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Am J Physiol Endocrinol Metab 296: E223-E227, 2009. First published December 2, 2008; doi:10.1152/ajpendo.90807.2008 Free Article
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REVIEW

Hormone signaling through protein destruction: a lesson from plants

Xu Tan1 and Ning Zheng1,2

1Department of Pharmacology and 2Howard Hughes Medical Institute, University of Washington, Seattle, Washington

Submitted 27 March 2008 ; accepted in final form 26 November 2008

ABSTRACT

Ubiquitin-dependent protein degradation has emerged as a major pathway regulating eukaryotic biology. By employing a variety of ubiquitin ligases to target specific cellular proteins, the ubiquitin-proteasome system controls physiological processes in a highly regulated fashion. Recent studies on a plant hormone auxin have unveiled a novel paradigm of signal transduction in which ubiquitin ligases function as hormone receptors. Perceived by the F-box protein subunit of the SCFTIR1 ubiquitin ligase, auxin directly promotes the recruitment of a family of transcriptional repressors for ubiquitination, thereby activating extensive transcriptional programs. Structural studies have revealed that auxin functions through a "molecular glue" mechanism to enhance protein-protein interactions with the assistance of another small molecule cofactor, inositol hexakisphosphate. Given the extensive repertoire of similar ubiquitin ligases in eukaryotic cells, this novel and widely adopted hormone-signaling mechanism in plants may also exist in other organisms.

auxin; phytohormone; hormone receptor; F-box protein; ubiquitin ligase; protein degradation


Address for correspondence: N. Zheng, Howard Hughes Medical Institute, Dept. of Pharmacology, Box 357280, Univ. of Washington, Seattle, WA 98195 (e-mail: nzheng{at}u.washington.edu)






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