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Research

Transcellular Stress Signaling in the Regulation of Organismal Proteostasis during Stress and Protein Conformational Diseases
 

Our lab is interested how components of the proteostasis network (PN) - such as molecular chaperones - maintain the integrity of the proteome in the face of stress, aging and human protein misfolding diseases.

Using a C. elegans Alzheimer’s Disease model, our lab has recently shown that activation of Hsp90 expression via Transcellular Chaperone Signalling prevents the formation of toxic amyloid protein deposits in the animal throughout aging (O’Brien et al, Cell Reports 2018).

Transcellular Chaperone Signalling is a novel concept in biology (van Oosten-Hawle et al, Cell 2013) that allows the activation of protective chaperone expression in tissues affected by aggregation-prone disease proteins via neuronal signalling pathways or signals mediated by the gut.

Our lab uses the power of C. elegans as a tractable genetic model system for human neurodegenerative diseases in combination with genomic approaches and the strength of biochemistry, structural biology and Cryo-EM.