The human poliovirus receptor alpha is a serine phosphoprotein.
The human receptors for poliovirus (hPVR) are members of the immunoglobulin superfamily. Whereas the two membrane-bound isoforms, hPVR alpha and hPVR delta, share identical three-domain extracellular portions, their C-terminal cytoplasmic parts differ considerably. This feature is well conserved in the corresponding monkey proteins AGM alpha 1, AGM delta 1, and AGM alpha 2. The cellular function of these proteins is presently unknown. In this short communication we report that hPVR alpha and possibly also AGM alpha 1 and AGM alpha 2, but not the delta isoforms, are phosphoproteins. The phosphorylation occurs at a serine in the cytoplasmic tails of these receptors. We further present evidence suggesting that the kinase responsible for the phosphorylation is calcium/calmodulin kinase II.
Bibb
J A
JA
Department of Microbiology, State University of New York at Stony Brook 11794-5222.
Bernhardt
G
G
Wimmer
E
E
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000378:metabolism*; D010768:Phosphoserine; D017955:Poliovirus / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D008565:Membrane Proteins; D010750:Phosphoproteins; D011991:Receptors, Virus; C066100:poliovirus receptor; D010768:Phosphoserine