Research

Systematic functional mapping of the cysteine proteome

Cysteines belong to the functionally most significant amino acids, owing to their distinct chemical profile and substantial reactivity. Across the human proteome over 260,000 cysteines have been acquired throughout evolution, which facilitate versatile biological functions from catalyzing enzymatic reactions to serving as regulatory nodes via their post-translational modulation. However, the majority of these residues in proteins remain poorly characterized. Advanced proteomic technologies enable deep profiling of the cysteine proteome and modification status but are constrained by our limited understanding of their functional role and relevance, marking a pivotal gap in elucidating cysteine biology. We combine computational and systems-based strategies to understand the functional significance of cysteines and their biological role in health and disease. Leverage this understanding we aim to identify novel functionally significant sites that can be targeted therapeutically.

Redox-control of metabolism in lung cancer

Metabolic reprogramming is a defining feature enabling cancer cells to sustain energy demand and support rapid growth, proliferation, and metastasis. However, the mechanisms through which metabolic adaptation is regulated remain ambiguous, and targeting metabolic proteins pharmacologically has been challenging. A major mode through which metabolic proteins are regulated is post-translational modification of cysteines by redox-active metabolites. We are leveraging mass spectrometry and systems-based strategies to establish the redox regulatory framework that controls metabolism in lung cancer. In deciphering these mechanisms, we aim at unveiling regulatory nodes in lung cancer vulnerabilities that could offer novel therapeutic prospects.

Regulation of mitochondrial Coenzyme Q

Coenzyme Q (CoQ) is a lipophilic electron carrier and antioxidant serving as a central component of mitochondrial energy metabolism and the principal point of contact for diverse metabolic pathways. In addition, the CoQ redox status is an important determinant of mitochondrial reactive oxygen species (ROS) formation, which are now recognized as pleiotropic signaling metabolites. Despite its pivotal role for cellular function the biosynthesis of CoQ and its regulation remain poorly understood. We leverage mass spectrometry and genetic strategies to investigate how cells sense their CoQ levels, how the CoQ biosynthetic pathway is regulated, and how the metabolic cues modulate this process.

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