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Title: Social Network: JAZ Protein Interactions Expand Our Knowledge of Jasmonate Signaling

Abstract

Members of the family of JASMONATE ZIM-DOMAIN (JAZ) proteins are key regulators of the jasmonate (JA) hormonal response. The 12-member family is characterized by three conserved domains, an N-terminal domain, a TIFY-containing ZINC-FINGER EXPRESSED IN INFLORESCENCE MERISTEM domain, and a C-terminal Jas domain. JAZ proteins regulate JA-responsive gene transcription by inhibiting DNA-binding transcription factors in the absence of JA. JAZ proteins interact in a hormone-dependent manner with CORONATINE INSENSITIVE 1 (COI1), the recognition component of the E3 ubiquitin ligase, SCFCOI1, resulting in the ubiquitination and subsequent degradation of JAZs via the 26S proteasome pathway. Since their discovery in 2007, JAZ proteins have been implicated in protein–protein interactions with multiple transcription factors. These studies have shed light on the mechanism by which JAZs repress transcription, are targeted for degradation, modulate the JA signaling response, and participate in crosstalk with other hormone signaling pathways. In this review, we will take a close look at the recent discoveries made possible by the characterization JAZ protein–protein interactions.

Authors:
 [1];  [1]
  1. Washington State Univ., Pullman, WA (United States). Inst. of Biological Chemistry
Publication Date:
Research Org.:
Washington State Univ., Pullman, WA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1628224
Grant/Contract Number:  
FG02-99ER20323; FG03-99ER20323
Resource Type:
Accepted Manuscript
Journal Name:
Frontiers in Plant Science
Additional Journal Information:
Journal Volume: 3; Journal ID: ISSN 1664-462X
Publisher:
Frontiers Research Foundation
Country of Publication:
United States
Language:
English
Subject:
54 ENVIRONMENTAL SCIENCES; Plant Sciences; Arabidopsis; hormone action; jasmonate; JAZ

Citation Formats

Wager, Amanda, and Browse, John. Social Network: JAZ Protein Interactions Expand Our Knowledge of Jasmonate Signaling. United States: N. p., 2012. Web. doi:10.3389/fpls.2012.00041.
Wager, Amanda, & Browse, John. Social Network: JAZ Protein Interactions Expand Our Knowledge of Jasmonate Signaling. United States. https://doi.org/10.3389/fpls.2012.00041
Wager, Amanda, and Browse, John. Sun . "Social Network: JAZ Protein Interactions Expand Our Knowledge of Jasmonate Signaling". United States. https://doi.org/10.3389/fpls.2012.00041. https://www.osti.gov/servlets/purl/1628224.
@article{osti_1628224,
title = {Social Network: JAZ Protein Interactions Expand Our Knowledge of Jasmonate Signaling},
author = {Wager, Amanda and Browse, John},
abstractNote = {Members of the family of JASMONATE ZIM-DOMAIN (JAZ) proteins are key regulators of the jasmonate (JA) hormonal response. The 12-member family is characterized by three conserved domains, an N-terminal domain, a TIFY-containing ZINC-FINGER EXPRESSED IN INFLORESCENCE MERISTEM domain, and a C-terminal Jas domain. JAZ proteins regulate JA-responsive gene transcription by inhibiting DNA-binding transcription factors in the absence of JA. JAZ proteins interact in a hormone-dependent manner with CORONATINE INSENSITIVE 1 (COI1), the recognition component of the E3 ubiquitin ligase, SCFCOI1, resulting in the ubiquitination and subsequent degradation of JAZs via the 26S proteasome pathway. Since their discovery in 2007, JAZ proteins have been implicated in protein–protein interactions with multiple transcription factors. These studies have shed light on the mechanism by which JAZs repress transcription, are targeted for degradation, modulate the JA signaling response, and participate in crosstalk with other hormone signaling pathways. In this review, we will take a close look at the recent discoveries made possible by the characterization JAZ protein–protein interactions.},
doi = {10.3389/fpls.2012.00041},
journal = {Frontiers in Plant Science},
number = ,
volume = 3,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2012},
month = {Sun Jan 01 00:00:00 EST 2012}
}

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