A novel, calcium-inhibitable casein kinase in Paramecium cells

Kissmehl, Roland; Treptau, Tilman; Hauser, Karin; Plattner, Helmut

A novel, calcium-inhibitable casein kinase in Paramecium cells

Dateien

A_novel.pdfGröße: 1.14 MBDownloads: 253

Datum

1997

Autor:innen

Kissmehl, Roland

Treptau, Tilman

Hauser, Karin

Plattner, Helmut

Publikationstyp

Zeitschriftenartikel

unikn.publication.listelement.citation.prefix.version.undefined

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.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Calcineurin, Calmodulin, Casein kinase, Exocytosis, Paramecium, Phosphorylation

Zitieren

ISO 690

KISSMEHL, 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>

Universitätsbibliographie

Nein