Leyser, O. and Kepinski, S. (2004) Auxin-induced SCFTIR1-Aux/IAA interaction involves stable modification of the SCFTIR1 complex. Proceedings of the National Academy of Sciences of the United States of America. pp. 12381-12386. ISSN 1091-6490
Abstract
The plant hormone auxin can regulate gene expression by destabilizing members of the Aux/IAA family of transcriptional repressors. Auxin-induced Aux/IAA degradation requires the protein-ubiquitin ligase SCFTIR1, with auxin acting to enhance the interaction between the Aux/IAAs and SCIFTIR1. SKP1, Cullin, and an F-box-containing protein (SCF)-mediated degradation is an important component of many eukaryotic signaling pathways. In all known cases to date, the interaction between the targets and their cognate SCFs is regulated by signal-induced modification of the target. The mechanism by which auxin promotes the interaction between SCFTIR1 and Aux/IAAs is not understood, but current hypotheses propose auxin-induced phosphorylation, hydroxylation, or proline isomerization of the Aux/IAAs. We found no evidence to support these hypotheses or indeed that auxin induces any stable modification of Aux/IAAs to increase their affinity for SCFTIR1. Instead, we present data suggesting that auxin promotes the SCIFTIR1-Aux/IAA interaction by affecting the SCIF component, TIR1, or proteins tightly associated with it.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2004 by The National Academy of Sciences of the USA |
Keywords: | AUX/IAA PROTEINS,UBIQUITIN-LIGASE,HIF-ALPHA,DEGRADATION,HYDROXYLATION,SCF |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Repository Officer |
Date Deposited: | 20 Apr 2005 |
Last Modified: | 16 Oct 2024 11:51 |
Published Version: | https://doi.org/10.1073/pnas.0402868101 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1073/pnas.0402868101 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:406 |