The general recognition motif for phsophorylation by CK2 is SXXE/D, although SXE/D and S/D, and variations of these sequences are also phosphorylated. The CK2 substrate specificity is invariably determined by multiple acidic residues located at positions between -2 and +5 relative to the target amino acid (mostly Ser and rarely Thr). coli expressing both α and β CK2 subunits derived from a human glioblastoma cDNA library (kindly provided by Dr. CK2 is implicated in a variety of cellular functions (1,2). Also, CK2 is able to phosphorylate, under special circumstances, tyrosyl residues in proteins. Recently it has been shown that CK2 α-subunits undergo intermolecular tyrosine-autophosphorylation at Y182, which may represent a specific regulatory mechanism. CK2 holoenzyme undergoes autophosphorylation at two serine residues (S2/S3) of its β-subunit. Casein Kinase II (CK2) is a constitutively active serine/threonine protein kinase composed of two 44 kDa catalytic α-subunits and two 26 kDa regulatory β-subunits in an α 2β 2 configuration to form stable heterotetramers.
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