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At 20 °C, the atx-3 and cdc-48.2 knockouts presented uncoordination levels similar to wild-type. Cdc-48.1 mutants had a slight increase in uncoordination at this temperature (p = 0.016) ( Fig. 2B). Surprisingly, at 25 °C, the atx-3 and cdc-48.1 mutants displayed 60% and 45% of uncoordination, respectively, while cdc-48.2 animals behave similarly to N2 ( Fig. 2C). The observed phenotypes for atx-3 and cdc-48.1 were temperature-dependent, since the atx-3 PF-01367338 is only manifested at 25 °C while the cdc-48.1 motility phenotype significantly increased with the temperature. This can indicate that at 25 °C these two proteins are more required, probably to exert a role in the UPP, known to be more active at higher temperatures.
The two CDC-48 proteins are highly similar and functionally redundant at least during development, as CDC-48 double knockouts are not viable while single knockouts are [21]. However, in the motility assay, only CDC-48.1 displayed a phenotype, suggesting that in this pathway the two proteins are not redundant. These results were not so surprising as the clearly different expression patterns of the two CDC-48 proteins strongly supports different biological roles [13]. In fact, and although both CDC-48 proteins are highly expressed in muscle cells, only cdc-48.1 loss of function was shown to suppress unc-45 motility defects, indicating that CDC-48.1 functions in the muscle to control UNC-45 activity, a chaperone essential for myosin assembly and correct muscle formation [20].