Fig. 7: Vangl2 forms a complex with PTK7 in a tyrosine phosphorylation-dependent manner. | Nature Communications

Fig. 7: Vangl2 forms a complex with PTK7 in a tyrosine phosphorylation-dependent manner.

From: FGF receptor modulates planar cell polarity in the neuroectoderm via Vangl2 tyrosine phosphorylation

Fig. 7: Vangl2 forms a complex with PTK7 in a tyrosine phosphorylation-dependent manner.The alt text for this image may have been generated using AI.

A, B Vangl2-PTK7 binding is enhanced by non-phosphorylated Vangl2 and reduced by phosphorylated Vangl2. Four-to-eight-cell Xenopus embryos were injected with RNAs encoding HA-Vangl2, HA-Vangl2 Y7Y10Y12 > F (Y > F) or HA-Vangl2 Y7Y10Y12 > E (Y > E) (40 pg each) as indicated, with or without PTK7-GFP RNA, 100 pg, into four animal blastomeres. Embryos were collected at stage 12 and PTK7-GFP (A) or HA-Vangl2 (B) were immunoprecipitated using GFP-trap or anti-HA antibody, respectively, to assess co-precipitated Vangl2 (A) or PTK7 (B). Protein levels in pull-downs and lysates were analyzed with anti-GFP and anti-HA antibodies. Irrelevant part of the membrane was removed (A). Data are representative of three experiments.

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