PRISMA: Protein Interaction Screen on Peptide Matrix reveals interaction footprints and modifications- dependent interactome of intrinsically disordered C/EBPb

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.; Leutz, A.

PRISMA: Protein Interaction Screen on Peptide Matrix reveals interaction footprints and modifications- dependent interactome of intrinsically disordered C/EBPb

Tools

Preview

PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
11MB

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

Repository Staff Only: item control page

Download Statistics

Downloads

Downloads per month over past year