Human transcription factor protein interaction networks.
Helka GöösMatias KinnunenKari SalokasZenglai TanXiaonan LiuLeena YadavQin ZhangGong-Hong WeiMarkku VarjosaloPublished in: Nature communications (2022)
Transcription factors (TFs) interact with several other proteins in the process of transcriptional regulation. Here, we identify 6703 and 1536 protein-protein interactions for 109 different human TFs through proximity-dependent biotinylation (BioID) and affinity purification mass spectrometry (AP-MS), respectively. The BioID analysis identifies more high-confidence interactions, highlighting the transient and dynamic nature of many of the TF interactions. By performing clustering and correlation analyses, we identify subgroups of TFs associated with specific biological functions, such as RNA splicing or chromatin remodeling. We also observe 202 TF-TF interactions, of which 118 are interactions with nuclear factor 1 (NFI) family members, indicating uncharacterized cross-talk between NFI signaling and other TF signaling pathways. Moreover, TF interactions with basal transcription machinery are mainly observed through TFIID and SAGA complexes. This study provides a rich resource of human TF interactions and also act as a starting point for future studies aimed at understanding TF-mediated transcription.
Keyphrases
- transcription factor
- endothelial cells
- mass spectrometry
- nuclear factor
- induced pluripotent stem cells
- pluripotent stem cells
- dna binding
- toll like receptor
- gene expression
- signaling pathway
- liquid chromatography
- immune response
- oxidative stress
- cell proliferation
- high resolution
- capillary electrophoresis
- inflammatory response
- dna methylation
- pi k akt
- rna seq
- genome wide identification
- cerebral ischemia
- nucleic acid
- amino acid