Professor Chuna Ram Choudhary
Professor, Group Leader, Proteomics Program
Novo Nordisk Foundation Center for Protein Research
University of Copenhagen, Denmark

Date: Wednesday, 29-May-2019
Time: 3:00 p.m.
Venue: Seminar Room 1, G/F, Laboratory Block
Faculty of Medicine Building, 21 Sassoon Road, Pokfulam, Hong Kong

Summary:
The eukaryotic cell signaling system is shaped by two major mechanisms: protein-protein interactions (PPIs) and posttranslational modifications (PTMs). Indeed, these mechanisms provide the ‘first line response’ to virtually all environmental and internal signals in a cell and form the heart of eukaryotic cellular communication system. The dynamic PPIs and PTMs vastly expand the functional complexity of the proteome. Because these mechanisms impact all proteins and processes in cell, a systematic analysis of PPIs and PTMs is fundamental for understanding the regulatory principles in biology. Professor Choudhary’s group use quantitative mass spectrometry to reveal the global scope, mechanisms and dynamics of lysine acetylation. Their latest findings reveal that metazoan-specific acetyltransferase CBP/p300-catalyzed rapid acetylation is an essential regulator of cell-type-specific gene transcription. In another work, they combined quantitative mass spectrometry with proximity biotinylation to obtain a detailed protein-protein interaction map of endogenous DNA repair networks. These analyses discovered the novel protein complex shieldin that protects DNA double-strand breaks and promotes DNA repair by non-homologous end joining. Higher-vertebrate-specific shieldin is required for antibody diversification as well as for clinical sensitivity of BRCA1-deficient tumors to PARP inhibitor therapy.

Organized by:

• School of Biomedical Sciences
• School of Public Health
• HKU-Pasteur Research Pole
• Proteomics and Metabolomics Core Facility

ALL ARE WELCOME