Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes.
Identifieur interne : 001701 ( Main/Exploration ); précédent : 001700; suivant : 001702Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes.
Auteurs : Vaibhav Srivastava [Suède] ; Joseph R. Weber [États-Unis] ; Erik Malm [Suède] ; Bruce W. Fouke [États-Unis] ; Vincent Bulone [Australie]Source :
- Frontiers in plant science [ 1664-462X ] ; 2016.
Abstract
S-acylation is a reversible post-translational modification of proteins known to be involved in membrane targeting, subcellular trafficking, and the determination of a great variety of functional properties of proteins. The aim of this work was to identify S-acylated proteins in poplar. The use of an acyl-biotin exchange method and mass spectrometry allowed the identification of around 450 S-acylated proteins, which were subdivided into three major groups of proteins involved in transport, signal transduction, and response to stress, respectively. The largest group of S-acylated proteins was the protein kinase superfamily. Soluble N-ethylmaleimide-sensitive factor-activating protein receptors, band 7 family proteins and tetraspanins, all primarily related to intracellular trafficking, were also identified. In addition, cell wall related proteins, including cellulose synthases and other glucan synthases, were found to be S-acylated. Twenty four of the identified S-acylated proteins were also enriched in detergent-resistant membrane microdomains, suggesting S-acylation plays a key role in the localization of proteins to specialized plasma membrane subdomains. This dataset promises to enhance our current understanding of the various functions of S-acylated proteins in plants.
DOI: 10.3389/fpls.2016.00477
PubMed: 27148305
PubMed Central: PMC4828459
Affiliations:
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The aim of this work was to identify S-acylated proteins in poplar. The use of an acyl-biotin exchange method and mass spectrometry allowed the identification of around 450 S-acylated proteins, which were subdivided into three major groups of proteins involved in transport, signal transduction, and response to stress, respectively. The largest group of S-acylated proteins was the protein kinase superfamily. Soluble N-ethylmaleimide-sensitive factor-activating protein receptors, band 7 family proteins and tetraspanins, all primarily related to intracellular trafficking, were also identified. In addition, cell wall related proteins, including cellulose synthases and other glucan synthases, were found to be S-acylated. Twenty four of the identified S-acylated proteins were also enriched in detergent-resistant membrane microdomains, suggesting S-acylation plays a key role in the localization of proteins to specialized plasma membrane subdomains. This dataset promises to enhance our current understanding of the various functions of S-acylated proteins in plants. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">27148305</PMID><DateCompleted><Year>2016</Year><Month>05</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><PubDate><Year>2016</Year></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes.</ArticleTitle><Pagination><MedlinePgn>477</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2016.00477</ELocationID><Abstract><AbstractText>S-acylation is a reversible post-translational modification of proteins known to be involved in membrane targeting, subcellular trafficking, and the determination of a great variety of functional properties of proteins. The aim of this work was to identify S-acylated proteins in poplar. The use of an acyl-biotin exchange method and mass spectrometry allowed the identification of around 450 S-acylated proteins, which were subdivided into three major groups of proteins involved in transport, signal transduction, and response to stress, respectively. The largest group of S-acylated proteins was the protein kinase superfamily. Soluble N-ethylmaleimide-sensitive factor-activating protein receptors, band 7 family proteins and tetraspanins, all primarily related to intracellular trafficking, were also identified. In addition, cell wall related proteins, including cellulose synthases and other glucan synthases, were found to be S-acylated. Twenty four of the identified S-acylated proteins were also enriched in detergent-resistant membrane microdomains, suggesting S-acylation plays a key role in the localization of proteins to specialized plasma membrane subdomains. This dataset promises to enhance our current understanding of the various functions of S-acylated proteins in plants. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Srivastava</LastName><ForeName>Vaibhav</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weber</LastName><ForeName>Joseph R</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Roy J. Carver Biotechnology Centre, Institute for Genomic Biology, University of Illinois Urbana-Champaign Urbana, IL, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Malm</LastName><ForeName>Erik</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fouke</LastName><ForeName>Bruce W</ForeName><Initials>BW</Initials><AffiliationInfo><Affiliation>Roy J. 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IdType="pubmed">11115124</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>Suède</li><li>États-Unis</li></country><region><li>Illinois</li></region></list><tree><country name="Suède"><noRegion><name sortKey="Srivastava, Vaibhav" sort="Srivastava, Vaibhav" uniqKey="Srivastava V" first="Vaibhav" last="Srivastava">Vaibhav Srivastava</name></noRegion><name sortKey="Malm, Erik" sort="Malm, Erik" uniqKey="Malm E" first="Erik" last="Malm">Erik Malm</name></country><country name="États-Unis"><region name="Illinois"><name sortKey="Weber, Joseph R" sort="Weber, Joseph R" uniqKey="Weber J" first="Joseph R" last="Weber">Joseph R. Weber</name></region><name sortKey="Fouke, Bruce W" sort="Fouke, Bruce W" uniqKey="Fouke B" first="Bruce W" last="Fouke">Bruce W. Fouke</name></country><country name="Australie"><noRegion><name sortKey="Bulone, Vincent" sort="Bulone, Vincent" uniqKey="Bulone V" first="Vincent" last="Bulone">Vincent Bulone</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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