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[Preprint]. 2023 Jun 16:rs.3.rs-3026818. [Version 1] doi: 10.21203/rs.3.rs-3026818/v1

Fig. 3. VPS35L bridges VPS26C and VPS29 through conserved surfaces.

Fig. 3.

(A-D) Interaction surface of VPS35L with VPS29 (A-B) and VPS26C (C-D). The binding surface is colored based on conservation score using the same scheme shown in Fig. 2. Contacting residues are shown as sticks. Yellow dashed lines indicate polar interactions. For clarity, the backbones of VPS29 and VPS26C in (B) and (D) are shown as loops. (E) Mutation rates (%) for VPS35L and VPS35 across multiple tumor types. (F) Overall structural model of Retriever showing the location of cancer-associated mutations on the surface of VPS35L. Residues mutated in this study are outlined with a black box. For clarity, VPS29 and VPS26 are shown as ribbons. (G-H) Immunoprecipitation of VPS35L (G) or VPS29 (H) carrying indicated point mutations expressed in HEK293T cells. Interactions with various components of Retriever and CCC were assessed by immunoblotting.