Generation and characterization of a novel, permanently active S100P mutant

Lade...
Vorschaubild
Dateien
Zu diesem Dokument gibt es keine Dateien.
Datum
2009
Autor:innen
Austermann, Judith
Nazmi, Ali Reza
Heil, Annika
Kolinski, Michal
Filipek, Slawomir
Gerke, Volker
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Elsevier. 2009, 1793(6), pp. 1078-1085. ISSN 0167-4889. eISSN 1879-2596. Available under: doi: 10.1016/j.bbamcr.2008.11.012
Zusammenfassung

S100 proteins function as Ca2+ signal transducers by regulating cellular targets in their Ca2+ bound conformation. S100P is a member of the S100 protein family that can activate the membrane and F-actin binding protein ezrin in a Ca2+ dependent manner at least in vitro. Here we generated a novel tool to elucidate directly the S100P–ezrin interaction in vivo. This was achieved by constructing a S100P derivative that contained mutations in the two EF hand loops predicted to lock the protein in a permanently active state. The resulting S100P mutant, termed here S100P pa, could be purified as a soluble protein and showed biochemical properties displayed by wild-type S100P only in the presence of Ca2+. Importantly, S100P pa bound to the N-terminal domain of ezrin in the absence of Ca2+ showing an affinity only slightly reduced as compared to that of Ca2+-bound WT S100P. In line with this permanent complex formation, S100P pa colocalized with ezrin to plasma membrane protrusions of epithelial cells even in the absence of intracellular Ca2+ transients. Thus, S100P pa is a novel type of S100 protein mutant locked in a permanently active state that shows an unregulated complex formation with its cellular target ezrin.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690AUSTERMANN, Judith, Ali Reza NAZMI, Annika HEIL, Günter FRITZ, Michal KOLINSKI, Slawomir FILIPEK, Volker GERKE, 2009. Generation and characterization of a novel, permanently active S100P mutant. In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Elsevier. 2009, 1793(6), pp. 1078-1085. ISSN 0167-4889. eISSN 1879-2596. Available under: doi: 10.1016/j.bbamcr.2008.11.012
BibTex
@article{Austermann2009-06Gener-58103,
  year={2009},
  doi={10.1016/j.bbamcr.2008.11.012},
  title={Generation and characterization of a novel, permanently active S100P mutant},
  number={6},
  volume={1793},
  issn={0167-4889},
  journal={Biochimica et Biophysica Acta (BBA) - Molecular Cell Research},
  pages={1078--1085},
  author={Austermann, Judith and Nazmi, Ali Reza and Heil, Annika and Fritz, Günter and Kolinski, Michal and Filipek, Slawomir and Gerke, Volker}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/58103">
    <dc:contributor>Fritz, Günter</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-07-21T06:40:38Z</dc:date>
    <dcterms:abstract xml:lang="eng">S100 proteins function as Ca&lt;sup&gt;2+&lt;/sup&gt; signal transducers by regulating cellular targets in their Ca&lt;sup&gt;2+&lt;/sup&gt; bound conformation. S100P is a member of the S100 protein family that can activate the membrane and F-actin binding protein ezrin in a Ca&lt;sup&gt;2+&lt;/sup&gt; dependent manner at least in vitro. Here we generated a novel tool to elucidate directly the S100P–ezrin interaction in vivo. This was achieved by constructing a S100P derivative that contained mutations in the two EF hand loops predicted to lock the protein in a permanently active state. The resulting S100P mutant, termed here S100P pa, could be purified as a soluble protein and showed biochemical properties displayed by wild-type S100P only in the presence of Ca&lt;sup&gt;2+&lt;/sup&gt;. Importantly, S100P pa bound to the N-terminal domain of ezrin in the absence of Ca&lt;sup&gt;2+&lt;/sup&gt; showing an affinity only slightly reduced as compared to that of Ca&lt;sup&gt;2+&lt;/sup&gt;-bound WT S100P. In line with this permanent complex formation, S100P pa colocalized with ezrin to plasma membrane protrusions of epithelial cells even in the absence of intracellular Ca&lt;sup&gt;2+&lt;/sup&gt; transients. Thus, S100P pa is a novel type of S100 protein mutant locked in a permanently active state that shows an unregulated complex formation with its cellular target ezrin.</dcterms:abstract>
    <dc:creator>Austermann, Judith</dc:creator>
    <dc:creator>Nazmi, Ali Reza</dc:creator>
    <dcterms:issued>2009-06</dcterms:issued>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-07-21T06:40:38Z</dcterms:available>
    <dc:creator>Filipek, Slawomir</dc:creator>
    <dc:contributor>Heil, Annika</dc:contributor>
    <dc:creator>Gerke, Volker</dc:creator>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/58103"/>
    <dcterms:title>Generation and characterization of a novel, permanently active S100P mutant</dcterms:title>
    <dc:creator>Fritz, Günter</dc:creator>
    <dc:contributor>Gerke, Volker</dc:contributor>
    <dc:contributor>Austermann, Judith</dc:contributor>
    <dc:contributor>Kolinski, Michal</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Heil, Annika</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Kolinski, Michal</dc:creator>
    <dc:contributor>Nazmi, Ali Reza</dc:contributor>
    <dc:contributor>Filipek, Slawomir</dc:contributor>
    <dc:language>eng</dc:language>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Ja
Diese Publikation teilen