4.8 Article

Human transcription factor protein interaction networks

Journal

NATURE COMMUNICATIONS
Volume 13, Issue 1, Pages -

Publisher

NATURE PORTFOLIO
DOI: 10.1038/s41467-022-28341-5

Keywords

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Funding

  1. Academy of Finland [288475, 294173]
  2. University of Helsinki Three-year Research Grant
  3. Academy of Finland (AKA) [294173, 288475, 294173, 288475] Funding Source: Academy of Finland (AKA)

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This study identifies protein-protein interactions for 109 different human transcription factors using BioID and AP-MS analyses, resulting in a rich resource of TF interactions. The analysis reveals the transient and dynamic nature of TF interactions and identifies subgroups of TFs associated with specific biological functions. Additionally, uncharacterized cross-talk between NFI signaling and other TF signaling pathways is observed.
Transcription factors (TFs) interact with several other proteins in the process of transcriptional regulation. Here the authors identify 6703 and 1536 protein-protein interactions for 109 different human TFs through BioID and AP-MS analyses, respectively. 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.

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