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. Author manuscript; available in PMC: 2022 Feb 19.
Published in final edited form as: Cell. 2022 Jan 20;185(4):712–728.e14. doi: 10.1016/j.cell.2021.12.041

Figure 2. Subcellular and subprotein domain Tau interactome in living human neurons identified by APEX-mediated biotinylation.

Figure 2.

(A) Workflow for proximity-dependent identification of Tau-associated proteins.

(B) Venn diagram of biotinylated proteins detected in human neurons with N-APEX Tau (n = 7 cultures), C-APEX Tau (n = 9 cultures), or APEX-α Tubulin (n = 12 cultures). See also Table S1.

(C) N-APEX Tau, C-APEX Tau, and APEX-α Tubulin biotinylated proteins include components of the microtubule cytoskeleton. Only interconnected nodes based on the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) database are shown. Function pathway analyses categories are grouped by color.

(D) ClueGO molecular function pathway enrichment of proteins biotinylated by both N-APEX Tau and C-APEX Tau but not APEX-α Tubulin. Node colors denote functionally grouped networks (kappa connectivity score ≥ 30%).

(E) Gene Set Enrichment Analysis (GSEA) on proteins biotinylated by both N-APEX and C-APEX Tau showing major cellular component categories.

(F and G) ClueGO biological processes pathway enrichment of proteins biotinylated only by N-APEX Tau (F) and only by C-APEX Tau (G).

(H and I) Subprotein-level APEX Tau associations identified that regulate autophagy (H) and proteasome degradation (I).