ _ |a Heat shock protein 10 as a chaperone modulating α‐synuclein amyloid fibril formation
260 _ _ |a Hoboken, NJ
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520 _ _ |a HSP10 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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700 1 _ |a Kumar, Ranjeet
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700 1 _ |a Buratti, Fiamma Ayelen
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700 1 _ |a Nyström, Sofie
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700 1 _ |a Wittung-Stafshede, Pernilla
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700 1 _ |a Hammarstrom, Per
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773 _ _ |a 10.1002/pro.70452
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856 4 _ |u https://onlinelibrary.wiley.com/doi/full/10.1002/pro.70452
856 4 _ |u https://bib-pubdb1.desy.de/record/646209/files/Protein%20Science%20-%202026%20-%20Larsson%20-%20Heat%20shock%20protein%2010%20as%20a%20chaperone%20modulating%20%E2%80%90synuclein%20amyloid%20fibril%20formation.pdf
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