Protein aggregation is an important aspect of normal animal development

What is it about?

Protein aggregation, once believed to be a harbinger and/or consequence of stress, age, and pathological conditions, is emerging as a novel concept in cellular regulation. Normal versus pathological aggregation may be distinguished by the capacity of cells to regulate the formation, modification, and dissolution of aggregates. We find that aggregates are observed in large cells/blastomeres (oocytes, embryos) and in smaller, further differentiated cells (primordial germ cells) in worms (C. elegans). These observations are consistent with the hypothesis that aggregates are involved in normal development.

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Why is it important?

Amyloids have primarily been studied in fully developed or in aging tissue. In this study, we ask whether the presence of amyloids in oocytes as seen in Xenopus (Hayes and Weeks, 2016) is a ubiquitous feature of early animal development, and if so, whether they are crucial to a successful developmental program, and finally, what function(s) they may carry out. Using cross-platform analysis in Saccharomyces cerevisiae, C. elegans, and Xenopus laevis, we present studies identifying a novel disaggregase family encoded by animal genomes and expressed embryonically. Our initial analysis of yeast Arb1/Abcf2 in disaggregation and animal ABCF proteins in embryogenesis is consistent with the possibility that members of the ABCF gene family may encode disaggregases needed for aggregate processing during the earliest stages of animal development.