Raymond J. Deshaies
Amgen, Inc.
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Primary Section: 21, Biochemistry Secondary Section: 22, Cellular and Developmental Biology Membership Type:
Member
(elected 2016)
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Biosketch
Raymond Deshaies is a biochemist and cell biologist recognized for his work on the mechanism and regulation of protein degradation by the ubiquitin-proteasome system. In particular, his laboratory discovered SCFCdc4, the first member of the large family of cullin–RING ubiquitin ligases (CRLs), and since then has made a number of seminal findings about how CRL enzymes work and how their activity is controlled. Dr. Deshaies was born and raised in Waterbury, CT. He graduated from Cornell University with a BS in biochemistry in 1983 and received his PhD in biochemistry in 1988 from the University of California, Berkeley. After postdoctoral work at the University of California, San Francisco, he joined the faculty of Caltech in 1994 and was appointed to the Howard Hughes Medical Institute in 2000. In addition to his academic work, Dr. Deshaies founded the biotechnology companies Proteolix (which developed Kyprolis) in 2003 and Cleave Biosciences in 2011.
Research Interests
Raymond Deshaies’s laboratory works on mechanisms of protein homeostasis in eukaryotic cells. They are particularly interested in the role of protein degradation via the ubiquitin-proteasome system (UPS). Protein degradation via the UPS serves two general functions: it is employed to regulate pathways such as the cell cycle, and it is critical for quality control of the cellular proteome. Cells express ~600 or so ubiquitin ligase (E3) enzymes that promote ubiquitin conjugation to substrate proteins. Cullin–RING ubiquitin ligases (CRLs) comprise a family of ~250 multisubunit E3s that function in many different regulatory pathways. The Deshaies group has studied how CRL enzymes assemble, how their activity is regulated by reversible modification with the ubiquitin-like protein Nedd8, how they promote catalysis, and what their substrates and cellular functions are. Another major focus is to understand how protein quality control works and how its malfunction or therapeutic manipulation relates to human diseases. This interest has motivated work on the mechanism, regulation, substrates, and inhibitors of the segregase p97/VCP, which plays a critical role in multiple cellular quality control pathways.
