Dr Andy Howden; University of Dundee
In this talk I will summarise my recent work mapping the activated B cell proteome. Using high resolution quantitative mass spectrometry I have explored how immune activation and the metabolic checkpoint kinase mTORC1 (mammalian target of rapamycin complex 1) regulate the proteome of B lymphocytes to control B cell differentiation. Triggering the B cell receptor in combination with co-stimulatory signals and cytokines induces considerable re-modelling of the B cell protein landscape. I reveal that mTORC1 activity is critical for the expression of transcription factors that regulate B cell differentiation and metabolism, including aryl hydrocarbon receptor (AHR) and MYC. Inhibiting mTORC1 activity also impairs the expression of nutrient and amino acid transporters. This work provides a detailed map of naïve and immune activated B cell proteomes, and a resource for exploring and understanding the cellular machinery that direct B cell phenotypes.
My research uses quantitative proteomics and protein biochemistry to provide new molecular understanding into how immune cells sense and respond to their environment and regulate core cellular processes. I completed my degree, PhD and postdoc positions in plant science (in Edinburgh, California, Oxford and Dundee), but in 2015 I moved fields to use my proteomics background to explore how immune cells respond to stimulation and stress. I have an active interest in how immune cell dysfunction is linked to neurodegenerative disease and I’m currently using quantitative mass spectrometry to map immune cells in Parkinson’s and Alzheimer’s disease for biomarker discovery and disease phenotyping. I’ve recently been appointed as a group leader (commencing November 2023) within the Division of Cell Signalling and Immunology at the University of Dundee.
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