Regulation of ethylene biosynthesis through protein degradation

Wendy J. Lyzenga, Sophia L. Stone

Research output: Contribution to journalReview articlepeer-review

24 Citations (Scopus)

Abstract

The function of hormones during plant growth, development and response to environmental stresses relies heavily upon the actions of the ubiquitin proteasome system (UPS), which selectively degrades numerous proteins. Synthesis of ethylene, a growth and stress hormone, is regulated in part by the ubiquitin-dependent degradation of the ratelimiting enzymatic protein aminocyclopropane-1-carboxylic acid synthase (ACS). Regulation of ACS protein stability, and therefore ethylene production, is mediated by noncatalytic sequences within the C-terminal extension of many ACS proteins. In this review we provide a brief overview of the E3 ligases that target ACS proteins for degradation and discuss how post-translational modification of the C-terminal extensions influence protein stability.

Original languageEnglish
JournalPlant Signaling and Behavior
Volume7
Issue number11
DOIs
Publication statusPublished - Nov 2012

Bibliographical note

Funding Information:
The authors would like to thank Lucy Federico for comments on the manuscript. SLS is supported by grants the Natural Sciences and Engineering Research Council of Canada (NSERC). WJL is supported by a post-graduate scholarship from NSERC.

ASJC Scopus Subject Areas

  • Plant Science

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