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Event Details
Description of Event
Washington University School of Medicine
The Garcia lab is interested in the development and application of quantitative mass spectrometry based proteomics for understanding dynamic proteome and protein post-translational modifications. In particular, we are interested in understanding combinatorial histone PTMs and their role in regulating gene expression.
{"start": "2024-06-12T18:00:00", "end": "2024-06-12T19:00:00"} bagarcia@wustl.edu
https://videocast.nih.gov/watch=51137
Histones are small proteins that package DNA into chromosomes, and a large number of studies have showed that several post-translational modification (PTM) sites on the histones are associated with both gene activation and silencing. Along with DNA and small non-coding RNA, histone PTMs make up epigenetic mechanisms that control gene expression patterns outside of DNA sequence mutations. Dysregulation of these chromatin networks underlie several human diseases such as cancer. Here I will give an update on technology advancements that have allowed for high-throughput quantitative mass spectrometry analyses of histone PTMs and chromatin structure, and how we are applying these methods to understand epigenetic reprogramming found in malignant peripheral nerve sheath tumors (MPNSTs). MPNST is an aggressive sarcoma with recurrent loss of function alterations in polycomb-repressive complex 2 (PRC2), a histone-modifying complex involved in transcriptional silencing.
Learning Objectives:
- Learn about how quantitative mass spectrometry can be utilized to characterize histone post-translational modifications
- Learn about histone modifications in human health and disease
- Understand how dysregulated histone modification patterns learn to malignant peripheral nerve sheath tumors.