Proteomic analysis reveals the recruitment of intrinsically disordered regions to stress granules
2019
Heat-stress triggers the formation of condensates known as
stress granules(
SGs), which store non-translating mRNA and stalled translation initiation complexes. To gain a better understanding of
SGs, we identified yeast proteins that sediment after heat-shock by mass spectrometry. Heat-regulated proteins are biased toward a subset of abundant proteins that are significantly enriched in intrinsically disordered regions (IDRs).
SGlocalization of over 80 heat-regulated proteins was confirmed using microscopy, including 32 proteins that were not known previously to localize to
SGs. We find that several IDRs are sufficient to mediate
SGrecruitment. Moreover, the diffusive exchange of IDRs within
SGs, observed via FRAP, can be highly dynamic while other components remain immobile. Lastly, we showed that the IDR of the Ubp3 deubiquitinase is critical for
SGformation. This work confirms that IDRs play an important role in cellular compartmentalization upon stress, can be sufficient for
SGincorporation, can remain dynamic in vitrified
SGs, and play a vital role during heat-stress.
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