Phosphorylation of isolated plasma membranes of AH-66 hepatoma ascites cells by casein kinase 1.
The isolated plasma membranes of AH-66 hepatoma cells were phosphorylated by casein kinase 1 purified from the cytosol fraction of AH-66 cells. Casein kinase 2 purified from the same source had little effect on the phosphorylation of the plasma membranes. Two-dimensional gel electrophoresis and autoradiography showed that casein kinase 1 enhanced the phosphorylation of approx. 10 plasma membrane proteins that are phosphorylated only faintly in the isolated plasma membranes by endogenous protein kinase. Among these phosphoproteins, tubulin was identified as judged from their molecular weights and isoelectric points. These results suggest that one of the physiological functions of casein kinase 1 is phosphorylation of plasma membrane and plasma membrane-associated proteins.
Nakaya
K
K
Shinkawa
K
K
Nakajo
S
S
Nakamura
Y
Y
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001345:Autoradiography; D047388:Casein Kinases; D002462:Cell Membrane / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007527:Isoenzymes / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000648:ultrastructure*; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism
D000596:Amino Acids; D007527:Isoenzymes; D008565:Membrane Proteins; D014404:Tubulin; D011494:Protein Kinases; D047388:Casein Kinases; D011493:Protein Kinase C