Structural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved TBM motif

Excel raw files and GraphPad Prism files related to graphs for Figure 1F, Figure 3B and 3D, Figure 3E, Figure 4B-F, Supplementary Figure S3B, Supplementary Figure S5A are presented here. Table of contents: Figure Number Raw File Name GraphPad Prism File Name Description 1F 1F-Graph-Raw-File 1F Bar plots describes the binding of RILPL1 with TMEM55B affected due to the presence of G396L and E398K point mutations. 3B and 3D 3B-3D_Violin-Plots-Raw-File 3B-3D_Violin-Plots Violin plots generated from the mass spectrometry experiment 1 [TMEM55B WT/ LRRK2 Y1699C/ Rab8A Q67L vs TMEM55B R151E/ LRRK2 Y1699C/ Rab8A Q67L] and experiment 2 [TMEM55B WT/ LRRK2 Y1699C/ Rab8A Q67L vs TMEM55B WT/ LRRK2 Y1699C D2017A/ Rab8A Q67L] 3E 3E_Graph-Raw-File 3E Representative graph shows that the interaction of RILPL1 with TMEM55B depends of kinase activity of LRRK2 and the presence of phosphoryted Rabs. 4B to 4F 4B-F_Graph-Raw-File 4B-F Bar plots describes the interaction of TMEM55B with JIP3, JIP4, OCRL, WDR81, and TBC1D9B depends on the TBM. Mutation in this motif at the critical residue disrupts the binding. Supplementary Figure S3B Sup3B_Raw-File Sup3B Bar plot shows that there is an additional interface presents in JIP4 where a mutation K103E of TMEM55B affects the binding of TMEM55B with JIP4 but not RILPL1. Supplementary Figure S5A Sup5A_Raw-File Sup5A Apart from the R151 in TMEM55B, E116 residue is critical for interaction with RILPL1.