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3 Briggs Hall

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    Our over-arching goal is to better understand the role of the ubiquitin modification system in plant biology using the model plant Arabidopsis thaliana. We seek to uncover the molecular mechanisms by which specific proteins are targetted for vacuolar or proteasomal degradation, and how the various stages of this pathway are regulated. This includes identifying the cis-acting signals that mediate the recognition of protein substrates by E3 ubiquitin ligases and discovering trans-acting factors that facilitate or impede substrate ubiquitination. Our lab focuses on three major projects.

Welcome to the Callis Lab

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PFKb

We are studying the function of the family of phosphofructokinase-B (pfkB) type proteins in plants. The Callis lab has begun characterization of two of these members, fructokinase like protein 1 and 2 (FLN1, -2), in Arabidopsis and found both to be important during chloroplast development.

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RING

We are examining the activity of another family of proteins containing RING and variant RING domains. These domains have been implicated in the E3 ubiquitin ligase activity of many proteins. We seek to identify putative proteins containing these domains, verify their ligase activity using in vitro ubiquitination assays, identify interacting partners, and characterize their function in vivo by studying the phenotypes of plants with mutations in RING-domain-containing proteins.

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Auxin Signaling

Auxin signal transduction requires the ubiquitin/proteasome pathway. We are interested in studying the degradation of the AUX/IAA family of transcriptional repressors as well as other components of auxin signaling pathways. We hope to characterize the regions required for recognition of the proteolytic targets, and to learn more about the ways in which auxin affects the rate of proteolysis of specific substrates.

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