John Yates III

Professor
Molecular Science, neuromedicine.
Scripps Research Institute

A PTM Code for Membrane Protein Maturation

Abstract

A component to understanding biological processes involves identifying the proteins expressed in cells as well as their modifications and the dynamics of processes. This process has benefited from the sequencing of genomes, although this information is not uncovered from DNA sequencing. Mass spectrometry together with informatic tools can uncover the type of modification and it’s a location in a peptide sequence.  Advances in multi-dimensional separations as well as mass spectrometry have improved the scale of experiments for protein identification. This has improved the analysis of protein complexes, and more complicated protein mixtures. Quantitative mass spectrometry has also helped to determine the role of modifications in regulating biological processes. Using the loss of function mutant form of the Cystic Fibrosis Transport Regulator (DF508) as it progresses through the folding pathway as a model to understand the regulation of protein maturation, we have discovered a post translational modification code that regulates the maturation of CFTR. This has provided a better understanding of the loss of function associated with mutation. We are now exploring if this code is general for membrane protein maturation

Biosketch

John Yates III is professor at the department of Molecular Medicine & Neuroscience from the Scripps Research Institute. After completing his Ph.D. at University of Virginia he joined the California Institute of Technology as a research fellow before accepting a position of associate professor at the Department of Molecular Biotechnology of University of Washington. He move to the Scripps Research Institute professor at the department of Cell biology and Chemical physiology. He also held the positions of director of Director of Protein and Metabolite Dynamics, Torrey Mesa Research Institute and Senior Research Fellow at Diversa, Inc. Dr. John Yates develops and applies proteomics tools for analyzing extremely complex protein mixtures, studying host-pathogen interactions in diseases such as malaria, and finding post-translational modifications to the proteins within these same complex mixtures. He received several awards for his contributions including the Pehr Edman Award, the Biemann Medal, ASMS Blue Ribbon, the HUPO distinguished achievement award in proteomics, and the Christian B. Anfinsen Award.

Date
Date(s) - May 13, 2019
6:00 pm - 9:00 pm

Emplacement / Location
Pavillon Roger Gaudry (M-415)