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. 2023 Dec 13;9(50):eadj1205. doi: 10.1126/sciadv.adj1205

Fig. 8. N-terminal conserved domain of TMEM55B facilitates the binding of RILPL1.

Fig. 8.

(A) Domain structure of full-length and truncated mutants of TMEM55B used here. (B) HEK293 cells were transiently transfected with the indicated proteins and lysed 24 hours after transfection. Halo-TMEM55B immunoprecipitations (top) or cell extracts (bottom) were subjected to quantitative immunoblot analysis using the LI-COR Odyssey CLx Western blot imaging system and indicated antibodies. Quantitation of immunoblotting data (performed using ImageStudioLite software version 5.2.5, RRID:SCR_013715) is shown as mean ± SEM. (C) Analysis of C-terminal residue conservation of TMEM55B using the ConSurf motif software (81) and conservation score scale. (D) Key residues that are involved in the interaction between TMEM55B and RILPL1 were analyzed by AlphaFold2 model of TMEM55B (80 to 160) and RIPL1 (389 to 403). (E) As in (B).