Richard D. Vierstra
Washington University in St. Louis
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Primary Section: 25, Plant Biology Secondary Section: 62, Plant, Soil, and Microbial Sciences Membership Type:
Member
(elected 2018)
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Biosketch
Richard Vierstra is a plant biologist recognized for his work on protein turnover and light signaling. He is particularly known for his characterizations of the ubiquitin/proteasome and autophagy degradative systems and for elucidating the molecular mechanisms underpinning photoperception by the phytochrome family of photoreceptors. Vierstra was born in Providence, Rhode Island and grew up in the nearby town of Cumberland. He earned his B.S. in biology from the University of Connecticut in 1972, his PhD in plant biology from the DOE-Plant Research Laboratory at Michigan State University in 1980, and then was a postdoctoral fellow with Dr. Peter Quail at the University of Wisconsin-Madison. In 1984, Vierstra joined that faculty of the University of Wisconsin with his final appointment being the Stanley J. Peloquin Professor of Genetics. He was a Fulbright senior scholar at the University of Melbourne, Australia in 1994. In 2005, Vierstra moved to the Biology Department at Washington University in St. Louis, where he is now the George and Charmaine Mallinckrodt Endowed Chair. He is a fellow of both the American Society of Plant Biologists and the American Association for the Advancement of Science, and is a member of the National Academy of Sciences.
Research Interests
Richard Vierstra’ laboratory has directed their research to two main questions; how do cells selectively recycle proteins? And how does light influence the growth and development of plants? The recycling studies first focused on the ubiquitin/proteasome proteolytic system, showing how it is organized, regulated, and chooses appropriate targets using a large cohort of ubiquitin ligases in the model plant Arabidopsis. Particularly information has been the use of mass spectrometry to catalog the plethora of ubiquitylation targets. Their research is now directed at the autophagy system, with discoveries that a number of organelles, protein complexes and a substantial portion of plant proteomes are influenced by this turnover. In particular, his group found a novel autophagic mechanism for clearing proteasomes that involves a sequence of ubiquitylation and aggregation events. Studies on phytochromes have centered on understanding how these photoreceptors convert light into a conformation signal that initiates downstream signaling cascades. Particularly notable were the development of the first atomic resolution structures of the photosensing region in both its ground and photoactivated states, using crystallographic, 2D-NMR and cryo-EM techniques, to reveal the early structural changes underpinning light perception. In addition, the Vierstra lab has characterized SUMO system in plants and how this post-translational modifier promotes stress tolerance.
