Regulation of ethylene biosynthesis through protein degradation

Wendy J. Lyzenga; Sophia L. Stone

doi:10.4161/psb.21930

Regulation of ethylene biosynthesis through protein degradation

Wendy J. Lyzenga, Sophia L. Stone

Medicine

Medicine

Research output: Contribution to journal › Review article › peer-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 language	English
Journal	Plant Signaling and Behavior
Volume	7
Issue number	11
DOIs	https://doi.org/10.4161/psb.21930
Publication status	Published - 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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10.4161/psb.21930

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title = "Regulation of ethylene biosynthesis through protein degradation",

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.",

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Regulation of ethylene biosynthesis through protein degradation

Abstract

Bibliographical note

ASJC Scopus Subject Areas

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