Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor.
The bovine papillomavirus E5 protein is a 44-amino-acid transmembrane protein that transforms cells by binding to the transmembrane region of the cellular platelet-derived growth factor (PDGF) beta receptor, resulting in sustained receptor signaling. However, there are published reports that certain mutants with amino acid substitutions in the membrane-spanning segment of the E5 protein transform cells without activating the PDGF beta receptor. We re-examined several of these transmembrane mutants, and here we present five lines of evidence that these mutants do in fact activate the PDGF beta receptor, resulting in cellular signaling and transformation.
Lai
Char-Chang
CC
Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
Edwards
Anne P B
AP
DiMaio
Daniel
D
D000818:Animals; D052688:Bovine papillomavirus 1 / Q000378:metabolism; D002417:Cattle; D002460:Cell Line; D002461:Cell Line, Transformed; D002472:Cell Transformation, Viral; D051379:Mice; D020125:Mutation, Missense; D041681:NIH 3T3 Cells; D009856:Oncogene Proteins, Viral / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D020797:Receptor, Platelet-Derived Growth Factor beta / Q000378:metabolism*; D015398:Signal Transduction; D014443:Tyrosine / Q000378:metabolism
D009856:Oncogene Proteins, Viral; C054304:oncogene protein E5, Bovine papillomavirus type 1; D014443:Tyrosine; D020797:Receptor, Platelet-Derived Growth Factor beta