A novel, calcium-inhibitable casein kinase in Paramecium cells

Lade...
Vorschaubild
Dateien
A_novel.pdf
A_novel.pdfGröße: 1.14 MBDownloads: 263
Datum
1997
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
FEBS Letters. 1997, 402(2-3), pp. 227-235. ISSN 0014-5793. Available under: doi: 10.1016/S0014-5793(96)01539-6
Zusammenfassung

This is the first identification of a Ca2+-inhibitable casein kinase (CPK) which we have isolated from the 100 000×g supernatant of Paramecium cell homogenates. The 1000-fold enriched CPK activity depends on millimolar Mg2+ and is inhibited by low concentrations of heparin or by ≥100 μM Ca2+. Enzyme activity is stimulated by polylysine or polyarginine with either casein or with specific casein kinase-2 (CK-2) peptide substrates (RRRDDDSDDD and RREEETEEE). The enzymic properties are similar with GTP instead of ATP. CPK does not undergo autophosphorylation. In gel kinase assays, enzyme activity is associated with a 36 kDa band. Calmodulin as another characteristic substrate for mammalian CK-2 has not been phosphorylated by this protein kinase. Besides casein, CPK phosphorylates in vitro the catalytic subunit of bovine brain calcineurin (CaN), a typical substrate of type 1 mammalian casein kinase (CK-1) in vitro. Again this phosphorylation is significantly reduced by Ca2+. Thus, CPK combines aspects of different casein kinases, but it is clearly different from any type known by its Ca2+ inhibition. Since CPK also phosphorylates the exocytosis-sensitive phosphoprotein, PP63, in Paramecium, which is known to be dephosphorylated by CaN, an antagonistic Ca2+-effect during phosphorylation/dephosphorylation cycles may be relevant for exocytosis regulation.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Calcineurin, Calmodulin, Casein kinase, Exocytosis, Paramecium, Phosphorylation
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690KISSMEHL, Roland, Tilman TREPTAU, Karin HAUSER, Helmut PLATTNER, 1997. A novel, calcium-inhibitable casein kinase in Paramecium cells. In: FEBS Letters. 1997, 402(2-3), pp. 227-235. ISSN 0014-5793. Available under: doi: 10.1016/S0014-5793(96)01539-6
BibTex
@article{Kissmehl1997novel-6792,
  year={1997},
  doi={10.1016/S0014-5793(96)01539-6},
  title={A novel, calcium-inhibitable casein kinase in Paramecium cells},
  number={2-3},
  volume={402},
  issn={0014-5793},
  journal={FEBS Letters},
  pages={227--235},
  author={Kissmehl, Roland and Treptau, Tilman and Hauser, Karin and Plattner, Helmut}
}
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/123456789/6792">
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Hauser, Karin</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:contributor>Kissmehl, Roland</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Treptau, Tilman</dc:contributor>
    <dcterms:title>A novel, calcium-inhibitable casein kinase in Paramecium cells</dcterms:title>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:13Z</dc:date>
    <dcterms:abstract xml:lang="deu">This is the first identification of a Ca2+-inhibitable casein kinase (CPK) which we have isolated from the 100 000×g supernatant of Paramecium cell homogenates. The 1000-fold enriched CPK activity depends on millimolar Mg2+ and is inhibited by low concentrations of heparin or by ≥100 μM Ca2+. Enzyme activity is stimulated by polylysine or polyarginine with either casein or with specific casein kinase-2 (CK-2) peptide substrates (RRRDDDSDDD and RREEETEEE). The enzymic properties are similar with GTP instead of ATP. CPK does not undergo autophosphorylation. In gel kinase assays, enzyme activity is associated with a 36 kDa band. Calmodulin as another characteristic substrate for mammalian CK-2 has not been phosphorylated by this protein kinase. Besides casein, CPK phosphorylates in vitro the catalytic subunit of bovine brain calcineurin (CaN), a typical substrate of type 1 mammalian casein kinase (CK-1) in vitro. Again this phosphorylation is significantly reduced by Ca2+. Thus, CPK combines aspects of different casein kinases, but it is clearly different from any type known by its Ca2+ inhibition. Since CPK also phosphorylates the exocytosis-sensitive phosphoprotein, PP63, in Paramecium, which is known to be dephosphorylated by CaN, an antagonistic Ca2+-effect during phosphorylation/dephosphorylation cycles may be relevant for exocytosis regulation.</dcterms:abstract>
    <dcterms:bibliographicCitation>First publ. in: FEBS Letters ; 402 (1997). - S. 227-235</dcterms:bibliographicCitation>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6792/1/A_novel.pdf"/>
    <dc:creator>Kissmehl, Roland</dc:creator>
    <dc:creator>Treptau, Tilman</dc:creator>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6792/1/A_novel.pdf"/>
    <dc:contributor>Plattner, Helmut</dc:contributor>
    <dc:creator>Plattner, Helmut</dc:creator>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dcterms:issued>1997</dcterms:issued>
    <dc:creator>Hauser, Karin</dc:creator>
    <dc:format>application/pdf</dc:format>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:13Z</dcterms:available>
    <dc:language>deu</dc:language>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6792"/>
  </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
Nein
Begutachtet
Diese Publikation teilen