Membrane Curvature Sensing by Amphipathic Helices Is Modulated by the Surrounding Protein Backbone
Fig 3
Reducing its hydrophobicity does not increase membrane curvature sensitivity of Nup133 ALPS motif.
(A) Amino-acid sequence of the ALPS motif of Nup133. The strongest hydrophobic region is highlighted in yellow, and the secondary region is framed in red. The hydrophobic residues mutated in this study are indicated by arrows. (B) L252 in GFP133 was mutated to less hydrophobic residues, namely Valine, Alanine and Glycine. (C) F263 in GFP133 was mutated to less hydrophobic residues, namely Valine, Alanine and Glycine. Scale bars are 10μm. (D) Normalized GLCM contrasts, as an indication of membrane-bound fractions, were measured in peripheral regions of cells transfected with the indicated constructs. Horizontal bars represent median values.