Journal
PLANT PHYSIOLOGY
Volume 160, Issue 1, Pages 135-142Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.112.202184
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Funding
- Paul G. Allen Family Foundation
- National Science Foundation [CISE-0832773, IOS-0919021]
- National Institutes of Health [T32HD007183]
- National Science Foundation Graduate Research Fellowship
- Seattle Chapter of the Achievement Rewards for College Scientists Foundation
- Direct For Computer & Info Scie & Enginr
- Division of Computing and Communication Foundations [832824] Funding Source: National Science Foundation
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [0919021] Funding Source: National Science Foundation
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Explaining how the small molecule auxin triggers diverse yet specific responses is a long-standing challenge in plant biology. An essential step in auxin response is the degradation of Auxin/Indole-3-Acetic Acid (Aux/IAA, referred to hereafter as IAA) repressor proteins through interaction with auxin receptors. To systematically characterize diversity in degradation behaviors among IAA vertical bar receptor pairs, we engineered auxin-induced degradation of plant IAA proteins in yeast (Saccharomyces cerevisiae). We found that IAA degradation dynamics vary widely, depending on which receptor is present, and are not encoded solely by the degron-containing domain II. To facilitate this and future studies, we identified a mathematical model able to quantitatively describe IAA degradation behavior in a single parameter. Together, our results demonstrate the remarkable tunability conferred by specific configurations of the auxin response pathway.
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