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Deciphering cell signaling networks through innovative proteomics.

Global mapping of the endogenous DNA damage repair networks identifies Shieldin as a novel protein complex in DNA damage repair.

Gupta R et al. Cell. 2018 May 3.[Pubmed]

Using a novel proteomic approach we reveal a comprehensive map of protein interaction of key DNA damage repair proteins. We show that the novel protein complex shieldin is an essential downstream effector of 53BP1 in regulating NHEJ, antibody class-switching and sensitivity to PARP inhibitors. Identification of Shieldin provides new insights into the evolution of vertebrate-specific DDR pathways with key relevance for understanding antibody diversification and PARP inhibitor resistance.

Time-resolved analysis reveals rapid dynamics and broad Scope of the CBP/p300 acetylome.

Weinert BT, Narita T et al. Cell. 2018 May 14. [Pubmed]

By combining quantitative proteomics with specific CBP/p300 catalytic inhibitors, bromodomain inhibitors, and genetic knockout cells, we reveal a comprehensive map of regulated acetylation sites and their dynamic turnover rates. CBP/p300 regulates a much larger number of acetylation sites than known previously, and CBP/p300-catalyzed rapid acetylation is essential for gene transcription. The entire resource dataset is freely accessible at:

A fully-funded postdoc position is available in the Group.

We offer exciting scientific environment and cutting-edge technologies for identifying and investigating novel regulatory mechanisms of cell signaling. More details about the position can be found here.

Interested candidates can also directly contact Chuna Choudhary:


The Choudhary Laboratory is a research group consisting of 10 international researchers with diverse academic background and expertise in biochemistry, cell signaling, genome editing, and quantitative mass spectrometry.

The Group is interested in systematically deciphering the code of cellular communication system (cell signaling networks) by applying innovative proteomic, genomic, and cell biological technologies.

We are located at the Novo Nordisk Foundation Center for Protein Research (CPR), Faculty of Health and Medical Sciences, University of Copenhagen.



A major focus of the Group is to obtain novel understanding of the regulatory mechanisms in cell signaling through `systems-wide` investigations of signaling networks. In particular, we are interested in unraveling the properties and the regulatory landscape of posttranslational modifications (PTMs) in signaling networks. PTMs have crucial roles in the dynamic regulation of protein activity, stability, spatial localization, and communication with other macromolecules within cells. PTMs are directly relevant for human health as dysregulation of PTM-regulating enzymes, such as protein kinases, ubiquitin ligases, and lysine deacetylases, is frequently associated with human disease.

Our laboratory applies cutting-edge mass spectrometry-based proteomic technologies for unbiased, global, and quantitative analysis of key regulatory PTMs, such as lysine acetylation and ubiquitylation. The laboratory has state-of-the-art facilities for work related to cell biology, biochemistry, and genome editing, and has access to in-house infrastructure and expertise for live cell imaging, flow cytometry, the next generation nucleic acid sequencing, and protein biophysical analyses. The unique combination of the Group´s expertise and collaboration with leading researchers from Denmark and around the world distinctively positions the group to investigate the functional relevance of PTMs in diverse biological contexts.


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