Auxin-induced SCFTIR1-Aux/IAA interaction involves stable modification of the SCFTIR1 complex

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, USA. pp. 12381-12386. ISSN 0027-8424

Full text available as:

Preview

Text (leysero6.pdf)
leysero6.pdf
Download (408Kb)

Published Version: http://dx.doi.org/10.1073/pnas.0402868101

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.

Item Type:	Article
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
Academic Units:	The University of York > Biology (York)
Depositing User:	Repository Officer
Date Deposited:	20 Apr 2005
Last Modified:	19 Feb 2013 11:53
Published Version:	http://dx.doi.org/10.1073/pnas.0402868101
Status:	Published
Refereed:	Yes
Related URLs:	http://www.pnas.org/cgi/content/short/10...
URI:	http://eprints.whiterose.ac.uk/id/eprint/406

Actions (login required)

View Item