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. 2022 Jan 6;39(2):msab371. doi: 10.1093/molbev/msab371

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© The Author(s) 2022. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Fig. 4. — Function of the CNH domain of mNRK and related proteins. (A) Domain architectures of mNRK and related proteins, and sequence similarities of their CNH domains. (B) Intracellular localization of full length (FL) proteins of mNRK, mNIK, mTNIK, mMINK1, and cNRK and their CNH domains. HeLa cells expressing indicated proteins were subjected to immunostaining with anti-FLAG antibody. Scale bar, 10 µm. (C) Profiles of phospholipids that were bound to the CNH domain of mNRK. Left panel, CBB staining of the CNH domain of mNRK and cNRK. Middle panel, phospholipids spotted on the lipid strips. Right panel, lipid overlay assay of the CNH domain of mNRK and cNRK. The data shown are representative of two independent experiments. (D) Effects of the deletion of the CNH domain and the fusion of CaaX motif to mNRK on mNRK localization. HeLa cells expressing indicated proteins were subjected to immunostaining. Scale bar, 10 µm. (E) Their effects of on AKT signaling. HEK293 cells expressing indicated proteins were subjected to immunoblotting, followed by densitometric analyses. The graph shows the mean ± SD of three independent experiments. ***P ≤ 0.001; ****P ≤ 0.0001 (one-way analysis of variance [ANOVA], followed by Dunnett’s multiple comparisons test).