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| Item Type: | Article |
|---|---|
| Title: | PRISMA: Protein Interaction Screen on Peptide Matrix reveals interaction footprints and modifications- dependent interactome of intrinsically disordered C/EBPb |
| Creators Name: | Dittmar, G., Perez Hernandez, D., Kowenz-Leutz, E., Kirchner, M., Kahlert, G., Wesolowski, R., Baum, K., Knoblich, M., Hofstätter, M., Muller, A., Wolf, J., Reimer, U. and Leutz, A. |
| Abstract: | CCAAT enhancer binding protein beta (C/EBPβ) is a pioneer transcription factor that specifies cell differentiation. C/EBPβ is intrinsically unstructured, a molecular feature common to many proteins involved in signal processing and epigenetics. The structure of C/EBPβ differs depending on alternative translation initiation and multiple post-translational modifications (PTM). Mutation of distinct PTM sites in C/EBPβ alters protein interactions and cell differentiation, suggesting a C/EBPβ PTM indexing code determines epigenetic outcomes. Herein, we systematically explored the interactome of C/EBPβ using an array technique based on spot-synthesized C/EBPβ-derived linear tiling peptides with and without PTM, combined with mass spectrometric proteomic analysis of protein interactions (PRISMA). We identified interaction footprints of ∼1300 proteins in nuclear extracts, many with chromatin modifying, remodeling and RNA processing functions. The results suggest C/EBPβ acts as a multi-tasking molecular switchboard, integrating signal-dependent modifications and structural plasticity to orchestrate interactions with numerous protein complexes directing cell fate and function. |
| Keywords: | C/EBPβ, PRISMA, Intrinsically Disordered Protein, Post-Translational Modification, Mass Spectrometry |
| Source: | iScience |
| ISSN: | 2589-0042 |
| Publisher: | Cell Press |
| Volume: | 13 |
| Page Range: | 351-370 |
| Date: | 29 March 2019 |
| Official Publication: | https://doi.org/10.1016/j.isci.2019.02.026 |
| PubMed: | View item in PubMed |
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