Journal: International Journal of Molecular Sciences

Article Title: Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins

doi: 10.3390/ijms25147672

Figure Lengend Snippet: Domain organization and structure of ERM-proteins. ERM-proteins are composed of an N-terminal FERM-domain that can be further divided into F1-F3 subdomains (green), an α-linker domain (purple) and a C-terminal domain (light purple). The residue numbering corresponds to human ezrin. The C-terminal domain binds F-actin while the FERM-domain binds membrane proteins directly or via adaptor proteins such as NHERF. In the dormant state, the C-terminal domain interacts with FERM thereby masking the actin and membrane protein binding sites (adapted from ).

Article Snippet: The E. coli codon-optimized gene for the human ezrin FERM-domain (residues 1–295) was synthesized (Genscript, Piscataway, NJ, USA) and cloned into pET15b using the NdeI and BamHI sites.

Techniques: Residue, Membrane, Protein Binding

Journal: International Journal of Molecular Sciences

Article Title: Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins

doi: 10.3390/ijms25147672

Figure Lengend Snippet: Domain organization and structure of ERM-proteins. ( a ) Crystal structure of the human ezrin FERM-domain (PDB:1NI2) showing F1–F3 subdomains and ( b ) in complex with interacting peptides from NHERF (black, PDB:2D10) and ICAM-2 (grey, PDB:1J19). ( c ) Crystal structure of the auto-inhibitory complex between Moesin-FERM (green) and the Moesin C-terminal domain (light blue) (PDB:1EF1) showing binding to both binding sites on the F3 subdomain.

Article Snippet: The E. coli codon-optimized gene for the human ezrin FERM-domain (residues 1–295) was synthesized (Genscript, Piscataway, NJ, USA) and cloned into pET15b using the NdeI and BamHI sites.

Techniques: Binding Assay

Journal: International Journal of Molecular Sciences

Article Title: Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins

doi: 10.3390/ijms25147672

Figure Lengend Snippet: MST analysis of the interaction between AQP2/AQP5 and the Ezrin FERM-domain. ( a ) Binding curves for full-length AQP2 (pink circles) and AQP5 (purple triangles). Curve fitting using a one-to-one binding model resulted in a K d of 7.8 ± 3.8 μM (R 2 = 0.94%) for AQP2 and 14 ± 5.7 μM for AQP5 (R 2 = 0.95%). ( b ) Binding curves for AQP2 (pink squares) and AQP5 (purple rhombuses) C-terminal peptides. Curve fitting using a one-to-one binding model resulted in a K d of 8.7 ± 2.4 μM (R 2 = 0.96%) for AQP2 and 2.9 ± 0.89 μM for AQP5 (R 2 = 0.97).

Article Snippet: The E. coli codon-optimized gene for the human ezrin FERM-domain (residues 1–295) was synthesized (Genscript, Piscataway, NJ, USA) and cloned into pET15b using the NdeI and BamHI sites.

Techniques: Binding Assay

Journal: Cell Adhesion & Migration

Article Title: EPB41L family serves as a prognostic biomarker for kidney renal clear cell carcinoma

doi: 10.1080/19336918.2026.2624964

Figure Lengend Snippet: mRNA and protein expression levels of EPB41L2 in KIRC cell lines and tissues. (A) mRNA expression levels of EPB41L2 in KIRC cell lines. (B) EPB41L2 protein expression in KIRC tissues compared to normal renal tubular epithelial tissues. (C) Comparison of EPB41L2 expression between cancerous and adjacent non-cancerous tissues. * p < .05.

Article Snippet: The antibodies used were as follows: rabbit polyclonal EPB41L2 antibody (Abmart, China, Cat No. TP72110S, 1:1000), mouse monoclonal GAPDH antibody (Proteintech, Cat No. 60,004–1-Ig, China, 1:1000), HRP-conjugated goat anti-rabbit secondary antibody (Proteintech, Cat No. SA00001-2, China, 1:5000), and HRP-conjugated goat anti-mouse secondary antibody (Proteintech, Cat No. SA00001-1, China, 1:5000).

Techniques: Expressing, Comparison

Journal: Cell Adhesion & Migration

Article Title: EPB41L family serves as a prognostic biomarker for kidney renal clear cell carcinoma

doi: 10.1080/19336918.2026.2624964

Figure Lengend Snippet: Lentiviral transfection of EPB41L2 in renal clear cell carcinoma cell lines and in vitro cell experiments. (A) the fluorescence transfection status of ACHN and 769-P KIRC cell lines after lentiviral transfection of EPB41L2 was observed for 72 hours. (B-C) After transduction with lentivirus overexpressing EPB41L2, the mRNA and protein expression levels of EPB41L2 in ACHN and 769-P were significantly elevated. (D) the proliferation of ACHN and 769-P cells was assessed by CCK-8 assay following overexpression of EPB41L2. (E) Scratch assay was performed to evaluate the migration of ACHN and 769-P cells overexpressing EPB41L2 for 12 hours. (F) Transwell invasion assay was conducted to investigate the alteration in invasive potential of ACHN and 769-P cells overexpressing EPB41L2. * p < .05, ** p < .01, *** p < .001.

Article Snippet: The antibodies used were as follows: rabbit polyclonal EPB41L2 antibody (Abmart, China, Cat No. TP72110S, 1:1000), mouse monoclonal GAPDH antibody (Proteintech, Cat No. 60,004–1-Ig, China, 1:1000), HRP-conjugated goat anti-rabbit secondary antibody (Proteintech, Cat No. SA00001-2, China, 1:5000), and HRP-conjugated goat anti-mouse secondary antibody (Proteintech, Cat No. SA00001-1, China, 1:5000).

Techniques: Transfection, In Vitro, Fluorescence, Transduction, Expressing, CCK-8 Assay, Over Expression, Wound Healing Assay, Migration, Transwell Invasion Assay

Journal: Theoretical Biology & Medical Modelling

Article Title: Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data

doi: 10.1186/1742-4682-3-17

Figure Lengend Snippet: Characteristics of the three-dimensional structures. Coordinate files were obtained from the Protein Data Bank [20]; 1HCI [28]; 1K8K [49]; 1IZN [61]; 1MIX [83]; 1MIZ [83]; 1QKR [93]; 1TR2 [92]; 1ST6 [94].

Article Snippet: , , FERM domain/Integrin β3 tail fragment (739–743) Complex , Gallus gallus , 200–400 , 1.9 , 0.204 , 1MIZ.

Techniques: