Chronic temperature stress inhibits reproduction and disrupts endocytosis via chaperone titration in Caenorhabditis elegans
| Autor: | Rosemary N Plagens, Eric Guisbert, Isiah Mossiah, Karen S. Kim Guisbert |
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| Rok vydání: | 2021 |
| Předmět: |
QH301-705.5
Physiology Endocytic cycle Plant Science Biology Endocytosis General Biochemistry Genetics and Molecular Biology Structural Biology Chaperones Animals Chronic stress HSP70 Heat-Shock Proteins Biology (General) Heat shock Caenorhabditis elegans Caenorhabditis elegans Proteins Transcription factor Ecology Evolution Behavior and Systematics Ecosystem Heat shock response Trafficking Reproduction Temperature Cell Biology biology.organism_classification Hsp70 Cell biology Chaperone (protein) biology.protein General Agricultural and Biological Sciences Developmental Biology Biotechnology Molecular Chaperones Research Article |
| Zdroj: | BMC Biology BMC Biology, Vol 19, Iss 1, Pp 1-14 (2021) |
| ISSN: | 1741-7007 |
| Popis: | BackgroundTemperature influences biology at all levels, from altering rates of biochemical reactions to determining sustainability of entire ecosystems. Although extended exposure to elevated temperatures influences organismal phenotypes important for human health, agriculture, and ecology, the molecular mechanisms that drive these responses remain largely unexplored. Prolonged, mild temperature stress (48 h at 28 °C) has been shown to inhibit reproduction inCaenorhabditis eleganswithout significantly impacting motility or viability.ResultsAnalysis of molecular responses to chronic stress using RNA-seq uncovers dramatic effects on the transcriptome that are fundamentally distinct from the well-characterized, acute heat shock response (HSR). While a large portion of the genome is differentially expressed ≥ 4-fold after 48 h at 28 °C, the only major class of oogenesis-associated genes affected is the vitellogenin gene family that encodes for yolk proteins (YPs). Whereas YP mRNAs decrease, the proteins accumulate and mislocalize in the pseudocoelomic space as early as 6 h, well before reproduction declines. A trafficking defect in a second, unrelated fluorescent reporter and a decrease in pre-synaptic neuronal signaling indicate that the YP mislocalization is caused by a generalized defect in endocytosis. Molecular chaperones are involved in both endocytosis and refolding damaged proteins. Decreasing levels of the major HSP70 chaperone, HSP-1, causes similar YP trafficking defects in the absence of stress. Conversely, increasing chaperone levels through overexpression of the transcription factor HSF-1 rescues YP trafficking and restores neuronal signaling.ConclusionsThese data implicate chaperone titration during chronic stress as a molecular mechanism contributing to endocytic defects that influence multiple aspects of organismal physiology. Notably, HSF-1 overexpression improves recovery of viable offspring after exposure to stress. These findings provide important molecular insights into understanding organismal responses to temperature stress as well as phenotypes associated with chronic protein misfolding. |
| Databáze: | OpenAIRE |
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