Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase

Molecular Biology of the Cell

Volumn 11, Issue 10, 2000, Pages 3589-3599

  Bell, C A ^a   Tynan, J A ^a   Hart, K C ^a   Meyer, A N ^a   Robertson, S C ^a   Donoghue, D J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; FIBROBLAST GROWTH FACTOR RECEPTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; TYROSINE KINASE RECEPTOR;

ANIMAL CELL; ARTICLE; BREAST CANCER; CELL STRAIN 3T3; DIMERIZATION; ENZYME ACTIVATION; GENE MUTATION; IMMEDIATE EARLY GENE; LIGAND BINDING; MOUSE; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

EID: 0033786730     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.10.3589     Document Type: Article

References (53)

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2. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
3. Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene
4. Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
5. Correlation of the structure of the transmembrane domain of the neu oncogene-encoded p185 protein with its function
6. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
7. Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface
8. A subdomain in the transmembrane domain is necessary for p185(neu*) activation
9. High-efficiency transformation of mammalian cells by plasmid DNA
10. Transmembrane donk main sequence requirements for activation of the p185c-neu receptor tyrosine kinase
11. Constitutive activation of fibroblast growth factor receptor 3 by mutations responsible for the lethal skeletal dysplasia thanatophoric dysplasia type I
12. Distinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformation
13. c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK
14. Signaling by receptor tyrosine kinases
15. The erbB-2 mitogenic signaling pathway: Tyrosine phosphorylation of phospholipase C-γ and GTPase-activating protein does not correlate with erbB-2 mitogenic potency
16. SH2 and SH3 domains as molecular adhesives: The interactions of Crk and Abl
17. Phosphotyrosine phosphatases with SH2 domains: Regulators of signal transduction
18. Constitutive receptor activation by Crouzon syndrome mutations in fibroblast growth factor receptor (FGFR) 2 and FGFR2/Neu chimeras
19. Three dimensional structure of the transmembrane region of the proto-oncogenic and oncogenic forms of the neu protein
20. Dimerization of cell surface receptors in signal transduction
21. Protein tyrosine kinase receptors
22. Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors
23. Binding of NCK to SOS and activation of ras-dependent gene expression
24. Identification of a 13 amino acid peptide mimetic of erythropoietin and description of amino acids critical for the mimetic activity of EMP1
25. Constitutively activating mutations of c-kit receptor tyrosine kinase confer factor-independent growth and tumorigenicity of factor-dependent hematopoietic cell lines
26. Modular peptide recognition domains in eukaryotic signaling
27. An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation
28. Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 angstrom
29. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
30. Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with acanthosis nigricans
31. Mutations of c-kit JM domain are found in a minority of human gastrointestinal stromal tumors
32. Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia
33. Oncogenic activation of the PDGF beta receptor by the transmembrane domain of p185(neu*)
34. Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions
35. Intermolecular association and trans-phosphorylation of different neu-kinase forms permit SH2-dependent signaling and oncogenic transformation
36. Mutations in the gene encoding fibroblast growth factor receptor-3 in achondroplasia
37. Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B
38. Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism; achondroplasia
39. Tyrosine kinases: Modular signaling enzymes with tunable specificities
40. Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors
41. Strong hydrogen bonding interactions involving a buried glutamic acid in the trans membrane sequence of the neu/erbB-2 receptor
42. Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond
43. Neu receptor dimerization
44. A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization
45. Signal transduction by receptors with tyrosine kinase activity
46. Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia
47. FGFR activation in skeletal disorders: Too much of a good thing
48. A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
49. Switching signals on or off by receptor dimerization
50. Novel mechanisms of RTK signal generation
51. Signal transduction by the platelet-derived growth factor receptor
52. Tyrosine phosphorylation of Shc proteins and formation of Shc/Grb2 complex correlate to the transformation of NIH3T3 cells mediated by the point-mutation activated neu
53. Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors