Autophagy machinery promotes the chaperone-mediated formation and compartmentalization of protein aggregates during appressorium development by the rice blast fungus.

ABSTRACT: The chaperone-mediated sequestration of misfolded proteins into specialized quality control compartments represents an important strategy for maintaining protein homeostasis in response to stress. However, precisely how this process is controlled in time and subcellular space and integrated with the cell's protein refolding and degradation pathways remains unclear. We set out to understand how aggregated proteins are managed during infection-related development by a globally devastating plant pathogenic fungus and to determine how impaired protein quality control impacts cellular differentiation and pathogenesis in this system. Here we show that in the absence of Hsp104 disaggregase activity, aggregated proteins are spatially sequestered into quality control compartments within conidia, bu

SUBMITTER: Rogers AM 

PROVIDER: S-EPMC7851963 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature