Figure S5.
SMA-1Δ11SR, but not SMA-1ΔPH, results in larger and more frequent ruptures of cyk-1(RNAi) rings that resemble those induced by SMA-1 loss. (A) Anti-SMA-1 immunoblot of adult worm lysates showing protein levels in wild-type, sma-1ΔPH and sma-1Δ11SR animals. α-tubulin serves as the loading control. (B) Kymographs of the peripheral ring arc in ABa cells, generated as indicated in Fig. 7 B′. First time point corresponds to the first frame when the ring perimeter is 60 µm. Gray bars indicate the period of time during which the rings constrict from a perimeter of 50–10 µm. Arrows point at large ruptures. (C) Number of perimeter changes larger than zero, +2, +4, and +6 µm, observed in a total of 11 rings for each condition. (D) Images of control, sma-1Δ11SR and sma-1(ru18) ring constriction in four-cell embryos co-expressing SPC-1::GFP and NMY-2::mKate2. Localization of SPC-1::GFP is normal in sma-1Δ11SR embryos and is lost in sma-1(ru18) embryos. (E) Total number of embryos laid (brood size) and total number of embryos that hatched (embryonic viability). n is the number of adult animals whose progeny was analyzed (n = 9 in control, n = 9 in unc-44(RNAi), n = 9 in cyk-1(RNAi), and n = 10 in cyk-1(RNAi);unc-44(RNAi)). Colors as in panel F. (F) Ring constriction rate of ABa/p rings (mean ±95% CI). n is the number of contractile rings analyzed (n = 9 in control, n = 9 in unc-44(RNAi), n = 8 in cyk-1(RNAi), and n = 10 in cyk-1(RNAi);unc-44(RNAi)). (G) Images of ABa rings from embryos co-expressing LifeAct::GFP and NMY-2::mCherry. In E and F, statistical significance was determined using unpaired one-way ANOVA followed by Bonferroni’s multiple comparison test. ****P < 0.0001; ns, not significant, P ≥ 0.05. Scale bars in D, 10 µm; in B and G, 5 µm. Source data are available for this figure: SourceData FS5.

SMA-1Δ11SR, but not SMA-1ΔPH, results in larger and more frequent ruptures of cyk-1(RNAi) rings that resemble those induced by SMA-1 loss. (A) Anti-SMA-1 immunoblot of adult worm lysates showing protein levels in wild-type, sma-1ΔPH and sma-1Δ11SR animals. α-tubulin serves as the loading control. (B) Kymographs of the peripheral ring arc in ABa cells, generated as indicated in Fig. 7 B′. First time point corresponds to the first frame when the ring perimeter is 60 µm. Gray bars indicate the period of time during which the rings constrict from a perimeter of 50–10 µm. Arrows point at large ruptures. (C) Number of perimeter changes larger than zero, +2, +4, and +6 µm, observed in a total of 11 rings for each condition. (D) Images of control, sma-1Δ11SR and sma-1(ru18) ring constriction in four-cell embryos co-expressing SPC-1::GFP and NMY-2::mKate2. Localization of SPC-1::GFP is normal in sma-1Δ11SR embryos and is lost in sma-1(ru18) embryos. (E) Total number of embryos laid (brood size) and total number of embryos that hatched (embryonic viability). n is the number of adult animals whose progeny was analyzed (n = 9 in control, n = 9 in unc-44(RNAi), n = 9 in cyk-1(RNAi), and n = 10 in cyk-1(RNAi);unc-44(RNAi)). Colors as in panel F. (F) Ring constriction rate of ABa/p rings (mean ±95% CI). n is the number of contractile rings analyzed (n = 9 in control, n = 9 in unc-44(RNAi), n = 8 in cyk-1(RNAi), and n = 10 in cyk-1(RNAi);unc-44(RNAi)). (G) Images of ABa rings from embryos co-expressing LifeAct::GFP and NMY-2::mCherry. In E and F, statistical significance was determined using unpaired one-way ANOVA followed by Bonferroni’s multiple comparison test. ****P < 0.0001; ns, not significant, P ≥ 0.05. Scale bars in D, 10 µm; in B and G, 5 µm. Source data are available for this figure: SourceData FS5.

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