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Comparative proteomic study of Arabidopsis mutants mpk4 and mpk6
Arabidopsis MPK4 and MPK6 are implicated in different signalling pathways responding to diverse external stimuli. This was recently correlated with transcriptomic profiles of Arabidopsis mpk4 and mpk6 mutants and thus it should be reflected also on the level of constitutive proteomes. Therefore, we...
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Published in: | Scientific reports 2016-06, Vol.6 (1), p.28306-28306, Article 28306 |
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description | Arabidopsis MPK4 and MPK6 are implicated in different signalling pathways responding to diverse external stimuli. This was recently correlated with transcriptomic profiles of Arabidopsis
mpk4
and
mpk6
mutants and thus it should be reflected also on the level of constitutive proteomes. Therefore, we performed a shot gun comparative proteomic analysis of Arabidopsis
mpk4
and
mpk6
mutant roots. We have used bioinformatic tools and propose several new proteins as putative MPK4 and MPK6 phosphorylation targets. Among these proteins in the
mpk6
mutant were important modulators of development such as CDC48A and phospholipase D alpha 1. In the case of the
mpk4
mutant transcriptional reprogramming might be mediated by phosphorylation and change in the abundance of mRNA decapping complex VCS. Further comparison of
mpk4
and
mpk6
root differential proteomes showed differences in the composition and regulation of defense related proteins. The
mpk4
mutant showed altered abundances of antioxidant proteins. The examination of catalase activity in response to oxidative stress revealed that this enzyme might be preferentially regulated by MPK4. Finally, we proposed developmentally important proteins as either directly or indirectly regulated by MPK4 and MPK6. These proteins contribute to known phenotypic defects in the
mpk4
and
mpk6
mutants. |
doi_str_mv | 10.1038/srep28306 |
format | article |
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mpk4
and
mpk6
mutants and thus it should be reflected also on the level of constitutive proteomes. Therefore, we performed a shot gun comparative proteomic analysis of Arabidopsis
mpk4
and
mpk6
mutant roots. We have used bioinformatic tools and propose several new proteins as putative MPK4 and MPK6 phosphorylation targets. Among these proteins in the
mpk6
mutant were important modulators of development such as CDC48A and phospholipase D alpha 1. In the case of the
mpk4
mutant transcriptional reprogramming might be mediated by phosphorylation and change in the abundance of mRNA decapping complex VCS. Further comparison of
mpk4
and
mpk6
root differential proteomes showed differences in the composition and regulation of defense related proteins. The
mpk4
mutant showed altered abundances of antioxidant proteins. The examination of catalase activity in response to oxidative stress revealed that this enzyme might be preferentially regulated by MPK4. Finally, we proposed developmentally important proteins as either directly or indirectly regulated by MPK4 and MPK6. These proteins contribute to known phenotypic defects in the
mpk4
and
mpk6
mutants.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep28306</identifier><identifier>PMID: 27324189</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/449/2661/2665 ; 631/449/2675 ; 82/1 ; 82/58 ; Amino Acid Sequence ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Binding Sites ; Catalase - metabolism ; Cell division ; Gene Knockout Techniques ; Gene Ontology ; Genes ; Humanities and Social Sciences ; Mitogen-Activated Protein Kinases - genetics ; multidisciplinary ; Mutants ; Mutation, Missense ; Ontology ; Oxidative stress ; Peroxidase - metabolism ; Phosphorylation ; Plant Roots - enzymology ; Plant Roots - genetics ; Protein Binding ; Protein Processing, Post-Translational ; Proteins ; Proteome - metabolism ; Proteomics ; Receptors for Activated C Kinase - metabolism ; Science ; Stress, Physiological</subject><ispartof>Scientific reports, 2016-06, Vol.6 (1), p.28306-28306, Article 28306</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Jun 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-a7e7859327d7fdef30980490d8ac15b64260803d5e29ad7b29915caeee09e6423</citedby><cites>FETCH-LOGICAL-c438t-a7e7859327d7fdef30980490d8ac15b64260803d5e29ad7b29915caeee09e6423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1800134077/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1800134077?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,725,778,782,883,25740,27911,27912,36999,37000,44577,53778,53780,74881</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27324189$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takáč, Tomáš</creatorcontrib><creatorcontrib>Vadovič, Pavol</creatorcontrib><creatorcontrib>Pechan, Tibor</creatorcontrib><creatorcontrib>Luptovčiak, Ivan</creatorcontrib><creatorcontrib>Šamajová, Olga</creatorcontrib><creatorcontrib>Šamaj, Jozef</creatorcontrib><title>Comparative proteomic study of Arabidopsis mutants mpk4 and mpk6</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Arabidopsis MPK4 and MPK6 are implicated in different signalling pathways responding to diverse external stimuli. This was recently correlated with transcriptomic profiles of Arabidopsis
mpk4
and
mpk6
mutants and thus it should be reflected also on the level of constitutive proteomes. Therefore, we performed a shot gun comparative proteomic analysis of Arabidopsis
mpk4
and
mpk6
mutant roots. We have used bioinformatic tools and propose several new proteins as putative MPK4 and MPK6 phosphorylation targets. Among these proteins in the
mpk6
mutant were important modulators of development such as CDC48A and phospholipase D alpha 1. In the case of the
mpk4
mutant transcriptional reprogramming might be mediated by phosphorylation and change in the abundance of mRNA decapping complex VCS. Further comparison of
mpk4
and
mpk6
root differential proteomes showed differences in the composition and regulation of defense related proteins. The
mpk4
mutant showed altered abundances of antioxidant proteins. The examination of catalase activity in response to oxidative stress revealed that this enzyme might be preferentially regulated by MPK4. Finally, we proposed developmentally important proteins as either directly or indirectly regulated by MPK4 and MPK6. These proteins contribute to known phenotypic defects in the
mpk4
and
mpk6
mutants.</description><subject>631/449/2661/2665</subject><subject>631/449/2675</subject><subject>82/1</subject><subject>82/58</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Catalase - metabolism</subject><subject>Cell division</subject><subject>Gene Knockout Techniques</subject><subject>Gene Ontology</subject><subject>Genes</subject><subject>Humanities and Social Sciences</subject><subject>Mitogen-Activated Protein Kinases - genetics</subject><subject>multidisciplinary</subject><subject>Mutants</subject><subject>Mutation, Missense</subject><subject>Ontology</subject><subject>Oxidative stress</subject><subject>Peroxidase - metabolism</subject><subject>Phosphorylation</subject><subject>Plant Roots - enzymology</subject><subject>Plant Roots - genetics</subject><subject>Protein Binding</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Proteome - metabolism</subject><subject>Proteomics</subject><subject>Receptors for Activated C Kinase - metabolism</subject><subject>Science</subject><subject>Stress, Physiological</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNplkU1LxDAQhoMoKurBPyAFLyqsTj7aJBdxWfyCBS96DtlmqtVtU5NW2H9vZHVZdS4z8D68M8NLyCGFcwpcXcSAHVMcig2yy0DkI8YZ21ybd8hBjK-QKmdaUL1NdpjkTFCld8nVxDedDbavPzDrgu_RN3WZxX5wi8xX2TjYWe18F-uYNUNv2z717k1ktnVfQ7FPtio7j3jw3ffI08314-RuNH24vZ-Mp6NScNWPrESpcs2ZdLJyWHHQCoQGp2xJ81khWAEKuMuRaevkjGlN89IiImhMKt8jl0vfbpg16Eps-2Dnpgt1Y8PCeFub30pbv5hn_2FEMgJaJIOTb4Pg3weMvWnqWOJ8blv0QzRUaqU1Y6ASevwHffVDaNN7hioAygVImajTJVUGH1MK1eoYCuYrGrOKJrFH69evyJ8gEnC2BGKS2mcMayv_uX0CvviXWw</recordid><startdate>20160621</startdate><enddate>20160621</enddate><creator>Takáč, Tomáš</creator><creator>Vadovič, Pavol</creator><creator>Pechan, Tibor</creator><creator>Luptovčiak, Ivan</creator><creator>Šamajová, Olga</creator><creator>Šamaj, Jozef</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160621</creationdate><title>Comparative proteomic study of Arabidopsis mutants mpk4 and mpk6</title><author>Takáč, Tomáš ; Vadovič, Pavol ; Pechan, Tibor ; Luptovčiak, Ivan ; Šamajová, Olga ; Šamaj, Jozef</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-a7e7859327d7fdef30980490d8ac15b64260803d5e29ad7b29915caeee09e6423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>631/449/2661/2665</topic><topic>631/449/2675</topic><topic>82/1</topic><topic>82/58</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Catalase - metabolism</topic><topic>Cell division</topic><topic>Gene Knockout Techniques</topic><topic>Gene Ontology</topic><topic>Genes</topic><topic>Humanities and Social Sciences</topic><topic>Mitogen-Activated Protein Kinases - genetics</topic><topic>multidisciplinary</topic><topic>Mutants</topic><topic>Mutation, Missense</topic><topic>Ontology</topic><topic>Oxidative stress</topic><topic>Peroxidase - metabolism</topic><topic>Phosphorylation</topic><topic>Plant Roots - enzymology</topic><topic>Plant Roots - genetics</topic><topic>Protein Binding</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Proteome - metabolism</topic><topic>Proteomics</topic><topic>Receptors for Activated C Kinase - metabolism</topic><topic>Science</topic><topic>Stress, Physiological</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takáč, Tomáš</creatorcontrib><creatorcontrib>Vadovič, Pavol</creatorcontrib><creatorcontrib>Pechan, Tibor</creatorcontrib><creatorcontrib>Luptovčiak, Ivan</creatorcontrib><creatorcontrib>Šamajová, Olga</creatorcontrib><creatorcontrib>Šamaj, Jozef</creatorcontrib><collection>SpringerOpen(OpenAccess)</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Databases</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takáč, Tomáš</au><au>Vadovič, Pavol</au><au>Pechan, Tibor</au><au>Luptovčiak, Ivan</au><au>Šamajová, Olga</au><au>Šamaj, Jozef</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative proteomic study of Arabidopsis mutants mpk4 and mpk6</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-06-21</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>28306</spage><epage>28306</epage><pages>28306-28306</pages><artnum>28306</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Arabidopsis MPK4 and MPK6 are implicated in different signalling pathways responding to diverse external stimuli. This was recently correlated with transcriptomic profiles of Arabidopsis
mpk4
and
mpk6
mutants and thus it should be reflected also on the level of constitutive proteomes. Therefore, we performed a shot gun comparative proteomic analysis of Arabidopsis
mpk4
and
mpk6
mutant roots. We have used bioinformatic tools and propose several new proteins as putative MPK4 and MPK6 phosphorylation targets. Among these proteins in the
mpk6
mutant were important modulators of development such as CDC48A and phospholipase D alpha 1. In the case of the
mpk4
mutant transcriptional reprogramming might be mediated by phosphorylation and change in the abundance of mRNA decapping complex VCS. Further comparison of
mpk4
and
mpk6
root differential proteomes showed differences in the composition and regulation of defense related proteins. The
mpk4
mutant showed altered abundances of antioxidant proteins. The examination of catalase activity in response to oxidative stress revealed that this enzyme might be preferentially regulated by MPK4. Finally, we proposed developmentally important proteins as either directly or indirectly regulated by MPK4 and MPK6. These proteins contribute to known phenotypic defects in the
mpk4
and
mpk6
mutants.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27324189</pmid><doi>10.1038/srep28306</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 631/449/2661/2665 631/449/2675 82/1 82/58 Amino Acid Sequence Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Binding Sites Catalase - metabolism Cell division Gene Knockout Techniques Gene Ontology Genes Humanities and Social Sciences Mitogen-Activated Protein Kinases - genetics multidisciplinary Mutants Mutation, Missense Ontology Oxidative stress Peroxidase - metabolism Phosphorylation Plant Roots - enzymology Plant Roots - genetics Protein Binding Protein Processing, Post-Translational Proteins Proteome - metabolism Proteomics Receptors for Activated C Kinase - metabolism Science Stress, Physiological |
title | Comparative proteomic study of Arabidopsis mutants mpk4 and mpk6 |
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