The human poliovirus receptor alpha is a serine phosphoprotein

James A. Bibb, Günter Bernhardt, Eckard Wimmer

Research output: Contribution to journalComment/debate

14 Scopus citations

Abstract

The human receptors for poliovirus (hPVR) are members of the immunoglobulin superfamily. Whereas the two membrane-bound isoforms, hPVRα and hPVRδ, share identical three-domain extracellular portions, their C- terminal cytoplasmic parts differ considerably. This feature is well conserved in the corresponding monkey proteins AGMα1, AGMδ1, and AGMα2. The cellular function of these proteins is presently unknown. In this short communication we report that hPVRα and possibly also AGMα1 and AGMα2, but not the δ 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.

Original languageEnglish (US)
Pages (from-to)6111-6115
Number of pages5
JournalJournal of virology
Volume68
Issue number9
StatePublished - Sep 1 1994

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'The human poliovirus receptor alpha is a serine phosphoprotein'. Together they form a unique fingerprint.

  • Cite this