Hummel, J. | Search bioRxiv

bioRxiv2021

The contrasting shape representations that support object recognition in humans and CNNs

Humans are particularly sensitive to changes in the relationships between parts of objects. It remains unclear why this is. One hypothesis is that relational features are highly diagnostic of object categories and emerge as a result of learning to classify objects. We tested this by analysing the internal representations of supervised convolutional neural networks (CNNs) trained to classify large sets of objects. We found that CNNs do not show the same sensitivity to relational changes as previously observed for human participants. Furthermore, when we precisely controlled the deformations to objects, human behaviour was best predicted by the amount of relational changes while CNNs were equally sensitive to all changes. Even changing the statistics of the learning environment by making relations uniquely diagnostic did not make networks more sensitive to relations in general. Our results show that learning to classify objects is not sufficient for the emergence of human shape representations.

neuroscience↗

bioRxiv2021

Quantitative proteomics identifies the universally conserved ATPase Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae

The universally conserved P-loop ATPase Ola1 is implicated in various cellular stress response pathways, as well as in cancer and tumor progression. However, Ola1p functions are divergent between species and the involved mechanisms are only poorly understood. Here, we studied the role of Ola1p in the heat shock response of the yeast Saccharomyces cerevisiae using a combination of quantitative and pulse labeling-based proteomics approaches, in vitro studies and cell-based assays. Our data show that when heat stress is applied to cells lacking Ola1p, the expression of stress-protective proteins is enhanced. During heat stress Ola1p associates with detergent-resistant protein aggregates and rapidly forms assemblies that localize to stress granules. The assembly of Ola1p was also observed in vitro using purified protein and conditions, which resembled those in living cells. We show that loss of Ola1p results in increased protein ubiquitination of detergent-insoluble aggregates recovered from heat-shocked cells. When subsequently cells lacking Ola1p were relieved from heat stress, reinitiation of translation was delayed, whereas, at the same time, de novo synthesis of central factors required for protein refolding and the clearance of aggregates was enhanced when compared to wildtype cells. The combined data suggest that upon acute heat stress, Ola1p is involved in the stabilization of misfolded proteins, which become sequestered in cytoplasmic stress granules. This function of Ola1p enables cells to resume translation in a timely manner as soon as heat stress is relieved.

cell biology↗