Proteomics

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The HSP40 chaperone Ydj1/DnaJA1 drives amyloid beta toxicity

ABSTRACT: Amyloid beta 42 (Abeta42) is the principal trigger of neurodegeneration during Alzheimer’s disease (AD); however, the etiology of Abeta42 toxicity remains elusive. In a proteomic approach using a yeast model for intracellular Abeta42 toxicity, we here identify the HSP40 family member Ydj1, the yeast orthologue of human DnaJA1, as a crucial factor in Abeta42-mediated toxicity.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Joern Dengjel  

LAB HEAD: Joern Dengjel

PROVIDER: PXD012612 | Pride | 2022-04-27

REPOSITORIES: Pride

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The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity.

Ring Julia J   Tadic Jelena J   Ristic Selena S   Poglitsch Michael M   Bergmann Martina M   Radic Nemanja N   Mossmann Dirk D   Liang YongTian Y   Maglione Marta M   Jerkovic Andrea A   Hajiraissi Roozbeh R   Hanke Marcel M   Küttner Victoria V   Wolinski Heimo H   Zimmermann Andreas A   Domuz Trifunović Lana L   Mikolasch Leonie L   Moretti Daiana N DN   Broeskamp Filomena F   Westermayer Julia J   Abraham Claudia C   Schauer Simon S   Dammbrueck Christopher C   Hofer Sebastian J SJ   Abdellatif Mahmoud M   Grundmeier Guido G   Kroemer Guido G   Braun Ralf J RJ   Hansen Niklas N   Sommer Cornelia C   Ninkovic Mirjana M   Seba Sandra S   Rockenfeller Patrick P   Vögtle Friederike-Nora FN   Dengjel Jörn J   Meisinger Chris C   Keller Adrian A   Sigrist Stephan J SJ   Eisenberg Tobias T   Madeo Frank F  

EMBO molecular medicine 20220404 5

Amyloid beta 42 (Abeta42) is the principal trigger of neurodegeneration during Alzheimer's disease (AD). However, the etiology of its noxious cellular effects remains elusive. In a combinatory genetic and proteomic approach using a yeast model to study aspects of intracellular Abeta42 toxicity, we here identify the HSP40 family member Ydj1, the yeast orthologue of human DnaJA1, as a crucial factor in Abeta42-mediated cell death. We demonstrate that Ydj1/DnaJA1 physically interacts with Abeta42 (  ...[more]

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