The Arabidopsis thaliana mitogen‐activated protein kinases MPK3 and MPK6 target a subclass of 'VQ‐motif'‐containing proteins to regulate immune responses. Issue 2 (22nd April 2014)
- Record Type:
- Journal Article
- Title:
- The Arabidopsis thaliana mitogen‐activated protein kinases MPK3 and MPK6 target a subclass of 'VQ‐motif'‐containing proteins to regulate immune responses. Issue 2 (22nd April 2014)
- Main Title:
- The Arabidopsis thaliana mitogen‐activated protein kinases MPK3 and MPK6 target a subclass of 'VQ‐motif'‐containing proteins to regulate immune responses
- Authors:
- Pecher, Pascal
Eschen‐Lippold, Lennart
Herklotz, Siska
Kuhle, Katja
Naumann, Kai
Bethke, Gerit
Uhrig, Joachim
Weyhe, Martin
Scheel, Dierk
Lee, Justin - Abstract:
- <abstract abstract-type="main" id="nph12817-abs-0001"> <title>Summary</title> <p> <list id="nph12817-list-0001" list-type="bullet"> <list-item> <p>Mitogen‐activated protein kinase (MAPK) cascades play key roles in plant immune signalling, and elucidating their regulatory functions requires the identification of the pathway‐specific substrates.</p> </list-item> <list-item> <p>We used yeast two‐hybrid interaction screens, <italic>in vitro</italic> kinase assays and mass spectrometry‐based phosphosite mapping to study a family of MAPK substrates. Site‐directed mutagenesis and promoter‐reporter fusion studies were performed to evaluate the impact of substrate phosphorylation on downstream signalling.</p> </list-item> <list-item> <p>A subset of the <italic>Arabidopsis thaliana </italic>VQ‐motif‐containing proteins (VQPs) were phosphorylated by the MAPKs MPK3 and MPK6, and renamed MPK3/6‐targeted VQPs (MVQs). When plant protoplasts (expressing these MVQs) were treated with the flagellin‐derived peptide flg22, several MVQs were destabilized <italic>in vivo</italic>. The MVQs interact with specific WRKY transcription factors. Detailed analysis of a representative member of the MVQ subset, MVQ1, indicated a negative role in WRKY‐mediated defence gene expression – with mutation of the VQ‐motif abrogating WRKY binding and causing mis‐regulation of defence gene expression.</p> </list-item> <list-item> <p>We postulate the existence of a variety of WRKY‐VQP‐containing transcriptional<abstract abstract-type="main" id="nph12817-abs-0001"> <title>Summary</title> <p> <list id="nph12817-list-0001" list-type="bullet"> <list-item> <p>Mitogen‐activated protein kinase (MAPK) cascades play key roles in plant immune signalling, and elucidating their regulatory functions requires the identification of the pathway‐specific substrates.</p> </list-item> <list-item> <p>We used yeast two‐hybrid interaction screens, <italic>in vitro</italic> kinase assays and mass spectrometry‐based phosphosite mapping to study a family of MAPK substrates. Site‐directed mutagenesis and promoter‐reporter fusion studies were performed to evaluate the impact of substrate phosphorylation on downstream signalling.</p> </list-item> <list-item> <p>A subset of the <italic>Arabidopsis thaliana </italic>VQ‐motif‐containing proteins (VQPs) were phosphorylated by the MAPKs MPK3 and MPK6, and renamed MPK3/6‐targeted VQPs (MVQs). When plant protoplasts (expressing these MVQs) were treated with the flagellin‐derived peptide flg22, several MVQs were destabilized <italic>in vivo</italic>. The MVQs interact with specific WRKY transcription factors. Detailed analysis of a representative member of the MVQ subset, MVQ1, indicated a negative role in WRKY‐mediated defence gene expression – with mutation of the VQ‐motif abrogating WRKY binding and causing mis‐regulation of defence gene expression.</p> </list-item> <list-item> <p>We postulate the existence of a variety of WRKY‐VQP‐containing transcriptional regulatory protein complexes that depend on spatio‐temporal <italic>VQP</italic> and <italic>WRKY</italic> expression patterns. Defence gene transcription can be modulated by changing the composition of these complexes – in part – through MAPK‐mediated VQP degradation.</p> </list-item> </list> </p> </abstract> … (more)
- Is Part Of:
- New phytologist. Volume 203:Issue 2(2014)
- Journal:
- New phytologist
- Issue:
- Volume 203:Issue 2(2014)
- Issue Display:
- Volume 203, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 203
- Issue:
- 2
- Issue Sort Value:
- 2014-0203-0002-0000
- Page Start:
- 592
- Page End:
- 606
- Publication Date:
- 2014-04-22
- Subjects:
- Botany -- Periodicals
580 - Journal URLs:
- http://nph.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1469-8137/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/nph.12817 ↗
- Languages:
- English
- ISSNs:
- 0028-646X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6085.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3227.xml