Phosphorylation of avian retrovirus matrix protein by Ca2+/phospholipid‐dependent protein kinase

Jonathan LEIS*, Nelson PHILLIPS, Xiangdong FU, Polygena T. TUAZON, Jolinda A. TRAUGH

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

The matrix protein from avian myeloblastosis virus and the Rous sarcoma virus, Prague C strain, is a phosphoprotein. A comparison of the amino acid sequences shows these phosphoproteins are very similar. The sites of phosphorylation of the matrix protein purified from virions are identified as serine residues 68 and 106. Treatment with purified rabbit skeletal‐muscle protein phosphatase 1 or 2A, selectively releases phosphate from serine 68, while alkali treatment releases phosphate from both sites. When analyzed as a substrate for six different protein kinases, only the Ca2+/phospholipid‐dependent protein kinase modifies the matrix protein. The serine residues phosphorylated in vivo are identical to those phosphorylated in vitro by this protein kinase. The role of these phosphorylation events in viral production is discussed.

Original languageEnglish (US)
Pages (from-to)415-422
Number of pages8
JournalEuropean Journal of Biochemistry
Volume179
Issue number2
DOIs
StatePublished - Feb 1989

ASJC Scopus subject areas

  • Biochemistry

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