Auxin Perception-Structural Insights

被引：120

作者：

Calderon-Villalobos, Luz Irina ^{[1
]}

Tan, Xu ^{[2
,3
]}

Zheng, Ning ^{[2
]}

Estelle, Mark ^{[1
]}

机构：

[1] Univ Calif San Diego, Sect Cell & Dev Biol, La Jolla, CA 92093 USA

[2] Univ Washington, Sch Med, Dept Pharmacol, Seattle, WA 98195 USA

[3] Harvard Univ, Brigham & Womens Hosp, Sch Med, Div Genet,Dept Genet, Boston, MA 02115 USA

来源：

COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY | 2010年 / 2卷 / 07期

关键词：

SCF UBIQUITIN-LIGASE; FUNCTIONAL GENOMIC ANALYSIS; GENE FAMILY-MEMBERS; BOX PROTEIN TIR1; AUX/IAA PROTEINS; TRANSCRIPTIONAL REPRESSION; ARABIDOPSIS-THALIANA; PLANT DEVELOPMENT; DEGRADATION; PROTEASOME;

D O I：

10.1101/cshperspect.a005546

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页数：16

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