Autoinhibition of the Kit Receptor Tyrosine Kinase by the Cytosolic Juxtamembrane Region

REFERENCES

• Barker, S. C., D. B. Kassel, D. Weigl, X. Huang, M. A. Luther, and W. B. Knight. 1995. Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process. Biochemistry 34: 14843–14851.
   PubMedGoogle Scholar
• Baxter, R. M., J. P. Secrist, R. R. Vaillancourt, and A. Kazlauskas. 1998. Full activation of the platelet-derived growth factor beta-receptor kinase involves multiple events. J. Biol. Chem. 273: 17050–17055.
   PubMedGoogle Scholar
• Besmer, P., J. E. Murphy, P. C. George, F. H. Qiu, P. J. Bergold, L. Lederman, H. W. Snyder, Jr., D. Brodeur, E. E. Zuckerman, and W. D. Hardy. 1986. A new acute transforming feline retrovirus and relationship of its oncogene v-kit with the protein kinase gene family. Nature 320: 415–421.
   PubMed Web of Science ®Google Scholar
• Binns, K. L., P. P. Taylor, F. Sicheri, T. Pawson, and S. J. Holland. 2000. Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors. Mol. Cell. Biol. 20: 4791–4805.
   PubMed Web of Science ®Google Scholar
• Buchwald, G., E. Hostinova, M. G. Rudolph, A. Kraemer, A. Sickmann, H. E. Meyer, K. Scheffzek, and A. Wittinghofer. 2001. Conformational switch and role of phosphorylation in PAK activation. Mol. Cell. Biol. 21: 5179–5189.
   PubMed Web of Science ®Google Scholar
• Casnellie, J. E. 1991. Assay of protein kinases using peptides with basic residues for phosphocellulose binding. Methods Enzymol. 200: 115–120.
   PubMedGoogle Scholar
• Chan, P. M., H. P. Nestler, and W. T. Miller. 2000. Investigating the substrate specificity of the HER2/Neu tyrosine kinase using peptide libraries. Cancer Lett. 160: 159–169.
   PubMedGoogle Scholar
• Dajani, R., E. Fraser, S. M. Roe, N. Young, V. Good, T. C. Dale, and L. H. Pearl. 2001. Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105:721–732.
   PubMed Web of Science ®Google Scholar
• Fersht, A. 1985. Enzyme structure and mechanism, 2nd ed. W. H. Freeman and Company, New York, N.Y.
   Google Scholar
• Frame, S., P. Cohen, and R. M. Biondi. 2001. A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol. Cell 7: 1321–1327.
   PubMed Web of Science ®Google Scholar
• Furitsu, T., T. Tsujimura, T. Tono, H. Ikeda, H. Kitayama, U. Koshimizu, H. Sugahara, J. H. Butterfield, L. K. Ashman, Y. Kanayama, et al. 1993. Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product. J. Clin. Investig. 92: 1736–1744.
   PubMed Web of Science ®Google Scholar
• Gille, H., J. Kowalski, L. Yu, H. Chen, M. T. Pisabarro, T. Davis-Smyth, and N. Ferrara. 2000. A repressor sequence in the juxtamembrane domain of Flt-1 (VEGFR-1) constitutively inhibits vascular endothelial growth factor-dependent phosphatidylinositol 3′-kinase activation and endothelial cell migration. EMBO J. 19: 4064–4073.
   PubMed Web of Science ®Google Scholar
• Hayakawa, F., M. Towatari, H. Kiyoi, M. Tanimoto, T. Kitamura, H. Saito, and T. Naoe. 2000. Tandem-duplicated Flt3 constitutively activates STAT5 and MAP kinase and introduces autonomous cell growth in IL-3-dependent cell lines. Oncogene 19: 624–631.
   PubMed Web of Science ®Google Scholar
• Heldin, C. H. 1995. Dimerization of cell surface receptors in signal transduction. Cell 80: 213–223.
   PubMed Web of Science ®Google Scholar
• Hirota, S., K. Isozaki, Y. Moriyama, K. Hashimoto, T. Nishida, S. Ishiguro, K. Kawano, M. Hanada, A. Kurata, M. Takeda, G. Muhammad Tunio, Y. Matsuzawa, Y. Kanakura, Y. Shinomura, and Y. Kitamura. 1998. Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors. Science 279: 577–580.
   PubMed Web of Science ®Google Scholar
• Hubbard, S. R. 2002. Autoinhibitory mechanisms in receptor tyrosine kinases. Front. Biosci. 7: d330–d340.
   PubMed Web of Science ®Google Scholar
• Hubbard, S. R., L. Wei, L. Ellis, and W. A. Hendrickson. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372: 746–754.
   PubMed Web of Science ®Google Scholar
• Huse, M., Y. G. Chen, J. Massague, and J. Kuriyan. 1999. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell 96: 425–436.
   PubMed Web of Science ®Google Scholar
• Irusta, P. M., and D. DiMaio. 1998. A single amino acid substitution in a WW-like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation. EMBO J. 17: 6912–6923.
   PubMed Web of Science ®Google Scholar
• Joensuu, H., P. J. Roberts, M. Sarlomo-Rikala, L. C. Andersson, P. Tervahartiala, D. Tuveson, S. Silberman, R. Capdeville, S. Dimitrijevic, B. Druker, and G. D. Demetri. 2001. Effect of the tyrosine kinase inhibitor STI571 in a patient with a metastatic gastrointestinal stromal tumor. N. Engl. J. Med. 344: 1052–1056.
   PubMed Web of Science ®Google Scholar
• Kozlowski, M., L. Larose, F. Lee, D. M. Le, R. Rottapel, and K. A. Siminovitch. 1998. SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol. Cell. Biol. 18: 2089–2099.
   PubMed Web of Science ®Google Scholar
• Lei, M., W. Lu, W. Meng, M. C. Parrini, M. J. Eck, B. J. Mayer, and S. C. Harrison. 2000. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102: 387–397.
   PubMed Web of Science ®Google Scholar
• Lev, S., D. Givol, and Y. Yarden. 1992. Interkinase domain of kit contains the binding site for phosphatidylinositol 3′ kinase. Proc. Natl. Acad. Sci. USA 89: 678–682.
   PubMed Web of Science ®Google Scholar
• Linnekin, D. 1999. Early signaling pathways activated by c-Kit in hematopoietic cells. Int. J. Biochem. Cell Biol. 31: 1053–1074.
   PubMed Web of Science ®Google Scholar
• Linnekin, D., C. S. DeBerry, and S. Mou. 1997. Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells. J. Biol. Chem. 272: 27450–27455.
   PubMed Web of Science ®Google Scholar
• Longley, B. J., M. J. Reguera, and Y. Ma. 2001. Classes of c-KIT activating mutations: proposed mechanisms of action and implications for disease classification and therapy. Leuk. Res. 25: 571–576.
   PubMed Web of Science ®Google Scholar
• Ma, Y., B. J. Longley, X. Wang, J. L. Blount, K. Langley, and G. H. Caughey. 1999. Clustering of activating mutations in c-KIT's juxtamembrane coding region in canine mast cell neoplasms. J. Investig. Dermatol. 112: 165–170.
   PubMed Web of Science ®Google Scholar
• Miettinen, M., and J. Lasota. 2001. Gastrointestinal stromal tumors-definition, clinical, histological, immunohistochemical, and molecular genetic features and differential diagnosis. Virchows Arch. 438: 1–12.
   PubMed Web of Science ®Google Scholar
• Mizuki, M., R. Fenski, H. Halfter, I. Matsumura, R. Schmidt, C. Muller, W. Gruning, K. Kratz-Albers, S. Serve, C. Steur, T. Buchner, J. Kienast, Y. Kanakura, W. E. Berdel, and H. Serve. 2000. Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways. Blood 96: 3907–3914.
   PubMed Web of Science ®Google Scholar
• Mohammadi, M., J. Schlessinger, and S. R. Hubbard. 1996. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86: 577–587.
   PubMed Web of Science ®Google Scholar
• Myles, G. M., C. S. Brandt, K. Carlberg, and L. R. Rohrschneider. 1994. Tyrosine 569 in the c-Fms juxtamembrane domain is essential for kinase activity and macrophage colony-stimulating factor-dependent internalization. Mol. Cell. Biol. 14: 4843–4854.
   PubMedGoogle Scholar
• Nakao, M., S. Yokota, T. Iwai, H. Kaneko, S. Horiike, K. Kashima, Y. Sonoda, T. Fujimoto, and S. Misawa. 1996. Internal tandem duplication of the flt3 gene found in acute myeloid leukemia. Leukemia 10: 1911–1918.
   PubMed Web of Science ®Google Scholar
• Plo, I., D. Lautier, N. Casteran, P. Dubreuil, M. Arock, and G. Laurent. 2001. Kit signaling and negative regulation of daunorubicin-induced apoptosis: role of phospholipase Cγ. Oncogene 20: 6752–6763.
   PubMed Web of Science ®Google Scholar
• Price, D. J., B. Rivnay, Y. Fu, S. Jiang, S. Avraham, and H. Avraham. 1997. Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. J. Biol. Chem. 272: 5915–5920.
   PubMed Web of Science ®Google Scholar
• Qiu, F. H., P. Ray, K. Brown, P. E. Barker, S. Jhanwar, F. H. Ruddle, and P. Besmer. 1988. Primary structure of c-kit: relationship with the CSF-1/PDGF receptor kinase family-oncogenic activation of v-kit involves deletion of extracellular domain and C terminus. EMBO J. 7: 1003–1011.
   PubMed Web of Science ®Google Scholar
• Santoro, M., F. Carlomagno, A. Romano, D. P. Bottaro, N. A. Dathan, M. Grieco, A. Fusco, G. Vecchio, B. Matoskova, M. H. Kraus, et al. 1995. Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B. Science 267: 381–383.
   PubMed Web of Science ®Google Scholar
• Schlessinger, J. 2000. Cell signaling by receptor tyrosine kinases. Cell 103: 211–225.
   PubMed Web of Science ®Google Scholar
• Serve, H., Y. C. Hsu, and P. Besmer. 1994. 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. 269: 6026–6030.
   PubMedGoogle Scholar
• Sicheri, F., I. Moarefi, and J. Kuriyan. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature 385: 602–609.
   PubMed Web of Science ®Google Scholar
• Till, J. H., P. M. Chan, and W. T. Miller. 1999. Engineering the substrate specificity of the Abl tyrosine kinase. J. Biol. Chem. 274: 4995–5003.
   PubMed Web of Science ®Google Scholar
• Wybenga-Groot, L. E., B. Baskin, S. H. Ong, J. Tong, T. Pawson, and F. Sicheri. 2001. Structural basis for autoinhibition of the EphB2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell 106: 745–757.
   PubMed Web of Science ®Google Scholar
• Xu, W., S. C. Harrison, and M. J. Eck. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385: 595–602.
   PubMed Web of Science ®Google Scholar