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. Author manuscript; available in PMC: 2012 Mar 1.

Published in final edited form as: Biochim Biophys Acta. 2010 Dec 29;1813(3):480–491. doi: 10.1016/j.bbamcr.2010.12.017

Fig. 5 — Representative blots of co-immunoprecipitations demonstrating interactions of full-length ErbB4 (190kDa) and its intracellular domain (80kDa) with (A) PSEN-1 and (B) YAP were studied in unstimulated (NRG−) and NRG-stimulated (NRG+, 5 minutes) E17 fetal type II cells, using co-immunoprecipitation conditions. Protein interactions were analyzed by Western blotting. The left two lanes show the cell lysates, the middle two lanes show the specific PSEN-1 and YAP immunoprecipitations and the right two lanes show unstimulated cell lysates and immunoprecipitations using anti-mouse-IgG (negative control for PSEN-1) and anti-rabbit-IgG (negative control for YAP). Blots of PSEN-1 co-immunoprecipitation and IgG co-immunoprecipitations were probed with anti-phospho-tyrosine, anti-ErbB4, anti-phospho-PSEN-1, and anti-PSEN-1 antibodies. PSEN-1 co-precipitated full-length ErbB4 and its intracellular fragment. This interaction was increased by NRG-stimulation. NRG induced phosphorylation of both ErbB4 and PSEN-1. Blots of YAP co-immunoprecipitation and IgG co-immunoprecipitations were reprobed with anti-phospho-tyrosine, anti-ErbB4, anti-phospho-YAP, and anti-YAP antibodies. YAP co-precipitated full-length ErbB4 and its intracellular fragment in fetal type II cells. This interaction was increased by NRG-stimulation. NRG induced phosphorylation of both ErbB4 and YAP. Quantitative data for the YAP co-immunoprecipitations are given in the text. Neither IgG co-immunoprecipitations (Figure 5A and B) pulled down any of the proteins.

Fig. 5 — Representative blots of co-immunoprecipitations demonstrating interactions of full-length ErbB4 (190kDa) and its intracellular domain (80kDa) with (A) PSEN-1 and (B) YAP were studied in unstimulated (NRG−) and NRG-stimulated (NRG+, 5 minutes) E17 fetal type II cells, using co-immunoprecipitation conditions. Protein interactions were analyzed by Western blotting. The left two lanes show the cell lysates, the middle two lanes show the specific PSEN-1 and YAP immunoprecipitations and the right two lanes show unstimulated cell lysates and immunoprecipitations using anti-mouse-IgG (negative control for PSEN-1) and anti-rabbit-IgG (negative control for YAP). Blots of PSEN-1 co-immunoprecipitation and IgG co-immunoprecipitations were probed with anti-phospho-tyrosine, anti-ErbB4, anti-phospho-PSEN-1, and anti-PSEN-1 antibodies. PSEN-1 co-precipitated full-length ErbB4 and its intracellular fragment. This interaction was increased by NRG-stimulation. NRG induced phosphorylation of both ErbB4 and PSEN-1. Blots of YAP co-immunoprecipitation and IgG co-immunoprecipitations were reprobed with anti-phospho-tyrosine, anti-ErbB4, anti-phospho-YAP, and anti-YAP antibodies. YAP co-precipitated full-length ErbB4 and its intracellular fragment in fetal type II cells. This interaction was increased by NRG-stimulation. NRG induced phosphorylation of both ErbB4 and YAP. Quantitative data for the YAP co-immunoprecipitations are given in the text. Neither IgG co-immunoprecipitations (Figure 5A and B) pulled down any of the proteins.