Fig. 5: Mechanism underlying hnRNPC-G3BP1 interaction. | Nature Communications

Fig. 5: Mechanism underlying hnRNPC-G3BP1 interaction.

From: Nanomaterial signatures program biomolecular condensates via triphasic separation for chemoplasticity remodeling

Fig. 5: Mechanism underlying hnRNPC-G3BP1 interaction.

A The binding conformation and contact interface of hnRNPC-NTF2L complex. B Key residues at the hnRNPC-NTF2L interface that make significant contributions to the binding energy (for its definition, please refer to Fig. 4M). C The conformation of the nanomaterial-hnRNPC-NTF2L ternary complex. D Time evolution of the interaction energy and CSA between NTF2L and the hnRNPC adsorbed on nanomaterials. E Immunofluorescence graphs of 60% CLS-AuNPs-treated cells overexpressing wild-type (FL) and truncated (ΔNTF2L) G3BP1 (both pseudo-colored in green) illustrate the susceptibility of G3BP1 towards the nanomaterial-hnRNPC complex. An enlarged view of the marked regions in each group (blue: FL; red: △NTF2L) was reconstructed in 3D as shown on the right side. The cell boundary was highlighted with white dashed lines for better visualization. The distance of G3BP1 to AuNPs-hnRNPC complex (n ≥ 30 cells per group from 3 independent biological replicates) was measured and depicted by a frequency distribution histogram, with a summative schematic provided (inset). Created in BioRender. Huo (2025) https://BioRender.com/hyjh4im. Source data are provided as a Source Data file.

Back to article page