Chaperone-assisted Protein Folding in Health and Disease

Event Details

Type

Friday Lecture Series

Speaker(s)

F. Ulrich Hartl, Ph.D., director and professor, department of cellular biochemistry, Max Planck Institute of Biochemistry

Speaker bio(s)

Our understanding of cellular protein folding has changed over the past two decades. While the three-dimensional structures of functional proteins are determined by their amino acid sequences, we now know that newly-synthesized polypeptides depend on molecular chaperone proteins to reach their folded states efficiently and at a biologically relevant time scale. Members of different chaperone classes act to prevent protein misfolding and aggregation, often in an ATP-dependent mechanism. Once folded, many proteins continue to require chaperone surveillance, especially under conditions of cell stress. Failure of the chaperone machinery to maintain proteostasis, i.e. the conformational integrity of the cellular proteome, facilitates the manifestation of diseases associated with toxic protein aggregation, including Alzheimer’s, Parkinson’s, and Huntington’s disease.

After receiving an M.D. and a doctorate in biochemistry from Heidelberg University in 1985, F. Ulrich Hartl worked with Walter Neupert in Munich and William Wickner at UCLA on intracellular protein transport. In 1991 he joined the faculty of Sloan-Kettering Institute in New York where he was tenured in 1993 and made HHMI investigator in 1994. Since 1997 he has been a director at Max Planck Institute of Biochemistry in Martinsried near Munich. Hartl’s research focuses on the role of molecular chaperones in protein folding and the mechanisms of diseases associated with protein aggregation. He has received several international prizes, including the Gairdner International Award, the Lasker Basic Medical Award, the Shaw Prize and the Breakthrough Prize in Lifesciences.

FLS lectures will take place in Caspary Auditorium and virtually via Zoom. We recommend virtual participants log out of VPN prior to logging in to Zoom. Please do not share the link or post on social media. This talk will be recorded for the RU community.

Open to

Tri-Institutional