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. Author manuscript; available in PMC: 2018 May 30.
Published in final edited form as: Nature. 2017 Nov 22;551(7682):629–633. doi: 10.1038/nature24620

Extended Data Figure 6. Proteasome involvement in germline proteostasis.

Extended Data Figure 6

a, LysoTracker-stained dissected germlines. b, GFP::PBS-1 localization. c, d, Schematic and imaging of proteasome sensor UbG76V::GFP. Active proteasomes degrade UbG76V::GFP, unless inhibited by MG132. e–g, GFP::RHO-1-aggregation following control or proteasomal pbs-1 RNAi. The gld-1(q485) mutation precluded aggregation following pbs-1 RNAi. This finding fits the model that the proteasome degrades GLD-1, but not the aggregates, consistent with aggregate engulfment by lysosomes. However, we note that proximal gld-1 germ cells, which form tumors20, could potentially be non-permissive for aggregation. Mean ± s.d. from three biological replicates, each of n = 50 animals. ****P < 0.0001. Bars, 10 µm.