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POSTPONED – Knowing right from wrong (protein conformation): the challenging choices of (molecular) chaperones

Wednesday, June 17, 2020 - 3:00pm to 4:00pm

Speaker

Judith Frydman, Ph.D.
Professor
Donald Kennedy Chair in Humanities and Sciences, Department of Biology and Genetics
Stanford University

Summary

Judith Frydman is a professor in the Departments of Biology and Genetics at Stanford University. She is originally from Argentina, where she majored in Chemistry and received her PhD in Biochemistry from the University of Buenos Aires. She carried out her postdoctoral training with Ulrich Hartl at the Sloan Kettering Institute in New York, where she had two major contributions to the field of cellular protein folding. First, she discovered that eukaryotic cells have a ring-shaped chaperonin complex, which was termed TRiC and secondly, she established that, unlike what was previously believed based on biophysical experiments, protein folding in in eukaryotic cells occurs cotranslationally as polypeptides emerge from ribosomes during their biosynthesis. Importantly, she showed that distinct molecular chaperones are specifically recruited to bind ribosome-nascent chain complexes to assist cotranslational folding. These fundamental discoveries have shaped current thinking of protein folding in vivo.

Her independent research at Stanford University has established many key principles of cellular protein folding and homeostasis. Her group discovered that distinct protein homeostasis networks mediate cotranslational folding and protein quality control: A network of Chaperones Linked to Protein Synthesis (CLIPS) function in the context of translation to assist in cotranslational protein folding and quality control. A distinct stress inducible chaperone network protects cells from proteotoxic stress. In recent year, Frydman made important contributions defining the management of misfolded and aggregation-prone proteins. Her group discovered that cells rely on chaperone-dependent spatial sequestration in specific cellular compartments to protect and repair their proteome. She also defined chaperone-dependent pathways that cooperate with specific sets of ubiquitin ligases to promote misfolded protein clearance. The insights her work provides on biological mechanisms controlling cellular protein folding, aggregation and quality control have important implications for the study of aging, neurodegenerative diseases and other misfolding-linked maladies and enable strategies for the treatment of infectious disease and neurodegenerative diseases.


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