Auxin Perception—Structural Insights
- 1Section of Cell and Developmental Biology, UCSD, La Jolla, California 92093
- 2Department of Pharmacology, University of Washington, School of Medicine, Seattle, Washington 98195
- 3Department of Genetics, Harvard Medical School, Division of Genetics, Brigham and Women's Hospital, Boston, Massachusetts 02115
- Correspondence: mestelle{at}ucsd.edu
Abstract
The identity of the auxin receptor(s) and the mechanism of auxin perception has been a subject of intense interest since the discovery of auxin almost a century ago. The development of genetic approaches to the study of plant hormone signaling led to the discovery that auxin acts by promoting degradation of transcriptional repressors called Aux/IAA proteins. This process requires a ubiquitin protein ligase (E3) called SCFTIR1 and related SCF complexes. Surprisingly, auxin works by directly binding to TIR1, the F-box protein subunit of this SCF. Structural studies demonstrate that auxin acts like a “molecular glue,” to stabilize the interaction between TIR1 and the Aux/IAA substrate. These exciting results solve an old problem in plant biology and reveal new mechanisms for E3 regulation and hormone perception.
Footnotes
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Editors: Mark Estelle, Dolf Weijers, Ottoline Leyser, and Karin Ljung
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Additional Perspectives on Auxin Signaling available at www.cshperspectives.org
- Copyright © 2010 Cold Spring Harbor Laboratory Press; all rights reserved
