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Biology subjects

Payne, N. L.

Publications and source records attributed to Payne, N. L..

2 recordsLinked to original sources

Heating tolerance of ectotherms is explained by temperature's non-linear influence on biological rates

The capacity of ectotherms to adjust their thermal tolerance limits through evolution or acclimation seems relatively modest and highly variable, and we lack satisfying explanations for both findings given a limited understanding of what ultimately determines an organisms thermal tolerance. Here, we test if the amount of heating an ectotherm tolerates throughout a heating event until organismal failure scales with temperatures non-linear influence on biological rates. To account for the non-linear influence of temperature on biological rates on heating tolerance, we rescaled the duration of heating events of 316 ectothermic taxa acclimated to different temperatures and describe the biological rate-corrected heating duration. This rescaling reveals that the capacity of an organism to resist a heating event is in fact remarkably constant across any acclimation temperature, enabling high-precision estimates of how organismal thermal tolerance limits vary under different thermal regimes. We also find that faster heating consistently reduces biological rate-corrected heating durations, which helps further explain why thermal tolerance limits seem so variable on absolute temperature scales. Existing paradigms are that heating tolerances and thermal tolerance limits reflect incomplete metabolic compensatory responses, are constrained by evolutionary conservatism, or index failure of systems such as membrane function; our data provide a different perspective and show that an organisms thermal tolerance emerges from the interaction between the non-linear thermal dependence of biological rates and heating durations, which is an approximately-fixed property of a species.

ecology↗

Cellular aging impedes stress-activation of a crucial JDP-Hsp70 protein disaggregase

The collapse of protein homeostasis manifests itself in a toxic protein aggregation cascade, which is associated with degenerative diseases and aging. To solubilize aggregates, dedicated protein disaggregases exist in unicellular organisms, but these have no nuclear/cytosolic orthologs in metazoa. Alternative metazoan disaggregation machines have been described, but how these are operated and regulated in vivo remained unknown. We show that protein disaggregases are functionally diversified in human cells to efficiently target different types of stress-induced aggregates in sequential and temporally distinct phases. In particular, we show the selective assembly of an Hsp70-DNAJA1-DNAJB1 trimeric disaggregase that forms during late phase of stress recovery., i.e., after VCP-dependent solubilization of non-native proteins that accumulate in cellular condensates such as nucleoli or stress granules. When activated, the trimeric disaggregase provides resistance to stress toxicity and contributes to amyloid disposal. Strikingly, this disaggregase collapses early in cells undergoing replicative aging with important underlining pathophysiological consequences.

cell biology↗