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Site-specific ubiquitination is required for relieving the transcription factor Miz1-mediated suppression on TNF-α-induced JNK activation and inflammation

The transcription factor zinc-finger protein Miz1 represses TNF-α-induced JNK activation and the repression is relieved upon TNF-α stimulation. However, the underlying mechanism is incompletely understood. Here we report that Miz1 interferes with the ubiquitin conjugating enzyme (E2) Ubc13 for bindi... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America 03 January 2012, Vol.109(1), pp.191-6
Main Author: Liu, Jing
Other Authors: Yan, Jie , Jiang, Shan , Wen, Jing , Chen, Long , Zhao, Yingming , Lin, Anning
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; PMID: 22184250 Version:1 ; DOI: 10.1073/pnas.1105176108
Link: http://pubmed.gov/22184250
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recordid: medline22184250
title: Site-specific ubiquitination is required for relieving the transcription factor Miz1-mediated suppression on TNF-α-induced JNK activation and inflammation
format: Article
creator:
  • Liu, Jing
  • Yan, Jie
  • Jiang, Shan
  • Wen, Jing
  • Chen, Long
  • Zhao, Yingming
  • Lin, Anning
subjects:
  • Inflammation -- Enzymology
  • Jnk Mitogen-Activated Protein Kinases -- Metabolism
  • Kruppel-Like Transcription Factors -- Metabolism
  • Nuclear Proteins -- Metabolism
  • Protein Inhibitors of Activated Stat -- Metabolism
  • Tumor Necrosis Factor-Alpha -- Pharmacology
  • Ubiquitination -- Drug Effects
ispartof: Proceedings of the National Academy of Sciences of the United States of America, 03 January 2012, Vol.109(1), pp.191-6
description: The transcription factor zinc-finger protein Miz1 represses TNF-α-induced JNK activation and the repression is relieved upon TNF-α stimulation. However, the underlying mechanism is incompletely understood. Here we report that Miz1 interferes with the ubiquitin conjugating enzyme (E2) Ubc13 for binding to the RING domain of TNF-receptor associated factor 2 (TRAF2), thereby inhibiting the ubiquitin ligase (E3) activity of TRAF2 and suppressing TNF-α-induced JNK activation. Upon TNF-α stimulation, Miz1 rapidly undergoes K48-linked polyubiquitination at Lys388 and Lys472 residues and subsequent proteasomal degradation in a TRAF2-dependent manner. Replacement of Lysine 388 and Lysine 472 by arginines generates a nondegradable Miz1 mutant, which significantly suppresses TNF-α-induced JNK1 activation and inflammation. Thus, our results reveal a molecular mechanism by which the repression of TNF-α-induced JNK activation by Miz1 is de-repressed by its own site-specific ubiquitination and degradation,...
language: eng
source:
identifier: E-ISSN: 1091-6490 ; PMID: 22184250 Version:1 ; DOI: 10.1073/pnas.1105176108
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleSite-specific ubiquitination is required for relieving the transcription factor Miz1-mediated suppression on TNF-α-induced JNK activation and inflammation
creatorLiu, Jing ; Yan, Jie ; Jiang, Shan ; Wen, Jing ; Chen, Long ; Zhao, Yingming ; Lin, Anning
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subjectInflammation -- Enzymology ; Jnk Mitogen-Activated Protein Kinases -- Metabolism ; Kruppel-Like Transcription Factors -- Metabolism ; Nuclear Proteins -- Metabolism ; Protein Inhibitors of Activated Stat -- Metabolism ; Tumor Necrosis Factor-Alpha -- Pharmacology ; Ubiquitination -- Drug Effects
descriptionThe transcription factor zinc-finger protein Miz1 represses TNF-α-induced JNK activation and the repression is relieved upon TNF-α stimulation. However, the underlying mechanism is incompletely understood. Here we report that Miz1 interferes with the ubiquitin conjugating enzyme (E2) Ubc13 for binding to the RING domain of TNF-receptor associated factor 2 (TRAF2), thereby inhibiting the ubiquitin ligase (E3) activity of TRAF2 and suppressing TNF-α-induced JNK activation. Upon TNF-α stimulation, Miz1 rapidly undergoes K48-linked polyubiquitination at Lys388 and Lys472 residues and subsequent proteasomal degradation in a TRAF2-dependent manner. Replacement of Lysine 388 and Lysine 472 by arginines generates a nondegradable Miz1 mutant, which significantly suppresses TNF-α-induced JNK1 activation and inflammation. Thus, our results reveal a molecular mechanism by which the repression of TNF-α-induced JNK activation by Miz1 is de-repressed by its own site-specific ubiquitination and degradation,...
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titleSite-specific ubiquitination is required for relieving the transcription factor Miz1-mediated suppression on TNF-α-induced JNK activation and inflammation
descriptionThe transcription factor zinc-finger protein Miz1 represses TNF-α-induced JNK activation and the repression is relieved upon TNF-α stimulation. However, the underlying mechanism is incompletely understood. Here we report that Miz1 interferes with the ubiquitin conjugating enzyme (E2) Ubc13 for binding to the RING domain of TNF-receptor associated factor 2 (TRAF2), thereby inhibiting the ubiquitin ligase (E3) activity of TRAF2 and suppressing TNF-α-induced JNK activation. Upon TNF-α stimulation, Miz1 rapidly undergoes K48-linked polyubiquitination at Lys388 and Lys472 residues and subsequent proteasomal degradation in a TRAF2-dependent manner. Replacement of Lysine 388 and Lysine 472 by arginines generates a nondegradable Miz1 mutant, which significantly suppresses TNF-α-induced JNK1 activation and inflammation. Thus, our results reveal a molecular mechanism by which the repression of TNF-α-induced JNK activation by Miz1 is de-repressed by its own site-specific ubiquitination and degradation,...
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abstractThe transcription factor zinc-finger protein Miz1 represses TNF-α-induced JNK activation and the repression is relieved upon TNF-α stimulation. However, the underlying mechanism is incompletely understood. Here we report that Miz1 interferes with the ubiquitin conjugating enzyme (E2) Ubc13 for binding to the RING domain of TNF-receptor associated factor 2 (TRAF2), thereby inhibiting the ubiquitin ligase (E3) activity of TRAF2 and suppressing TNF-α-induced JNK activation. Upon TNF-α stimulation, Miz1 rapidly undergoes K48-linked polyubiquitination at Lys388 and Lys472 residues and subsequent proteasomal degradation in a TRAF2-dependent manner. Replacement of Lysine 388 and Lysine 472 by arginines generates a nondegradable Miz1 mutant, which significantly suppresses TNF-α-induced JNK1 activation and inflammation. Thus, our results reveal a molecular mechanism by which the repression of TNF-α-induced JNK activation by Miz1 is de-repressed by its own site-specific ubiquitination and degradation,...
doi10.1073/pnas.1105176108
pmid22184250
date2012-01-03