Phosphorylation of muscle and non-muscle actins by casein kinase 1 in vitro.
Skeletal muscle and Physarum actins were markedly phosphorylated by casein kinase 1, but not by casein kinase 2. The amount of radioactive phosphate incorporated into muscle actin with 110 units of casein kinase 1 was approx. 0.2 mol per mol of actin, which was significantly greater than those catalyzed using the same number of enzyme units of protein kinase A or protein kinase C. The Km values of casein kinase 1 for muscle and Physarum actins were 0.270 and 0.667 mg/ml, respectively.
Shibayama
T
T
Shinkawa
K
K
Nakajo
S
S
Nakaya
K
K
Nakamura
Y
Y
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology; D047388:Casein Kinases; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008114:Liver Neoplasms, Experimental; D009132:Muscles / Q000378:metabolism*; D010766:Phosphorylation; D010804:Physarum / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D000199:Actins; D011494:Protein Kinases; D047388:Casein Kinases; D011493:Protein Kinase C