Multiple transmembrane amino acid requirements suggest a highly specific interaction between the bovine papillomavirus E5 oncoprotein and the platelet-derived growth factor beta receptor

Journal of Virology

Volumn 76, Issue 16, 2002, Pages 7976-7986

  Nappi, Valerie M ^a   Petti, Lisa M ^a  

^a ALBANY MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ONCOPROTEIN; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR BETA RECEPTOR; PROTEIN TYROSINE KINASE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIMERIZATION; MOUSE; NONHUMAN; PAPILLOMA VIRUS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; BOVINE PAPILLOMAVIRUS 1; CATTLE; CELL LINE; LYSINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; ONCOGENE PROTEINS, VIRAL; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, PLATELET-DERIVED GROWTH FACTOR BETA; RECOMBINANT FUSION PROTEINS; THREONINE;

EID: 0036311546     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.16.7976-7986.2002     Document Type: Article

References (39)

1. The E5 gene of bovine papillomavirus type 1 is sufficient for complete oncogenic transformation of mouse fibroblasts
2. Genetic and biochemical definition of the bovine papillomavirus E5 transforming protein
3. The E5 oncoprotein of bovine papillomavirus is oriented asymmetrically in Golgi and plasma membranes
4. Platelet-derived growth factor receptor signals
5. The conserved C-terminal domain of the bovine papillomavirus E5 oncoprotein can associate with an alpha-adaptin-like molecule: A possible link between growth factor receptors and viral transformation
6. Transformation-specific interaction of the bovine papillomavirus E5 oncoprotein with the platelet-derived growth factor receptor transmembrane domain and the epidermal growth factor receptor cytoplasmic domain
7. Translation of open reading frame E5 of bovine papillomavirus is required for its transforming activity
8. Ligand-independent activation of the platelet derived growth factor beta receptor: Requirements for bovine papillomavirus E5-induced mitogenic signaling
9. Amplification and/or overexpression of platelet-derived growth factor receptors and epidermal growth factor receptor in human glial tumors
10. The E5 oncoprotein of bovine papillomavirus binds to a 16 κDa cellular protein
11. +-ATPases
12. The bovine papillomavirus-1 E5 protein, the 16 κDa membrane pore-forming protein and the PDGF receptor exist in a complex that is dependent on hydrophobic transmembrane interactions
13. The bovine papillomavirus type 1 E5 transforming protein specifically binds and activates the beta-type receptor for the platelet-derived growth factor but not other related tyrosine kinase-containing receptors to induce cellular transformation
14. Dimerization of cell surface receptors in signal transduction
15. 44-Amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids
16. Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor beta receptor activation and cell transformation
17. The bovine papillomavirus E5 protein requires a juxtamembrane negative charge for activation of the platelet-derived growth factor beta receptor and transformation of C127 cells
18. The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
19. Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor beta receptor
20. Sequence specificity in the dimerization of transmembrane alpha-helices
21. Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices
22. Specificity and promiscuity in membrane helix interactions
23. A dimerization motif for transmembrane alpha-helices
24. The bovine papillomavirus E5 transforming protein can stimulate the transforming activity of EGF and CSF-1 receptors
25. Cellular transformation by a transmembrane peptide: Structural requirements for the bovine papillomavirus E5 oncoprotein
26. Platelet-derived growth factor receptor can mediate tumorigenic transformation by the bovine papillomavirus E5 protein
27. Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells
28. 11-3-Dependent mouse clones that express B-220 surface antigen, contain 1g genes in germ-line configuration, and generate B lymphocytes in vivo
29. Activation of the platelet-derived growth factor receptor by the bovine papillomavirus E5 transforming protein
30. Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells
31. Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells
32. Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein
33. Transformation of mortal human fibroblasts and activation of a growth inhibitory pathway by the bovine papillomavirus E5 oncoprotein
34. E5 open reading frame of bovine papillomavirus type 1 encodes a transforming gene
35. The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic polypeptide
36. The glycophorin A transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helices
37. Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus
38. Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors
39. Interhelical hydrogen bonding drives strong interactions in membrane proteins