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Echinobase
ECB-ART-36312
Biochem Biophys Res Commun 1996 Apr 25;2213:498-502. doi: 10.1006/bbrc.1996.0625.
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Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2.

Baldan B , Navazio L , Friso A , Mariani P , Meggio F .


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Calreticulin isolated from spinach leaves has been specifically phosphorylated in vitro by protein kinase CK2 while animal calreticulin from rabbit liver is not a substrate of this kinase under the same conditions. Phosphoserine is the only phosphoamino acid detected. High affinity binding (Km = 4.4 microM) and a nearly stoichiometric incorporation of phosphate was determined. Partially purified spinach calreticulin is phosphorylated at the same site(s) by a copurifying protein kinase sharing biochemical properties very similar if not identical to those of mammalian CK2. Other plant calreticulins isolated from Liriodendron tulipifera appear to be also phosphorylated by CK2.

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Genes referenced: LOC586799