Proximal interaction networks to annotate, predict, and interrogate protein function based upon quantitative mass spectrometry.
The Wright laboratory leverages quantitative mass spectrometry platforms to probe the subcellular composition of protein complexes in preclinical models of human disease. Our goal is to understand the molecular circuitry of cellular signaling to identify the most druggable protein receptors. We focus on either selectively activating latent cell death pathways or facilitating growth arrest through cellular differentiation.
Our approach annotates subcellular protein–protein interactions using proximity-labeling methods coupled with quantitative mass spectrometry.
Constructing proximity interaction networks for key regulators of cellular proliferation, cell death, and cellular differentiation to reveal how protein complexes coordinate cell-fate decisions.
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Developing novel proximity-labeling enzymes to capture post-translational modifications in complex biological matrices, extending the reach of quantitative proteomics into hard-to-study systems.
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Optimizing cell biology reagents and methods to interrogate the molecular function of protein complexes, enabling reproducible, mechanism-level insight into signal-transduction pathways in preclinical models of human prostate cancer.
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We welcome inquiries from prospective graduate students, postdoctoral researchers, and collaborators working at the intersection of proteomics and disease biology.