This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nappi, V. M.
Right arrow Articles by Petti, L. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nappi, V. M.
Right arrow Articles by Petti, L. M.

 Previous Article  |  Next Article 

Journal of Virology, August 2002, p. 7976-7986, Vol. 76, No. 16
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.16.7976-7986.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Multiple Transmembrane Amino Acid Requirements Suggest a Highly Specific Interaction between the Bovine Papillomavirus E5 Oncoprotein and the Platelet-Derived Growth Factor Beta Receptor

Valerie M. Nappi and Lisa M. Petti*

Center for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208

Received 26 February 2002/ Accepted 16 May 2002

The bovine papillomavirus E5 protein activates the cellular platelet-derived growth factor ß receptor (PDGFßR) tyrosine kinase in a ligand-independent manner. Evidence suggests that the small transmembrane E5 protein homodimerizes and physically interacts with the transmembrane domain of the PDGFßR, thereby inducing constitutive dimerization and activation of this receptor. Amino acids in the receptor previously found to be required for the PDGFßR-E5 interaction are a transmembrane Thr513 and a juxtamembrane Lys499. Here, we sought to determine if these are the only two receptor amino acids required for an interaction with the E5 protein. Substitution of large portions of the PDGFßR transmembrane domain indicated that additional amino acids in both the amino and carboxyl halves of the receptor transmembrane domain are required for a productive interaction with the E5 protein. Indeed, individual amino acid substitutions in the receptor transmembrane domain identified roles for the extracellular proximal transmembrane residues in the interaction. These data suggest that multiple amino acids within the transmembrane domain of the PDGFßR are required for a stable interaction with the E5 protein. These may be involved in direct protein-protein contacts or may support the proper transmembrane alpha-helical conformation for optimal positioning of the primary amino acid requirements.

* Corresponding author. Mailing address: Center for Immunology and Microbial Disease, MC-151, Albany Medical College, 47 New Scotland Ave., Albany, NY 12208. Phone: (518) 262-6285. Fax: (518) 262-5748. E-mail: pettil{at}mail.amc.edu.

Journal of Virology, August 2002, p. 7976-7986, Vol. 76, No. 16
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.16.7976-7986.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Petti, L. M., Ricciardi, E. C., Page, H. J., Porter, K. A. (2008). Transforming signals resulting from sustained activation of the PDGF{beta} receptor in mortal human fibroblasts. J. Cell Sci. 121: 1172-1182 [Abstract] [Full Text]  
  • Ptacek, J. B., Edwards, A. P. B., Freeman-Cook, L. L., DiMaio, D. (2007). Packing contacts can mediate highly specific interactions between artificial transmembrane proteins and the PDGFbeta receptor. Proc. Natl. Acad. Sci. USA 104: 11945-11950 [Abstract] [Full Text]  
  • Nappi, V. M., Schaefer, J. A., Petti, L. M. (2002). Molecular Examination of the Transmembrane Requirements of the Platelet-derived Growth Factor beta Receptor for a Productive Interaction with the Bovine Papillomavirus E5 Oncoprotein. J. Biol. Chem. 277: 47149-47159 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»