Yale Bulletin and Calendar

October 19, 2007|Volume 36, Number 7

Dr. Arthur Horwich

Horwich appointed to Sterling Professorship

Dr. Arthur Horwich, the newly named Sterling Professor of Genetics and Pediatrics, has conducted research that has fundamentally changed science’s view of how proteins are made — and how they can misform with disastrous results.

Appointment to a Sterling Professorship is one of the University’s highest faculty honors.

A longtime member of the School of Medicine faculty, Horwich has been a Howard Hughes Medical Institute investigator since 1990, and has served as an attending physician in pediatrics for almost 20 years at Yale-New Haven Hospital (YNHH).

In his research, Horwich has helped unravel one of the most vexing mysteries in cell biology: how the chains of amino acids that make up proteins fold into the unique three-dimensional shapes needed for the proteins to successfully perform their tasks, which are as varied as muscle contraction, immunity, digestion, metabolism and higher functions such as perception and cognition.

The Yale professor led the team that discovered and described ?chaperonins, “machines” within the cell that play a key role in the proper folding and configuration of proteins. Chaperonins help chains of amino acids fold into proteins that are then able, by virtue of their shape, to interact with drug molecules, hormones and brain transmitters such as serotonin and dopamine. The chaperonins, which are present in all living cells, are part of a quality-control network that ensures that proteins are properly configured, and that poorly folded proteins are targeted for destruction.

When proteins fail to configure correctly, disease can result. Clumps of unfolded or improperly folded proteins, called “aggregates,” have been associated with such conditions as Alzheimer’s, Parkinson’s, “mad cow” disease and the paralyzing nerve disorder amytrophic lateral sclerosis (ALS, also known as “Lou Gehrig’s disease”).

Through his characterization of the structure and function of the chaperonins, Horwich has opened the possibility of new, targeted treatments for these and other disorders.

In recent years, Horwich has been focusing on the question of why the chaperonins are unable to prevent the protein aggregation seen in neurodegenerative diseases. His group is seeking to elucidate the structure of fibrillar aggregates, so-called amyloid, that collect in the nerves and the heart in one such disease, familial amyloid polyneuropathy. He is also working on a model of ALS, which is in some cases caused by misfolding of a specific enzyme.

Horwich received his B.A. and M.D. degrees from Brown University. He completed his residency in pediatrics at YNHH, and then spent three years doing research at the Salk Institute in La Jolla, California, in the laboratories of tumor biologists Walter Eckhart and Tony Hunter. He returned to Yale in 1981 to work with human geneticist Leon Rosenberg, who later became dean of the School of Medicine. Horwich joined the Yale faculty in 1984 as an assistant professor in genetics, and was named a full professor in that department in 1995. He was appointed as the Eugene Higgins Professor of Cellular and Molecular Physiology in 2003. Horwich is now a “bicoastal” scientist with laboratories at Yale and at the Scripps Institute in La Jolla.

His honors include election to the National Academy of Sciences in 2003, the Gairdner International Award for achievement in 2004, the 2006 Stein and Moore Award of the Protein Society and the Wiley Prize in the Biomedical Sciences in February of this year. He is a member of the American Association for the Advancement of Science, the American Chemical Society, the American Society of Cell Biology, the American Society of Human Genetics and the Protein Society.

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