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Auxin perception--structural insights Calderon-Villalobos LI; Tan X; Zheng N; Estelle MCold Spring Harb Perspect Biol 2010[Jul]; 2 (7): a005546The 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 SCF(TIR1) 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.|Hydrolysis[MESH]|Indoleacetic Acids/*metabolism[MESH]|Signal Transduction[MESH] |
