Histidyl phosphorylation of P36 in rat hepatoma Fao cells in vitro and in vivo.
We have previously shown that a membrane-associated P36 from rat liver was in vitro phosphorylated at His residue(s) with a phosphoric amide bond (FEBS Lett., 319:75-79, 1993), and the activity was solubilized and partially purified (J. Biol. Chem., 269:9030-9037, 1994). The present study demonstrates that the P36 histidyl phosphorylation occurs in rat hepatoma cells under normal conditions. Phosphorylation and dephosphorylation of histidine as well as those of serine, threonine and tyrosine residues may also play an important role in animal cells.
Motojima
K
K
Department of Biochemistry, School of Pharmaceutical Sciences, Toho University, Chiba, Japan.
Passilly
P
P
Jannin
B
B
Latruffe
N
N
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D006639:Histidine / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D051381:Rats; D014407:Tumor Cells, Cultured
D008565:Membrane Proteins; D010761:Phosphorus Radioisotopes; D006639:Histidine