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Cited by 274

The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.

Jasmonates: Structural Requirements for Lipid-Derived Signals Active in Plant Stress Responses and Development

Wasternack, Claus, Kombrink, Erich·2010·ACS Chemical Biology
DOI 10.1021/cb900269u
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Abstract

Jasmonates are lipid-derived signals that mediate plant stress responses and development processes. Enzymes participating in biosynthesis of jasmonic acid (JA) (1, 2) and components of JA signaling have been extensively characterized by biochemical and molecular-genetic tools. Mutants of Arabidopsis and tomato have helped to define the pathway for synthesis of jasmonoyl-isoleucine (JA-Ile), the active form of JA, and to identify the F-box protein COI1 as central regulatory unit. However, details of the molecular mechanism of JA signaling have only recently been unraveled by the discovery of JAZ proteins that function in transcriptional repression. The emerging picture of JA perception and signaling cascade implies the SCF(COI1) complex operating as E3 ubiquitin ligase that upon binding of JA-Ile targets JAZ repressors for degradation by the 26S-proteasome pathway, thereby allowing the transcription factor MYC2 to activate gene expression. The fact that only one particular stereoisomer, (+)-7-iso-JA-l-Ile (4), shows high biological activity suggests that epimerization between active and inactive diastereomers could be a mechanism for turning JA signaling on or off. The recent demonstration that COI1 directly binds (+)-7-iso-JA-l-Ile (4) and thus functions as JA receptor revealed that formation of the ternary complex COI1-JA-Ile-JAZ is an ordered process. The pronounced differences in biological activity of JA stereoisomers also imply strict stereospecific control of product formation along the JA biosynthetic pathway. The pathway of JA biosynthesis has been unraveled, and most of the participating enzymes are well-characterized. For key enzymes of JA biosynthesis the crystal structures have been established, allowing insight into the mechanisms of catalysis and modes of substrate binding that lead to formation of stereospecific products.

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Metadata

Authors
Wasternack, C., & Kombrink, E.
Venue
ACS Chemical Biology
Publisher
American Chemical Society (ACS)
Published
2009-12-21
Volume
5
Issue
1
Pages
63-77
ISSN
  • 1554-8929 (ISSN-L)
  • 1554-8937
DOI
10.1021/cb900269u
OpenAlex
W2068634426
Cited by
274
References
91
FWCI
8.64
Type
journal article
Language
en
Open access
closed

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