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. 2017 Sep 13;2(5):e00248-17. doi: 10.1128/mSphere.00248-17

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Copyright © 2017 Krtková et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 7 — S330 and S338 of Gl-actin contribute to 14-3-3 complex formation. (A) Model of Gl-actin showing the positions of S330 and S338 in an actin monomer. (B) Multiplexed immunoblot of total Giardia extracts after Phos-tag phosphate-affinity electrophoresis comparing phosphorylation of TS-actin and TS-actin^{S330A S338A}; anti-Gl-actin (green), StrepTactin-HRP (blue), and anti-HA (red). Note equal loading as indicated by 14-3-3 levels. (C) Samples from panel B were overloaded and probed with anti-Gl-actin antibody. Colored asterisks mark specific P-actin bands: note that only two bands are visible in the TS-actin^{S330A S338A} double mutant. (D) Affinity pulldown of TS-actin variants blotted for Gl-actin and 14-3-3–HA. (E) Quantification of three independent affinity pulldown experiments shows S330 and S338 contribute to 14-3-3 association. *, P < 0.05; **, P < 0.01; ***, P < 0.001.