RPTOR BioID2 reveals spatial association between mTORC1 and FAs. (A) Network representation of RPTOR BioID2 dataset. Proteins identified include well-known regulators of mTORC1 (protein complexes shown in green boxes), autophagy, and protein translation (black dashed boxes; see Table S1 for a full list). ND, not detected in the proteomics dataset. Thick blue node border indicates BioID2-RPTOR. Edges (red lines) indicate reported physical protein–protein interactions. (B) Gene Ontology overrepresentation enrichment analyses of proteins identified by RPTOR BioID2. Molecular functions enriched with P < 10−3 and cellular components enriched with P < 10−5 are shown (hypergeometric tests with Benjamini–Hochberg correction; 5% FDR threshold). Bar color represents enrichment ratio of overrepresented terms. NTP, nucleoside triphosphatase. (C) Network representation of consensus adhesome proteins identified in the RPTOR BioID2 dataset. Edges (red lines) indicate reported physical protein–protein interactions. The largest interconnected subnetwork is shown. (D) Proportion of RPTOR-proximal proteins in the meta-adhesome database, including the consensus adhesome (Horton et al., 2015; number of identified proteins indicated in parentheses). Segments are labeled with respective coverage of the meta-adhesome, consensus adhesome, and literature-curated adhesome (Winograd-Katz et al., 2014) by RPTOR-proximal proteins. See also Table S1. (E) Identification of 10 proteins significantly enriched in the RPTOR BioID2 dataset that were also identified in published BioID datasets of the FA proteins paxillin and kindlin-2 in U2OS cells (Dong et al., 2016).
