A novel, calcium-inhibitable casein kinase in Paramecium cells
A novel, calcium-inhibitable casein kinase in Paramecium cells
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1997
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FEBS Letters ; 402 (1997), 2-3. - pp. 227-235. - ISSN 0014-5793
Abstract
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.
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570 Biosciences, Biology
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Calcineurin,Calmodulin,Casein kinase,Exocytosis,Paramecium,Phosphorylation
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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. Available under: doi: 10.1016/S0014-5793(96)01539-6BibTex
@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} }
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