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Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
KTH, Skolan för teknik och hälsa (STH), Medicinsk teknik, Strukturell bioteknik.
Vise andre og tillknytning
2017 (engelsk)Inngår i: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, artikkel-id 2081Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

. Protein misfolding and aggregation is increasingly being recognized as a cause of disease. In Alzheimer's disease the amyloid-beta peptide (A beta) misfolds into neurotoxic oligomers and assembles into amyloid fibrils. The Bri2 protein associated with Familial British and Danish dementias contains a BRICHOS domain, which reduces A beta fibrillization as well as neurotoxicity in vitro and in a Drosophila model, but also rescues proteins from irreversible nonfibrillar aggregation. How these different activities are mediated is not known. Here we show that Bri2 BRICHOS monomers potently prevent neuronal network toxicity of A beta, while dimers strongly suppress A beta fibril formation. The dimers assemble into high-molecular-weight oligomers with an apparent two-fold symmetry, which are efficient inhibitors of non-fibrillar protein aggregation. These results indicate that Bri2 BRICHOS affects qualitatively different aspects of protein misfolding and toxicity via different quaternary structures, suggesting a means to generate molecular chaperone diversity.

sted, utgiver, år, opplag, sider
Nature Publishing Group, 2017. Vol. 8, artikkel-id 2081
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URN: urn:nbn:se:kth:diva-220596DOI: 10.1038/s41467-017-02056-4ISI: 000417702300032PubMedID: 29234026Scopus ID: 2-s2.0-85037854373OAI: oai:DiVA.org:kth-220596DiVA, id: diva2:1174802
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QC 20180116

Tilgjengelig fra: 2018-01-16 Laget: 2018-01-16 Sist oppdatert: 2018-01-16bibliografisk kontrollert

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Nilsson, Harriet E.Koeck, Philip J. B.
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