A novel, calcium-inhibitable casein kinase in Paramecium cells


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KISSMEHL, Roland, Tilman TREPTAU, Karin HAUSER, Helmut PLATTNER, 1997. A novel, calcium-inhibitable casein kinase in Paramecium cells. In: FEBS Letters. 402(2-3), pp. 227-235. ISSN 0014-5793

@article{Kissmehl1997novel-6792, title={A novel, calcium-inhibitable casein kinase in Paramecium cells}, year={1997}, doi={10.1016/S0014-5793(96)01539-6}, 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 xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/6792"> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:13Z</dcterms:available> <dcterms:title>A novel, calcium-inhibitable casein kinase in Paramecium cells</dcterms:title> <dc:creator>Kissmehl, Roland</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:13Z</dc:date> <dcterms:bibliographicCitation>First publ. in: FEBS Letters ; 402 (1997). - S. 227-235</dcterms:bibliographicCitation> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Treptau, Tilman</dc:contributor> <dc:creator>Treptau, Tilman</dc:creator> <dc:language>deu</dc:language> <dc:contributor>Hauser, Karin</dc:contributor> <dc:creator>Plattner, Helmut</dc:creator> <dc:contributor>Plattner, Helmut</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6792"/> <dcterms:issued>1997</dcterms:issued> <dc:format>application/pdf</dc:format> <dc:rights>deposit-license</dc:rights> <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> <dc:creator>Hauser, Karin</dc:creator> <dc:contributor>Kissmehl, Roland</dc:contributor> </rdf:Description> </rdf:RDF>

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