2008 Rosenstiel Award announced

Award goes to pioneering researchers in neurodegenerative disease

The 2008 Rosenstiel Award in biomedical sciences was awarded today to two pioneers in the field of protein-mediated protein folding, Arthur L. Horwich and Franz-Ulrich Hartl. They were chosen for their elucidation of the molecular machinery that guides proteins into their proper functional shape, thereby preventing the accumulation of protein aggregates that underlie many diseases, such as Alzheimer's and Parkinson's.

“This award honors two remarkable pioneers who solved one of the most fundamental problems in protein biochemistry: how newly synthesized proteins can be properly folded up into a very specific shape that is required for them to work as enzymes or as structural elements of the cell,” said Jim Haber, Abraham and Etta Goodman Professor of Biology and Director, Rosenstiel Basic Medical Sciences Research Center. “It has become increasingly evident that failures in protein folding and assembly underlie many human neurological disorders.” 

Dr. Horwich is the Eugene Higgins Professor of Cellular and Molecular Physiology at the Yale University School of Medicine, and Investigator, Howard Hughes Medical Institute.  Dr. Hartl is Director at the Max Planck Institute of Biochemistry, in Martinsried, Germany.

Dr. Horwich received his undergraduate and medical degrees from Brown University, then trained in pediatric medicine at Yale. A Yale faculty member in genetics starting in 1984, he examined the mitochondrial "machinery" that posttranslationally imports precursor proteins and, in a genetic screen in yeast, uncovered Hsp60 (the yeast homologue of GroEL) as essential for folding newly imported proteins in work in collaboration with Dr. Hartl.

This led to further studies of chaperones in structure and mechanism using the bacterial GroEL-GroES system, including X-ray crystallographic studies with Paul Sigler, cryoEM studies with Helen Saibil, and NMR studies with Kurt Wüthrich. Currently he is Sterling Professor of Genetics and Investigator of the Howard Hughes Medical Institute.
Ulrich Hartl studied medicine at Heidelberg University. After receiving his M.D. in 1982 and his doctoral degree in biochemistry in 1985 he began working on the mechanism of protein transport into mitochondria. In 1988 he initiated the work on molecular chaperones and demonstrated, together with Dr. Horwich and another colleague, the basic role of chaperones in assisting protein folding.

In the nineties while working at Sloan Kettering Cancer Center in New York, Dr. Hartl investigated the mechanisms of protein folding in the bacterial and eukaryotic cytosol. He reconstituted the pathway of chaperone-assisted folding in which the Hsp70 and the GroEL chaperone systems cooperate and discovered that GroEL and its co-factor GroES provide a nano-cage for single protein molecules to fold unimpaired by aggregation.

In 1994 he became an Investigator of the Howard Hughes Medical Institute and in 1997 Dr. Hartl returned to Munich to head the Department of Cellular Biochemistry at the Max Planck Institute of Biochemistry (MPIB). Dr. Hartl continues to investigate the mechanisms of cellular protein folding using a range of methods from cell biology, biochemistry and structural biology. In addition, he initiated research into neurodegenerative diseases caused by protein misfolding and aggregation. This work led to the finding that chaperones can effectively inhibit the formation of amyloid aggregates associated with neurodegeneration. Much of this work was done in collaboration with Manajit Hayer-Hartl.

“There is now great interest in developing new therapies based on the knowledge that has been provided by Drs. Hartl and Horwich and other scientists inspired by their work,” said Dr. Haber.

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