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. 2016 Jun 15;5:e15460. doi: 10.7554/eLife.15460

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© 2016, Panayiotou et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

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Figure 7. — Cells expressing MRTF-A derivatives, with or without RafER, were treated as indicated and their subcellular localisation was scored by immunofluorescence. (A) Summary of MRTF-A NES predictions and NES-inactivating deletions and point mutations (see also Figure 7—figure supplement 1A). (B–E) MRTF-A NES elements functionally cooperate with each other (B,C) and with N-terminal phosphorylations (D,E) to maintain cytoplasmic localisation of full-length MRTF-A. Data in panels D and E are from the same experiment. Data are mean ± half-range n = 2 (B,D,E) or mean ± SEM, n =3 (C). (B) NES1 cooperates with the C-terminal NES elements. Nuclear accumulation is enhanced by inactivation of NES1 (p<0.001), NES2 (p<0.001) or NES5/6 (p<0.05); inactivation of NES1 enhances the effect of inactivating NES2 and NES5/6 (p<0.001); one-way ANOVA with Bonferroni multiple comparison test. (C) Inactivation of NES5/6 significantly enhances effect of NES1/2/4 inactivation (p<0.001); one-way ANOVA with Bonferroni multiple comparison test. (D) Effect of alanine substitution at S33 is similar to NES1 inactivation. S33A enhances the effect of inactivation of NES2 (p<0.05) or NES2+4 (p<0.001), and is not significantly different from NES1 inactivation; NES1 inactivation enhances inactivation of NES2+NES4 (p<0.001); one-way ANOVA with Bonferroni multiple comparison test. (E) The S98D phosphomimetic mutation cooperates with inactivation of NES2 (p<0.01) and NES2+4 (p<0.001). One-way ANOVA, Bonferroni's multiple comparison test.

DOI: http://dx.doi.org/10.7554/eLife.15460.016

Figure 7—figure supplement 1. — Cells expressing MRTF-A derivatives, with or without RafER, were treated as indicated and their subcellular localisation was scored by immunofluorescence. (A) Summary of MRTF-A NES predictions and NES-inactivating deletions and point mutations (see also Figure 7—figure supplement 1A). (B–E) MRTF-A NES elements functionally cooperate with each other (B,C) and with N-terminal phosphorylations (D,E) to maintain cytoplasmic localisation of full-length MRTF-A. Data in panels D and E are from the same experiment. Data are mean ± half-range n = 2 (B,D,E) or mean ± SEM, n =3 (C). (B) NES1 cooperates with the C-terminal NES elements. Nuclear accumulation is enhanced by inactivation of NES1 (p<0.001), NES2 (p<0.001) or NES5/6 (p<0.05); inactivation of NES1 enhances the effect of inactivating NES2 and NES5/6 (p<0.001); one-way ANOVA with Bonferroni multiple comparison test. (C) Inactivation of NES5/6 significantly enhances effect of NES1/2/4 inactivation (p<0.001); one-way ANOVA with Bonferroni multiple comparison test. (D) Effect of alanine substitution at S33 is similar to NES1 inactivation. S33A enhances the effect of inactivation of NES2 (p<0.05) or NES2+4 (p<0.001), and is not significantly different from NES1 inactivation; NES1 inactivation enhances inactivation of NES2+NES4 (p<0.001); one-way ANOVA with Bonferroni multiple comparison test. (E) The S98D phosphomimetic mutation cooperates with inactivation of NES2 (p<0.01) and NES2+4 (p<0.001). One-way ANOVA, Bonferroni's multiple comparison test.

DOI: http://dx.doi.org/10.7554/eLife.15460.016