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Updated: Aug 20, 2026

In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
Published on: July 23, 2010
Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived
Char-Chang Lai1, Anne P B Edwards, Daniel DiMaio
1Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA.
Abstract:
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.
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