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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.
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E. Sethe Burgie,Katherine Basore,Michael J. Rau,Brock Summers, Alayna J. Mickles, Vadim Grigura, James A. J. Fitzpatrick,Richard D. Vierstra
NATURE COMMUNICATIONSno. 1 (2024)
Journal of Biological Chemistrypp.107369, (2024)
Plant physiologyno. 2 (2023): 1395-1415
Nature Plantsno. 7 (2023): 1116-1129
Journal of Biological Chemistryno. 3 (2023): 103943-S505
Proceedings of the National Academy of Sciences of the United States of Americano. 14 (2022)
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#Papers: 341
#Citation: 34640
H-Index: 101
G-Index: 180
Sociability: 7
Diversity: 0
Activity: 1
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