@Article{IPB-1541,
author = {Calderon-Villalobos, L. I. and Tan, X. and Zheng, N. and Estelle, M.},
title = {{Auxin Perception—Structural Insights}},
year = {2010},
pages = {a005546},
journal = {Cold Spring Harb. Perspect. Biol.},
doi = {10.1101/cshperspect.a005546},
volume = {2},
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.}    
}