@Article{IPB-1277, 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}, url = {http://cshperspectives.cshlp.org/content/2/7/a005546.full?sid=084e458a-ebe2-449e-a254-577d24ee0e29}, 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.} }