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. 2010 Feb 1;5(2):e8981. doi: 10.1371/journal.pone.0008981

Figure 2. Lrig1 and Lrig3 bind to and co-localize with ErbB receptor tyrosine kinases in vitro.

Figure 2

(A) Like Lrig1, Lrig3 can co-immunoprecipitate with multiple ErbB receptors in HEK293T cells. Lysates were immunoprecipitated with anti-flag antibodies and blotted with anti-ErbB (top) and anti-flag (bottom) antibodies. Both Lrig1-flag and Lrig3-flag can bind to EGFR (left), ErbB2 (middle), and ErbB4 (right) in the absence (−) or presence (+) of ligand (EGF or NRG). No ErbB receptors were precipitated in the absence of epitope-tagged Lrig (vector). Western blotting confirms the presence of each ErbB receptor (ErbB), and epitope-tagged Lrig family member (flag) in total lysates (bottom). Actin was used as a loading control. (B–D) Flag and ErbB4 immunocytochemistry on HEK293T cells transfected with ErbB4, Lrig1-flag, and/or Lrig3-flag alone (B) or in combinations (C,D). When expressed on their own, Lrig1, Lrig3 and ErbB4 are detected at the cell surface (B). When either Lrig1 (C) or Lrig3 (D) is expressed in combination with ErbB4, the proteins co-localize in intracellular compartments (arrowheads in C and D).