Campus Units

Genetics, Development and Cell Biology

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

3-7-2018

Journal or Book Title

Molecular & Cellular Proteomics

DOI

10.1074/mcp.MR117.000476

Abstract

Ubiquitin-mediated control of protein stability is central to most aspects of plant hormone signaling. Attachment of ubiquitin to target proteins occurs via an enzymatic cascade with the final step being catalyzed by a family of enzymes known as E3 ubiquitin ligases, which have been classified based on their protein domains and structures. While E3 ubiquitin ligases are conserved among eukaryotes, in plants they are well-known to fulfill unique roles as central regulators of phytohormone signaling, including hormone perception and regulation of hormone biosynthesis. This review will highlight up-to-date findings that have refined well-known E3 ligase-substrate interactions and defined novel E3 ligase substrates that mediate numerous hormone signaling pathways. Additionally, examples of how particular E3 ligases may mediate hormone crosstalk will be discussed as an emerging theme. Looking forward, promising experimental approaches and methods that will provide deeper mechanistic insight into the roles of E3 ubiquitin ligases in plants will be considered.

Comments

This research was originally published in Molecular & Cellular Proteomics. Kelley, Dior. "E3 ubiquitin ligases: key regulators of hormone signaling in plants." Mol Cell Proteomics. 2018; 17:1047-1054. doi: 10.1074/mcp.MR117.000476. © the American Society for Biochemistry and Molecular Biology.

Copyright Owner

The American Society for Biochemistry and Molecular Biology, Inc.

Language

en

File Format

application/pdf

Published Version

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