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Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
Published on: November 11, 2014
Failure in heat-shock protein expression in response to UBB+1 protein in progressive supranuclear palsy in humans
Andrew D Hope1, Tammaryn Lashley, Andrew J Lees
1Reta Lila Weston Institute of Neurological Studies, University College London, 46 Cleveland Street, London, W1T 4JF, UK. hope.andrew@mayo.edu
Abstract:
UBB+1 protein is an aberrant ubiquitin associated with progressive supranuclear palsy (PSP). It leads to proteasome inhibition, heat-shock protein (HSP) expression and apoptosis in cell cultures. Despite UBB+1 polyubiquitination (an indication of proteasome inhibition), we demonstrate that UBB+1 and HSP40/HSP70 immunoreactivity do not co-localize in the pons of patients with PSP. As HSPs are involved in both normal tau and proteasome function, these findings may be relevant to the aetiology of PSP and other tauopathies.
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