Richard D. Vierstra

ORCID: 0000-0003-0210-3516
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About
Contact & Profiles
Research Areas
  • Ubiquitin and proteasome pathways
  • Photosynthetic Processes and Mechanisms
  • Light effects on plants
  • Plant Molecular Biology Research
  • Autophagy in Disease and Therapy
  • Glycosylation and Glycoproteins Research
  • Endoplasmic Reticulum Stress and Disease
  • Peptidase Inhibition and Analysis
  • Plant Parasitism and Resistance
  • Algal biology and biofuel production
  • Plant tissue culture and regeneration
  • Plant and Biological Electrophysiology Studies
  • Plant responses to water stress
  • Photoreceptor and optogenetics research
  • Plant Gene Expression Analysis
  • Plant Stress Responses and Tolerance
  • RNA modifications and cancer
  • Transgenic Plants and Applications
  • Genomics and Phylogenetic Studies
  • Lipid metabolism and biosynthesis
  • Plant nutrient uptake and metabolism
  • Plant Reproductive Biology
  • RNA and protein synthesis mechanisms
  • 14-3-3 protein interactions
  • Biocrusts and Microbial Ecology

Washington University in St. Louis
2016-2025

University of Wisconsin–Madison
2013-2022

ORCID
2022

University of Helsinki
2021

Medical University Pleven
2017

Madison Group (United States)
2002-2015

University of Wisconsin–Eau Claire
2012

Wake Forest University
2011

University of California, Davis
1990-2007

University of Kentucky
2007

Combining heat and light responses Plants integrate a variety of environmental signals to regulate growth patterns. Legris et al. Jung analyzed how the quality is interpreted through ambient temperature transcription (see Perspective by Halliday Davis). The phytochromes responsible for reading ratio red far-red were also responsive small shifts in that occur when dusk falls or shade from neighboring plants cools soil. Science , this issue p. 897 886 ; see 832

10.1126/science.aaf5656 article EN cc-by Science 2016-10-28

The covalent attachment of ubiquitin is an important determinant for selective protein degradation by the 26S proteasome in plants and animals. specificity ubiquitination often controlled ubiquitin-protein ligases (or E3s), which facilitate transfer to appropriate targets. One ligase type, SCF E3s are composed four proteins, cullin1/Cdc53, Rbx1/Roc1/Hrt1, Skp1, F-box protein. protein, identifies targets, binds Skp1 component complex through a degenerate N-terminal ≈60-aa motif called F-box....

10.1073/pnas.162339999 article EN Proceedings of the National Academy of Sciences 2002-08-08

The vacuole/lysosome serves an important recycling function during starvation and senescence in eukaryotes via a process called autophagy. Here bulk cytosolic constituents organelles become sequestered specialized autophagic vesicles, which then deliver their cargo to the vacuole for degradation. In yeasts, genetic screens have identified two novel post-translational modification pathways remarkably similar ubiquitination that are required From searches of <i>Arabidopsis</i>genome, we gene...

10.1074/jbc.m204630200 article EN cc-by Journal of Biological Chemistry 2002-08-30

Abstract Autophagy is an important mechanism for nonselective intracellular breakdown whereby cytosol and organelles are encapsulated in vesicles, which then engulfed digested by lytic vacuoles/lysosomes. In yeast, this encapsulation employs a set of autophagy (ATG) proteins that direct the conjugation two ubiquitin-like protein tags, ATG8 ATG12, to phosphatidylethanolamine ATG5 protein, respectively. Using Arabidopsis (Arabidopsis thaliana) atg7 mutant unable ligate either tag, we...

10.1104/pp.105.060673 article EN PLANT PHYSIOLOGY 2005-07-22

Smallubiquitin-like modifier (SUMO) is a member of the superfamily ubiquitin-like polypeptides that become covalently attached to various intracellular target proteins as way alter their function, location, and/or half-life. Here we show SUMO conjugation system operates in plants through characterization the<i>Arabidopsis</i> pathway. An eight-gene family encoding tag was discovered were genes enzymes required for processing, ligation, and release. A diverse array conjugates could be...

10.1074/jbc.m209694200 article EN cc-by Journal of Biological Chemistry 2003-02-01

Ubiquitination of various intracellular proteins by ubiquitin-protein ligases (or E3s) plays an essential role in eukaryotic cell regulation primarily through its ability to selectively target for degradation the 26S proteasome. Skp1, Cullin, F-box (SCF) complexes are one influential E3 class that use deliver targets a core ligase activity provided and Rbx1 subunits. Almost 700 can be found Arabidopsis, indicating SCF E3s likely play pervasive plant physiology development. Here, we describe...

10.1073/pnas.0401698101 article EN Proceedings of the National Academy of Sciences 2004-04-16

The 26S proteasome is an essential proteolytic complex that responsible for degrading proteins conjugated with ubiquitin. It has been proposed the recognition of substrates by mediated a multiubiquitin-chain-binding protein previously characterized in both plants and animals. In this study, we identified Saccharomyces cerevisiae homolog protein, designated Mcb1. Mcb1 copurified conventional nickel chelate chromatography. addition, significant fraction cell extracts was present...

10.1128/mcb.16.11.6020 article EN Molecular and Cellular Biology 1996-11-01

Abstract Analysis of the Arabidopsis thaliana RING-ANK (for Really Interesting New Gene-Ankyrin) family, a subgroup RING-type E3 ligases, identified KEEP ON GOING (KEG) as essential for growth and development. In addition to RING-HCa ankyrin repeats, KEG contains kinase domain 12 HERC2-like repeats. The domains were functional in vitro ubiquitylation phosphorylation assays, respectively. Seedlings homozygous T-DNA insertions undergo arrest immediately after germination, suggestive increased...

10.1105/tpc.106.046532 article EN The Plant Cell 2006-12-01

Abstract Autophagy is an intracellular recycling route in eukaryotes whereby organelles and cytoplasm are sequestered vesicles, which subsequently delivered to the vacuole for breakdown. The process induced by various nutrient-responsive signaling cascades converging on Autophagy-Related1 (ATG1)/ATG13 kinase complex. Here, we describe ATG1/13 complex Arabidopsis thaliana show that it both a regulator target of autophagy. Plants missing ATG13 hypersensitive nutrient limitations senesce...

10.1105/tpc.111.090993 article EN The Plant Cell 2011-10-01

Autophagic recycling of intracellular plant constituents is maintained at a basal level under normal growth conditions but can be induced in response to nutritional demand, biotic stress, and senescence. One route requires the ubiquitin-fold proteins Autophagy-related (ATG)-8 ATG12, which become attached lipid phosphatidylethanolamine (PE) ATG5 protein, respectively, during formation engulfing vesicle delivery its cargo vacuole for breakdown. Here, we genetically analyzed conjugation...

10.1111/j.1365-313x.2010.04166.x article EN The Plant Journal 2010-02-03

Autophagy-mediated turnover removes damaged organelles and unwanted cytoplasmic constituents thus plays critical roles in cellular housekeeping nutrient recycling. This "self eating" is tightly regulated by the AUTOPHAGY-RELATED1/13 (ATG1/13) kinase complex, which connects metabolic environmental cues to vacuolar delivery of autophagic vesicles. Here, we describe Arabidopsis thaliana accessory proteins ATG11 ATG101, help link ATG1/13 complex membranes. promotes vesicle vacuole but not...

10.1105/tpc.113.120014 article EN The Plant Cell 2014-02-01

The covalent attachment of SUMO (small ubiquitin-like modifier) to other intracellular proteins affects a broad range nuclear processes in yeast and animals, including chromatin maintenance, transcription, transport across the envelope, as well protects from ubiquitin addition. Substantial increases SUMOylated upon various stresses have also implicated this modification general stress response. To help understand role(s) SUMOylation plants, we developed stringent method isolate SUMO-protein...

10.1073/pnas.1004181107 article EN Proceedings of the National Academy of Sciences 2010-09-02

Abstract The posttranslational addition of ubiquitin (Ub) profoundly controls the half-life, interactions, and/or trafficking numerous intracellular proteins. Using stringent two-step affinity methods to purify Ub-protein conjugates followed by high-sensitivity mass spectrometry, we identified almost 950 ubiquitylation substrates in whole Arabidopsis thaliana seedlings. list includes key factors regulating a wide range biological processes, including metabolism, cellular transport, signal...

10.1105/tpc.112.108613 article EN The Plant Cell 2013-05-01

In plants, autophagy has been assigned 'pro-death' and 'pro-survival' roles in controlling programmed cell death associated with microbial effector-triggered immunity. The role of basal immunity to virulent pathogens not addressed systematically, however. Using several autophagy-deficient (atg) genotypes, we determined the function plant Arabidopsis mutants lacking ATG5, ATG10 ATG18a develop spreading necrosis upon infection necrotrophic fungal pathogen, Alternaria brassicicola, which is...

10.1111/j.1365-313x.2011.04546.x article EN The Plant Journal 2011-02-19

Autophagy is a primary route for nutrient recycling in plants by which superfluous or damaged cytoplasmic material and organelles are encapsulated delivered to the vacuole breakdown. Central autophagy conjugation pathway that attaches AUTOPHAGY-RELATED8 (ATG8) phosphatidylethanolamine, then coats emerging autophagic membranes helps with cargo recruitment, vesicle enclosure, subsequent docking tonoplast. A key component ATG8 function ATG12, promotes lipidation upon its attachment ATG5. Here,...

10.1105/tpc.15.00158 article EN The Plant Cell 2015-05-01
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