Phosphorylation of the Sendai virus C proteins.
We show that the Sendai virus C' and C proteins exist as both phosphorylated and nonphosphorylated forms, while the Y1 and Y2 proteins are not phosphorylated in virus-infected cells. Phosphorylation occurs primarily on serine residues, most likely at the N-terminus of the C' and C proteins. Phosphatases PP1 and PP2A significantly modulate the phosphorylation status of the C proteins as evidenced by okadaic acid inhibition of these phosphatases. The other Sendai virus proteins including the cotranslationally expressed P protein are not necessary for the appropriate phosphorylation of the C' and C proteins. Differential phosphorylation and potential for the modulation of phosphorylation suggests regulatory functions for the C proteins.
Hendricks
D D
DD
Department of Immunology/Microbiology, Rush Presbyterian St. Luke's Medical Center, Chicago, Illinois.
Ono
E
E
Seyer
J M
JM
Gupta
K C
KC
D000818:Animals; D001345:Autoradiography; D002460:Cell Line; D002522:Chlorocebus aethiops; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D007668:Kidney; D008970:Molecular Weight; D010222:Parainfluenza Virus 1, Human / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D012333:RNA, Messenger / Q000378:metabolism; D013462:Sulfur Radioisotopes; D014162:Transfection; D014764:Viral Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*
D010710:Phosphates; D010761:Phosphorus Radioisotopes; D012333:RNA, Messenger; D013462:Sulfur Radioisotopes; D014764:Viral Proteins; C051221:nonstructural C protein, Sendai virus