Fig. 4: Exploring interaction networks prone to perturbation by oncoviral PBMs in host cell models by AP-MS. | Nature Communications

Fig. 4: Exploring interaction networks prone to perturbation by oncoviral PBMs in host cell models by AP-MS.

From: Quantitative fragmentomics allow affinity mapping of interactomes

Fig. 4

A Identification, from extracts of indicated cell lines, of PDZ-containing prey proteins retained by HPV E6 and HTLV1 Tax1 PBM baits. Results of comparable studies by Strickland et al.39 (*) Thomas et al.38 (**) and Al-Saleem et al.40 (***) are also provided. For each PDZ-protein identified, the number of PDZ domains and the presence or absence of PDZ-oligomerization L27 domains are indicated at the bottom of the table. The four prey proteins containing the 6 PDZ domains that we selected as baits for the next round of AP-MS experiments are highlighted in gray. B Identification, from indicated cell extracts, of PBM-containing prey proteins retained by the 6 PDZ domains selected in A. The ten top prey proteins of the list belong to the oncoviral-like human PBM clade revealed by our quantitative fragmental interactome. Interaction partners in A and B were found by comparing the prey quantities compared to a control resin. Binding threshold was defined at >2-fold enrichment and <0.01 P value, calculated by two-tailed unpaired T-test. Blue cells indicate detectable interaction between the immobilized bait (minimal binding fragment) and the endogenous prey (full-length protein). Note that only interaction partners containing PDZ domains or C-terminal PBMs are indicated. For a comprehensive list of all identified interaction partners, see Supplementary Data 2.

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