KIDs rule: Regulatory phosphorylation of RTKs

Trends in Biochemical Sciences

Volumn 38, Issue 2, 2013, Pages 75-84

  Locascio, Lauren E ^a   Donoghue, Daniel J ^a  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

Cellular signaling; Kinase insert domain; Phosphorylation; Receptor tyrosine kinases

Indexed keywords

EPIDERMAL GROWTH FACTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 1; FIBROBLAST GROWTH FACTOR RECEPTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR 3; PLATELET DERIVED GROWTH FACTOR; PROTEIN RET; PROTEIN TYROSINE KINASE; RECEPTOR TYROSINE KINASE LIKE ORPHAN RECEPTOR; SERINE; TYROSINE; TYROSINE KINASE RECEPTOR; VASCULOTROPIN RECEPTOR 1; VASCULOTROPIN RECEPTOR 2;

AUTOPHOSPHORYLATION; BINDING SITE; CELL DIFFERENTIATION; CELL GROWTH; CHEMOTAXIS; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; REVIEW;

AMINO ACID SEQUENCE; BINDING SITES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR PROTEIN-TYROSINE KINASES; SIGNAL TRANSDUCTION;

EID: 84872796862     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2012.12.001     Document Type: Review

References (69)

1. Lemmon M.A., Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010, 141:1117-1134.
2. Robertson S.C., et al. RTK mutations and human syndromes: when good receptors turn bad. Trends Genet. 2000, 16:265-271.
3. Shamah S.M., et al. Detection of activated platelet-derived growth factor receptors in human meningioma. Cancer Res. 1997, 57:4141-4147.
4. Wouters V., et al. Hereditary cutaneomucosal venous malformations are caused by TIE2 mutations with widely variable hyper-phosphorylating effects. Eur. J. Hum. Genet. 2010, 18:414-420.
5. Gschwind A., et al. The discovery of receptor tyrosine kinases: targets for cancer therapy. Nat. Rev. Cancer 2004, 4:361-370.
6. Heldin C.H., et al. Signal transduction via platelet-derived growth factor receptors. Biochim. Biophys. Acta 1998, 1378:F79-F113.
7. Claesson-Welsh L. Platelet-derived growth factor receptor signals. J. Biol. Chem. 1994, 269:32023-32026.
8. Kelly J.D., et al. Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation. J. Biol. Chem. 1991, 266:8987-8992.
9. Escobedo J.A., Williams L.T. A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF. Nature 1988, 335:85-87.
10. Wennstrom S., et al. Membrane ruffling and chemotaxis transduced by the PDGF beta-receptor require the binding site for phosphatidylinositol 3' kinase. Oncogene 1994, 9:651-660.
11. Kazlauskas A., et al. GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit. Mol. Cell Biol. 1992, 12:2534-2544.
12. Bae Y.S., et al. Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase. J. Biol. Chem. 2000, 275:10527-10531.
13. Mitchell D., et al. The lipoxin A4 receptor is coupled to SHP-2 activation: implications for regulation of receptor tyrosine kinases. J. Biol. Chem. 2007, 282:15606-15618.
14. Lennartsson J., et al. Erk 5 is necessary for sustained PDGF-induced Akt phosphorylation and inhibition of apoptosis. Cell. Signal. 2010, 22:955-960.
15. Ruusala A., et al. Nck adapters are involved in the formation of dorsal ruffles, cell migration, and Rho signaling downstream of the platelet-derived growth factor beta receptor. J. Biol. Chem. 2008, 283:30034-30044.
16. Chen M., et al. Nckβ adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb. Mol. Cell. Biol. 2000, 20:7867-7880.
17. Nishimura R., et al. Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor. Mol. Cell Biol. 1993, 13:6889-6896.
18. Panayotou G., et al. Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J. 1992, 11:4261-4272.
19. Ronnstrand L., et al. SHP-2 binds to Tyr763 and Tyr1009 in the PDGF β-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis. Oncogene 1999, 18:3696-3702.
20. Ruusala A., et al. Platelet-derived growth factor (PDGF)-induced actin rearrangement is deregulated in cells expressing a mutant Y778F PDGF β-receptor. J. Cell Sci. 1998, 111:111-120.
21. Arvidsson A.K., et al. Tyr-716 in the platelet-derived growth factor β-receptor kinase insert is involved in GRB2 binding and Ras activation. Mol. Cell Biol. 1994, 14:6715-6726.
22. Heuchel R., et al. Platelet-derived growth factor β receptor regulates interstitial fluid homeostasis through phosphatidylinositol-3' kinase signaling. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:11410-11415.
23. Heidaran M.A., et al. Deletion or substitution within the α platelet-derived growth factor receptor kinase insert domain: effects on functional coupling with intracellular signaling pathways. Mol. Cell Biol. 1991, 11:134-142.
24. Hooshmand-Rad R., et al. Platelet-derived growth factor-mediated signaling through the Shb adaptor protein: effects on cytoskeletal organization. Exp. Cell Res. 2000, 257:245-254.
25. Bazenet C.E., et al. Phosphorylation of tyrosine 720 in the platelet-derived growth factor α receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation. Mol. Cell Biol. 1996, 16:6926-6936.
26. Matsumoto T., et al. Differential interaction of CrkII adaptor protein with platelet-derived growth factor α- and β-receptors is determined by its internal tyrosine phosphorylation. Biochem. Biophys. Res. Commun. 2000, 270:28-33.
27. Yokote K., et al. Identification of Tyr-762 in the platelet-derived growth factor α-receptor as the binding site for Crk proteins. Oncogene 1998, 16:1229-1239.
28. Bourette R.P., et al. Suppressor of cytokine signaling 1 interacts with the macrophage colony-stimulating factor receptor and negatively regulates its proliferation signal. J. Biol. Chem. 2001, 276:22133-22139.
29. Rohrschneider L.R., et al. Growth and differentiation signals regulated by the M-CSF receptor. Mol. Reprod. Dev. 1997, 46:96-103.
30. van der Geer P., Hunter T. Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding site, abrogates signal transduction by the murine CSF-1 receptor expressed in Rat-2 fibroblasts. EMBO J. 1993, 12:5161-5172.
31. Joos H., et al. Tyrosine phosphorylation of the juxtamembrane domain of the v-Fms oncogene product is required for its association with a 55-kDa protein. J. Biol. Chem. 1996, 271:24476-24481.
32. Mancini A., et al. Identification of a second Grb2 binding site in the v-Fms tyrosine kinase. Oncogene 1997, 15:1565-1572.
33. Flick M.B., et al. Recognition of activated CSF-1 receptor in breast carcinomas by a tyrosine 723 phosphospecific antibody. Oncogene 1997, 14:2553-2561.
34. Thommes K., et al. Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor. Biochem. J. 1999, 341:211-216.
35. Roskoski R. Signaling by Kit protein-tyrosine kinase - the stem cell factor receptor. Biochem. Biophys. Res. Commun. 2005, 337:1-13.
36. Serve H., et al. Tyrosine residue 719 of the c-kit receptor is essential for binding of the P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-kit-associated PI 3-kinase activity in COS-1 cells. J. Biol. Chem. 1994, 269:6026-6030.
37. Blume-Jensen P., et al. Identification of the major phosphorylation sites for protein kinase C in kit/stem cell factor receptor in vitro and in intact cells. J. Biol. Chem. 1995, 270:14192-14200.
38. Edling C.E., et al. Haematopoietic progenitor cells utilise conventional PKC to suppress PKB/Akt activity in response to c-Kit stimulation. Br. J. Haematol. 2007, 136:260-268.
39. Sambol E.B., et al. Flavopiridol targets c-KIT transcription and induces apoptosis in gastrointestinal stromal tumor cells. Cancer Res. 2006, 66:5858-5866.
40. Maulik G., et al. Modulation of c-Kit/SCF pathway leads to alterations in topoisomerase-I activity in small cell lung cancer. J. Environ. Pathol. Toxicol. Oncol. 2004, 23:237-251.
41. Koch S., et al. Signal transduction by vascular endothelial growth factor receptors. Biochem. J. 2011, 437:169-183.
42. Holmes K., et al. Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition. Cell Signal. 2007, 19:2003-2012.
43. Sinha S., et al. Dopamine regulates phosphorylation of VEGF receptor 2 by engaging Src-homology-2-domain-containing protein tyrosine phosphatase 2. J. Cell Sci. 2009, 122:3385-3392.
44. D'Souza S., et al. HIP/RPL29 antagonizes VEGF and FGF2 stimulated angiogenesis by interfering with HS-dependent responses. J. Cell Biochem. 2008, 105:1183-1193.
45. Olszewska-Pazdrak B., et al. Chronic hypoxia attenuates VEGF signaling and angiogenic responses by downregulation of KDR in human endothelial cells. Am. J. Physiol. Cell Physiol. 2009, 296:C1162-C1170.
46. Tahir S.A., et al. Caveolin-1 regulates VEGF-stimulated angiogenic activities in prostate cancer and endothelial cells. Cancer Biol. Ther. 2009, 8:2286-2296.
47. Wedam S.B., et al. Antiangiogenic and antitumor effects of bevacizumab in patients with inflammatory and locally advanced breast cancer. J. Clin. Oncol. 2006, 24:769-777.
48. Strochlic L., et al. The synaptic muscle-specific kinase (MuSK) complex: new partners, new functions. Bioessays 2005, 27:1129-1135.
49. Till J.H., et al. Crystal structure of the MuSK tyrosine kinase: insights into receptor autoregulation. Structure 2002, 10:1187-1196.
50. Finn A.J., et al. Postsynaptic requirement for Abl kinases in assembly of the neuromuscular junction. Nat. Neurosci. 2003, 6:717-723.
51. Mohamed A.S., et al. Src-class kinases act within the agrin/MuSK pathway to regulate acetylcholine receptor phosphorylation, cytoskeletal anchoring, and clustering. J. Neurosci. 2001, 21:3806-3818.
52. Cheusova T., et al. Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction. Genes Dev. 2006, 20:1800-1816.
53. Limaye N., et al. Somatic mutations in angiopoietin receptor gene TEK cause solitary and multiple sporadic venous malformations. Nat. Genet. 2009, 41:118-124.
54. Shewchuk L.M., et al. Structure of the Tie2 RTK domain: self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail. Structure 2000, 8:1105-1113.
55. Wang J.K., Goldfarb M. Amino acid residues which distinguish the mitogenic potentials of two FGF receptors. Oncogene 1997, 14:1767-1778.
56. Lindholm C.K., et al. Shf, a Shb-like adapter protein, is involved in PDGF-α-receptor regulation of apoptosis. Biochem. Biophys. Res. Commun. 2000, 278:537-543.
57. Jazayeri A., et al. SHP-2 can suppress transformation induced by platelet-derived growth factor. Exp. Cell Res. 2000, 254:197-203.
58. Ekman S., et al. Increased mitogenicity of an αβ heterodimeric PDGF receptor complex correlates with lack of RasGAP binding. Oncogene 1999, 18:2481-2488.
59. Valgeirsdottir S., et al. Activation of Stat5 by platelet-derived growth factor (PDGF) is dependent on phosphorylation sites in PDGF β-receptor juxtamembrane and kinase insert domains. Oncogene 1998, 16:505-515.
60. Yokote K., et al. Grb7 is a downstream signaling component of platelet-derived growth factor α- and β-receptors. J. Biol. Chem. 1996, 271:30942-30949.
61. Yokote K., et al. Direct interaction between Shc and the platelet-derived growth factor β-receptor. J. Biol. Chem. 1994, 269:15337-15343.
62. Kashishian A., et al. Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo. EMBO J. 1992, 11:1373-1382.
63. Ota J., et al. Association of Cbl with Fms and p85 in response to macrophage colony-stimulating factor. FEBS Lett. 2000, 466:96-100.
64. Downing J.R., et al. Peptide antisera to human colony-stimulating factor 1 receptor detect ligand-induced conformational changes and a binding site for phosphatidylinositol 3-kinase. Mol. Cell Biol. 1991, 11:2489-2495.
65. Dellinger M.T., Brekken R.A. Phosphorylation of Akt and ERK1/2 is required for VEGF-A/VEGFR2-induced proliferation and migration of lymphatic endothelium. PLoS ONE 2011, 6:e28947.
66. Dougher M., Terman B.I. Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization. Oncogene 1999, 18:1619-1627.
67. Matsumoto T., et al. VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis. EMBO J. 2005, 24:2342-2353.
68. Matsumoto T., Mugishima H. Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis. J. Atheroscler. Thromb. 2006, 13:130-135.
69. Wu L.W., et al. VRAP is an adaptor protein that binds KDR, a receptor for vascular endothelial cell growth factor. J. Biol. Chem. 2000, 275:6059-6062.