Fig. 1: ANXA11 is a structurally bipartite protein capable of biomolecular condensation and lipid binding. | Nature Communications

Fig. 1: ANXA11 is a structurally bipartite protein capable of biomolecular condensation and lipid binding.

From: ANXA11 biomolecular condensates facilitate protein-lipid phase coupling on lysosomal membranes

Fig. 1

a A schematic of full length (FL) ANXA11 binding to lysosomal membranes, illustrating the Ca2+-dependent annexin repeat domain (ARD) association with PI(3)P, and the cytosolic-facing low complexity domain (LCD). b Fluorescence micrographs of recombinant AF647-labelled FL (aa 1-502), LCD (aa 1-185) and ARD (aa 186–502) ANXA11 at varying protein concentrations. Scale bar –5 µm. Representative images repeated in three independent experiments (c) Representative fluorescence images of ATTO488 GUVs incubated with 0.5 µM AF555-labelled ANXA11 FL, LCD and ARD in the presence or absence of 500 µM Ca2+. Scale bar –5 µm. d Quantification of the fluorescence intensity of AF555-labelled FL, LCD and ARD recruited to GUVs as shown in (c) at varying Ca2+ concentrations. Mean ± SD. Kruskal-Wallis test with Dunn’s multiple comparison, ***p = 0.0002, ****p < 0.0001, ns - not significant (p > 0.05), n = 3 repeats (110-379 GUVs).

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