Proteins That Interact with the Mucin-Type Glycoprotein Msb2p Include a Regulator of the Actin Cytoskeleton.
Identifieur interne : 000217 ( Main/Exploration ); précédent : 000216; suivant : 000218Proteins That Interact with the Mucin-Type Glycoprotein Msb2p Include a Regulator of the Actin Cytoskeleton.
Auteurs : Aditi Prabhakar [États-Unis] ; Nadia Vadaie [États-Unis] ; Thomas Krzystek [États-Unis] ; Paul J. Cullen [États-Unis]Source :
- Biochemistry [ 1520-4995 ] ; 2019.
Descripteurs français
- KwdFr :
- Cytosquelette d'actine (génétique), Cytosquelette d'actine (métabolisme), Domaines protéiques (MeSH), Liaison aux protéines (MeSH), Polarité de la cellule (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du cytosquelette (composition chimique), Protéines du cytosquelette (génétique), Protéines du cytosquelette (métabolisme), Protéines et peptides de signalisation intracellulaire (composition chimique), Protéines et peptides de signalisation intracellulaire (génétique), Protéines et peptides de signalisation intracellulaire (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (composition chimique), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Transduction du signal (MeSH).
- MESH :
- composition chimique : Protéines de Saccharomyces cerevisiae, Protéines du cytosquelette, Protéines et peptides de signalisation intracellulaire, Saccharomyces cerevisiae.
- cytologie : Saccharomyces cerevisiae.
- génétique : Cytosquelette d'actine, Protéines de Saccharomyces cerevisiae, Protéines du cytosquelette, Protéines et peptides de signalisation intracellulaire, Saccharomyces cerevisiae.
- métabolisme : Cytosquelette d'actine, Protéines de Saccharomyces cerevisiae, Protéines du cytosquelette, Protéines et peptides de signalisation intracellulaire, Saccharomyces cerevisiae.
- Domaines protéiques, Liaison aux protéines, Polarité de la cellule, Régulation de l'expression des gènes fongiques, Transduction du signal.
English descriptors
- KwdEn :
- Actin Cytoskeleton (genetics), Actin Cytoskeleton (metabolism), Cell Polarity (MeSH), Cytoskeletal Proteins (chemistry), Cytoskeletal Proteins (genetics), Cytoskeletal Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Intracellular Signaling Peptides and Proteins (chemistry), Intracellular Signaling Peptides and Proteins (genetics), Intracellular Signaling Peptides and Proteins (metabolism), Protein Binding (MeSH), Protein Domains (MeSH), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH).
- MESH :
- chemical , chemistry : Cytoskeletal Proteins, Intracellular Signaling Peptides and Proteins, Saccharomyces cerevisiae Proteins.
- chemistry : Saccharomyces cerevisiae.
- cytology : Saccharomyces cerevisiae.
- genetics : Actin Cytoskeleton, Cytoskeletal Proteins, Intracellular Signaling Peptides and Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins.
- metabolism : Actin Cytoskeleton, Cytoskeletal Proteins, Intracellular Signaling Peptides and Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins.
- Cell Polarity, Gene Expression Regulation, Fungal, Protein Binding, Protein Domains, Signal Transduction.
Abstract
Transmembrane mucin-type glycoproteins can regulate signal transduction pathways. In yeast, signaling mucins regulate mitogen-activated protein kinase (MAPK) pathways that induce cell differentiation to filamentous growth (fMAPK pathway) and the response to osmotic stress (HOG pathway). To explore regulatory aspects of signaling mucin function, protein microarrays were used to identify proteins that interact with the cytoplasmic domain of the mucin-like glycoprotein Msb2p. Eighteen proteins were identified that comprised functional categories of metabolism, actin filament capping and depolymerization, aerobic and anaerobic growth, chromatin organization and bud growth, sporulation, ribosome biogenesis, protein modification by iron-sulfur clusters, RNA catabolism, and DNA replication and DNA repair. A subunit of actin capping protein, Cap2p, interacted with the cytoplasmic domain of Msb2p. Cells lacking Cap2p showed altered localization of Msb2p and increased levels of shedding of Msb2p's N-terminal glycosylated domain. Consistent with its role in regulating the actin cytoskeleton, Cap2p was required for enhanced cell polarization during filamentous growth. Our study identifies proteins that connect a signaling mucin to diverse cellular processes and may provide insight into new aspects of mucin function.
DOI: 10.1021/acs.biochem.9b00725
PubMed: 31710471
Affiliations:
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Cullen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences , State University of New York at Buffalo , Buffalo , New York 14260-1300 , United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences , State University of New York at Buffalo , Buffalo , New York 14260-1300 </wicri:regionArea><wicri:noRegion>New York 14260-1300 </wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actin Cytoskeleton (genetics)</term><term>Actin Cytoskeleton (metabolism)</term><term>Cell Polarity (MeSH)</term><term>Cytoskeletal Proteins (chemistry)</term><term>Cytoskeletal Proteins (genetics)</term><term>Cytoskeletal Proteins (metabolism)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Intracellular Signaling Peptides and Proteins (chemistry)</term><term>Intracellular Signaling Peptides and Proteins (genetics)</term><term>Intracellular Signaling Peptides and Proteins (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Domains (MeSH)</term><term>Saccharomyces cerevisiae (chemistry)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (chemistry)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cytosquelette d'actine (génétique)</term><term>Cytosquelette d'actine (métabolisme)</term><term>Domaines protéiques (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Polarité de la cellule (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (composition chimique)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines du cytosquelette (composition chimique)</term><term>Protéines du cytosquelette (génétique)</term><term>Protéines du cytosquelette (métabolisme)</term><term>Protéines et peptides de signalisation intracellulaire (composition chimique)</term><term>Protéines et peptides de signalisation intracellulaire (génétique)</term><term>Protéines et peptides de signalisation intracellulaire (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (composition chimique)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cytoskeletal Proteins</term><term>Intracellular Signaling Peptides and Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du cytosquelette</term><term>Protéines et peptides de signalisation intracellulaire</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Actin Cytoskeleton</term><term>Cytoskeletal Proteins</term><term>Intracellular Signaling Peptides and Proteins</term><term>Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytosquelette d'actine</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du cytosquelette</term><term>Protéines et peptides de signalisation intracellulaire</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Actin Cytoskeleton</term><term>Cytoskeletal Proteins</term><term>Intracellular Signaling Peptides and Proteins</term><term>Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosquelette d'actine</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du cytosquelette</term><term>Protéines et peptides de signalisation intracellulaire</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Polarity</term><term>Gene Expression Regulation, Fungal</term><term>Protein Binding</term><term>Protein Domains</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Domaines protéiques</term><term>Liaison aux protéines</term><term>Polarité de la cellule</term><term>Régulation de l'expression des gènes fongiques</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Transmembrane mucin-type glycoproteins can regulate signal transduction pathways. In yeast, signaling mucins regulate mitogen-activated protein kinase (MAPK) pathways that induce cell differentiation to filamentous growth (fMAPK pathway) and the response to osmotic stress (HOG pathway). To explore regulatory aspects of signaling mucin function, protein microarrays were used to identify proteins that interact with the cytoplasmic domain of the mucin-like glycoprotein Msb2p. Eighteen proteins were identified that comprised functional categories of metabolism, actin filament capping and depolymerization, aerobic and anaerobic growth, chromatin organization and bud growth, sporulation, ribosome biogenesis, protein modification by iron-sulfur clusters, RNA catabolism, and DNA replication and DNA repair. A subunit of actin capping protein, Cap2p, interacted with the cytoplasmic domain of Msb2p. Cells lacking Cap2p showed altered localization of Msb2p and increased levels of shedding of Msb2p's N-terminal glycosylated domain. Consistent with its role in regulating the actin cytoskeleton, Cap2p was required for enhanced cell polarization during filamentous growth. Our study identifies proteins that connect a signaling mucin to diverse cellular processes and may provide insight into new aspects of mucin function.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31710471</PMID><DateCompleted><Year>2020</Year><Month>06</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>06</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>58</Volume><Issue>48</Issue><PubDate><Year>2019</Year><Month>12</Month><Day>03</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Proteins That Interact with the Mucin-Type Glycoprotein Msb2p Include a Regulator of the Actin Cytoskeleton.</ArticleTitle><Pagination><MedlinePgn>4842-4856</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.9b00725</ELocationID><Abstract><AbstractText>Transmembrane mucin-type glycoproteins can regulate signal transduction pathways. In yeast, signaling mucins regulate mitogen-activated protein kinase (MAPK) pathways that induce cell differentiation to filamentous growth (fMAPK pathway) and the response to osmotic stress (HOG pathway). To explore regulatory aspects of signaling mucin function, protein microarrays were used to identify proteins that interact with the cytoplasmic domain of the mucin-like glycoprotein Msb2p. Eighteen proteins were identified that comprised functional categories of metabolism, actin filament capping and depolymerization, aerobic and anaerobic growth, chromatin organization and bud growth, sporulation, ribosome biogenesis, protein modification by iron-sulfur clusters, RNA catabolism, and DNA replication and DNA repair. A subunit of actin capping protein, Cap2p, interacted with the cytoplasmic domain of Msb2p. Cells lacking Cap2p showed altered localization of Msb2p and increased levels of shedding of Msb2p's N-terminal glycosylated domain. Consistent with its role in regulating the actin cytoskeleton, Cap2p was required for enhanced cell polarization during filamentous growth. Our study identifies proteins that connect a signaling mucin to diverse cellular processes and may provide insight into new aspects of mucin function.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Prabhakar</LastName><ForeName>Aditi</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences , State University of New York at Buffalo , Buffalo , New York 14260-1300 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vadaie</LastName><ForeName>Nadia</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences , State University of New York at Buffalo , Buffalo , New York 14260-1300 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Krzystek</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences , State University of New York at Buffalo , Buffalo , New York 14260-1300 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cullen</LastName><ForeName>Paul J</ForeName><Initials>PJ</Initials><Identifier Source="ORCID">0000-0002-6703-1480</Identifier><AffiliationInfo><Affiliation>Department of Biological Sciences , State University of New York at Buffalo , Buffalo , New York 14260-1300 , United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United 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UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016764" MajorTopicYN="N">Cell Polarity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003598" MajorTopicYN="N">Cytoskeletal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047908" MajorTopicYN="N">Intracellular Signaling Peptides and Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31710471</ArticleId><ArticleId IdType="doi">10.1021/acs.biochem.9b00725</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Prabhakar, Aditi" sort="Prabhakar, Aditi" uniqKey="Prabhakar A" first="Aditi" last="Prabhakar">Aditi Prabhakar</name></noRegion><name sortKey="Cullen, Paul J" sort="Cullen, Paul J" uniqKey="Cullen P" first="Paul J" last="Cullen">Paul J. Cullen</name><name sortKey="Krzystek, Thomas" sort="Krzystek, Thomas" uniqKey="Krzystek T" first="Thomas" last="Krzystek">Thomas Krzystek</name><name sortKey="Vadaie, Nadia" sort="Vadaie, Nadia" uniqKey="Vadaie N" first="Nadia" last="Vadaie">Nadia Vadaie</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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