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J. Biol. Chem., Vol. 277, Issue 49, 47149-47159, December 6, 2002

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Molecular Examination of the Transmembrane Requirements of the Platelet-derived Growth Factor  Receptor for a Productive Interaction with the Bovine Papillomavirus E5 Oncoprotein^*

Valerie M. Nappi, Julia A. Schaefer, and Lisa M. Petti

From the Albany Medical College, Albany, New York 12208

The small transmembrane E5 protein of bovine papillomavirus (BPV) transforms cells by forming a stable complex with and activating the platelet-derived growth factor  receptor (PDGFR). The E5/PDGFR interaction is thought to involve specific physical contacts between the transmembrane domains of the two proteins. Lys⁴⁹⁹ at the extracellular juxtamembrane position and Thr⁵¹³ within the transmembrane domain of the PDGFR are required for the interaction and are predicted to contact analogously positioned residues in the E5 protein. Here, mutagenic analysis of the transmembrane region of the PDGFR was performed to further characterize the nature of the E5/PDGFR interaction. We show that the receptor transmembrane domain, with minimal extracellular and intracellular sequence, is sufficient for the interaction. In addition, we provide evidence that the polar nature of Thr⁵¹³ as well as its positioning along the transmembrane -helix is important for the interaction. We also identify the receptor transmembrane amino acids Ile⁵⁰⁶ and Leu⁵²⁰ as additional requirements for the interaction. Because Lys⁴⁹⁹, Thr⁵¹³, Ile⁵⁰⁶, and Leu⁵²⁰ all align along the same face of the predicted PDGFR transmembrane -helix, our data support the model that the PDGFR contacts the E5 protein via multiple amino acids along a single -helical interface.

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