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. 2019 Jun 25;14(6):e0218203. doi: 10.1371/journal.pone.0218203

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© 2019 Williams et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 3 — (A) Model of the domain structure of LRIM1/APL1C (LRIM1 only, magenta) indicating the location of C-terminal truncations CC1 and CC2. A schematic diagram of LRIM1-FLAG/APL1C-Δ26-130-6×His construct and coiled-coil domain constructs CC1 and CC2, coiled-coil shown in green, cysteines as red bars, N-linked glycosylation site as yellow ball, 6×His tag in blue. (B) α6×His Western blot of supernatant (supe) and αFLAG immunoprecipitate (IP) of TEP1*S1-K969C/Y1275C seven days post-cleavage. The first sample is wt TEP1*S1 immediately following cleavage. Both uncleaved and cleaved TEP1 remain in the supernatatant and do not co-immunoprecipitate with LRIM1/APL1C. (C) αTEP1 Western blot of precipitate (p) and soluble (s) fractions for TEP1*S1 full-length (TEP1-F) and cleaved form (TEP1-C) after 24 h incubation with LRIM1/APL1C-CC1 and LRIM1/APL1C-CC2.