There was an error published in Development 137, .
In Fig. 2D, owing to the PPH-6 film being inadvertently flipped during scanning, the two lanes labelled as input instead showed flowthrough. A revised Fig. 2 with the correct input samples in D is shown below. In addition, a note has been added to the end of the legend to clarify the lack of GFP-SAPS-1 signal in these input lanes.
PPH-6 and SAPS-1 associate in vivo. (A) Western blot analysis using PPH-6 antibodies on wild-type or pph-6(RNAi) embryonic extracts. The blot was reprobed with α-tubulin antibodies as a loading control (bottom). Note the presence of two species, with the lower one exhibiting the predicted molecular weight of PPH-6 (∼37 kDa). Note also that the ratio between these two species varies among extracts (compare A with inputs in C). Similar variability is observed for SAPS-1 (B,C). The variation might be due to differences in the developmental stages of the embryos in the different preparations. (B) Western blot analysis of wild-type or saps-1(RNAi) embryonic extracts probed with SAPS-1 antibodies. Note presence of two major specific species, exhibiting the predicted molecular weight of the splice variants of SAPS-1 (∼80 kDa and 87 kDa). A non-specific band (NS) served as a loading control. (C) Coimmunoprecipitation from wild-type, pph-6(RNAi) or saps-1(RNAi) embryonic extracts using PPH-6 antibodies. Western blots were probed with antibodies against PPH-6, SAPS-1 or α-tubulin, as indicated. In the second row, the input is exposed 10 times longer than the IP. Input/IP=1:50. In three independent experiments, we observed that PPH-6 antibodies retrieved more PPH-6 from the saps-1(RNAi) extract than from the pph-6(RNAi) extract, despite similar depletion levels of PPH-6. Perhaps PPH-6 not bound to SAPS-1 is more accessible to PPH-6 antibodies. (D) Extract from embryos expressing GFP-SAPS-1 or from wild-type embryos immunoprecipitated with GFP antibodies and analyzed by western blot with GFP or PPH-6 antibodies, as indicated. Note that only the PPH-6 species with the lower molecular weight co-immunoprecipitates with GFP-SAPS-1. Input/IP=1:50 (overall levels of GFP-SAPS-1 protein in the embryonic lysates are low, hence the lack of detection of GFP-SAPS-1 in the input lanes).
PPH-6 and SAPS-1 associate in vivo. (A) Western blot analysis using PPH-6 antibodies on wild-type or pph-6(RNAi) embryonic extracts. The blot was reprobed with α-tubulin antibodies as a loading control (bottom). Note the presence of two species, with the lower one exhibiting the predicted molecular weight of PPH-6 (∼37 kDa). Note also that the ratio between these two species varies among extracts (compare A with inputs in C). Similar variability is observed for SAPS-1 (B,C). The variation might be due to differences in the developmental stages of the embryos in the different preparations. (B) Western blot analysis of wild-type or saps-1(RNAi) embryonic extracts probed with SAPS-1 antibodies. Note presence of two major specific species, exhibiting the predicted molecular weight of the splice variants of SAPS-1 (∼80 kDa and 87 kDa). A non-specific band (NS) served as a loading control. (C) Coimmunoprecipitation from wild-type, pph-6(RNAi) or saps-1(RNAi) embryonic extracts using PPH-6 antibodies. Western blots were probed with antibodies against PPH-6, SAPS-1 or α-tubulin, as indicated. In the second row, the input is exposed 10 times longer than the IP. Input/IP=1:50. In three independent experiments, we observed that PPH-6 antibodies retrieved more PPH-6 from the saps-1(RNAi) extract than from the pph-6(RNAi) extract, despite similar depletion levels of PPH-6. Perhaps PPH-6 not bound to SAPS-1 is more accessible to PPH-6 antibodies. (D) Extract from embryos expressing GFP-SAPS-1 or from wild-type embryos immunoprecipitated with GFP antibodies and analyzed by western blot with GFP or PPH-6 antibodies, as indicated. Note that only the PPH-6 species with the lower molecular weight co-immunoprecipitates with GFP-SAPS-1. Input/IP=1:50 (overall levels of GFP-SAPS-1 protein in the embryonic lysates are low, hence the lack of detection of GFP-SAPS-1 in the input lanes).
This error does not affect the conclusions of this experiment or of the paper. The authors apologise to readers for this mistake.
