The protein kinase activity of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) fused to the extracellular domain of the epidermal growth factor receptor is ligand-inducible

Virology
C C SmithL Aurelian

Abstract

The gene coding for the large subunit of herpes simplex virus type 2 ribonucleotide reductase (RR) (ICP10) has a unique 5' terminal domain the product of which has a serine/threonine (Ser/Thr) protein kinase (PK) catalytic domain preceded by a transmembrane (TM) segment. Because ICP10 localizes on the cell surface and is internalized by the endocytic pathway like an activated growth factor receptor (Hunter et al., 1995, Virology 210, 345-360), we asked whether it is ligand-inducible in order to examine whether it has intrinsic transphosphorylating activity. We constructed a chimeric expression vector that contains the extracellular and TM domains of the epidermal growth factor receptor (EGFR) joined to the intracellular PK and RR domains of ICP10 (pCH5) and established constitutively expressing cell lines in NIH3T3 2.2 cells that do not express EGFR. The chimeric protein, designated p210 CH5, localized to the surface of these cells as determined by immunofluorescent staining with MAb EGFR, and it bound 125I-EGF.p210 CH5 coprecipitated with protein species p170, p120, p88, p60, p44, p34, and p25. EGF treatment activated the PK activity of p210 CH5, resulting in its autophosphorylation and the phosphorylation of the p120, p88, an...Continue Reading

Citations

Mar 23, 2010·Biochimica Et Biophysica Acta·Harilaos FilippakisGeorge Sourvinos
Dec 1, 2009·Viruses·Jesper MelchjorsenSøren R Paludan
Jan 20, 2005·The Biochemical Journal·Makoto HaseJunichi Sadoshima

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