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. 2018 Aug 30;293(43):16583–16595. doi: 10.1074/jbc.RA118.004478

Figure 4.

Figure 4.

The N- and C-terminal halves of Ptch2 bind to but do not complement the activity of the reciprocal halves of Ptch1. A, stick diagram depicting the amino acid boundaries of the Ptch2 constructs. Amino acid numbering refers to the sequence of mPtch2. B, straight Western blots detecting transient expression of the N- and C-terminal portions of Ptch1 and Ptch2 in lysates from HEK293 cells. C, from left to right, co-immunoprecipitation of mycPtch2-C with FLAGPtch2-N (lane 2), mycPtch2-C with Ptch1-N (lane 4), and FLAGPtch2-N with Ptch1-CHA (lane 6). Both halves of Ptch2 noncovalently interact with the reciprocal halves of Ptch1. D, Ptch1-deficient MEFs were transiently transfected with an 8×Gli-luciferase construct, a constitutively expressing Renilla luciferase construct, and constructs expressing Ptch1 or Ptch2 halves individually or together. Neither half of Ptch2 is capable of complementing the respective half of Ptch1 to restore Smo-repressing activity, nor does full-length Ptch2 repress the Hh pathway. **, p < 0.01.