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. 2023 Feb 22;11:1105657. doi: 10.3389/fcell.2023.1105657

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Copyright © 2023 Radhakrishnan, Leung, Solanki and Lobo.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Cellular localization and expression of WT-RBPR2 and RBPR2-mutants.(A) Transient expression and staining of mouse V5-tagged WT-RBPR2 and variants in NIH3T3 cells using the V5-antibody. Nucleus, DAPI, blue; RBPR2-V5, Green. Scale bar = 50 μm. (B) Protein expression and representative western blot images of WT-RBPR2 and RBPR2-mutant proteins, which affect the “SYL” domain; anti-Actin = protein loading control. (C) Subcellular fractionation of stable cells expressing WT-RBPR2 or individual RBPR2-RBP4 mutants. Stable NIH3T3/LRAT cells expressing either WT-RBPR2 or individual RBPR2-RBP4 binding residues mutants were fractionated as outlined in the methods. Normalized portions of each extract (∼30 μg) were analyzed by Western blotting using antibodies against proteins from cytoplasmic (HSP90) and plasma membrane (EGFR).