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Volumn 13, Issue 2, 2004, Pages 169-178

The Structural Basis for Autoinhibition of FLT3 by the Juxtamembrane Domain

Author keywords

[No Author keywords available]

Indexed keywords

CD135 ANTIGEN; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 0842310394     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00505-7     Document Type: Article
Times cited : (421)

References (58)
  • 2
    • 0027931013 scopus 로고
    • Genomic structure of the downstream part of the human FLT3 gene: Exon/intron structure conservation among genes encoding receptor tyrosine kinases (RTK) of subclass III
    • Agnes F., Shamoon B., Dina C., Rosnet O., Birnbaum D., Galibert F. Genomic structure of the downstream part of the human FLT3 gene. exon/intron structure conservation among genes encoding receptor tyrosine kinases (RTK) of subclass III Gene. 145:1994;283-288.
    • (1994) Gene , vol.145 , pp. 283-288
    • Agnes, F.1    Shamoon, B.2    Dina, C.3    Rosnet, O.4    Birnbaum, D.5    Galibert, F.6
  • 3
    • 3042716081 scopus 로고    scopus 로고
    • A single amino acid exchange inverts susceptibility of related receptor tyrosine kinases for the ATP site inhibitor STI-571
    • Bohmer F.D., Karagyozov L., Uecker A., Serve H., Botzki A., Mahboobi S., Dove S. A single amino acid exchange inverts susceptibility of related receptor tyrosine kinases for the ATP site inhibitor STI-571. J. Biol. Chem. 278:2003;5148-5155.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5148-5155
    • Bohmer, F.D.1    Karagyozov, L.2    Uecker, A.3    Serve, H.4    Botzki, A.5    Mahboobi, S.6    Dove, S.7
  • 4
    • 0027409462 scopus 로고
    • Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 a structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24)
    • Bossemeyer D., Engh R.A., Kinzel V., Ponstingl H., Huber R. Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 12:1993;849-859.
    • (1993) EMBO J. , vol.12 , pp. 849-859
    • Bossemeyer, D.1    Engh, R.A.2    Kinzel, V.3    Ponstingl, H.4    Huber, R.5
  • 7
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 8
    • 0037405026 scopus 로고    scopus 로고
    • Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region
    • Chan P.M., Ilangumaran S., La Rose J., Chakrabartty A., Rottapel R. Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region. Mol. Cell Biol. 23:2003;3067-3078.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3067-3078
    • Chan, P.M.1    Ilangumaran, S.2    La Rose, J.3    Chakrabartty, A.4    Rottapel, R.5
  • 10
    • 0030002950 scopus 로고    scopus 로고
    • Expression of FLT3 receptor and response to FLT3 ligand by leukemic cells
    • Drexler H.G. Expression of FLT3 receptor and response to FLT3 ligand by leukemic cells. Leukemia. 10:1996;588-599.
    • (1996) Leukemia , vol.10 , pp. 588-599
    • Drexler, H.G.1
  • 12
    • 0043245991 scopus 로고    scopus 로고
    • SU5416, a small molecule tyrosine kinase receptor inhibitor, has biologic activity in patients with refractory acute myeloid leukemia or myelodysplastic syndromes
    • Giles F.J., Stopeck A.T., Silverman L.R., Lancet J.E., Cooper M.A., Hannah A.L., Cherrington J.M., O'Farrell A.M., Yuen H.A., Louie S.G.et al. SU5416, a small molecule tyrosine kinase receptor inhibitor, has biologic activity in patients with refractory acute myeloid leukemia or myelodysplastic syndromes. Blood. 102:2003;795-801.
    • (2003) Blood , vol.102 , pp. 795-801
    • Giles, F.J.1    Stopeck, A.T.2    Silverman, L.R.3    Lancet, J.E.4    Cooper, M.A.5    Hannah, A.L.6    Cherrington, J.M.7    O'Farrell, A.M.8    Yuen, H.A.9    Louie, S.G.10
  • 13
    • 0036720398 scopus 로고    scopus 로고
    • The roles of FLT3 in hematopoiesis and leukemia
    • Gilliland D.G., Griffin J.D. The roles of FLT3 in hematopoiesis and leukemia. Blood. 100:2002;1532-1542.
    • (2002) Blood , vol.100 , pp. 1532-1542
    • Gilliland, D.G.1    Griffin, J.D.2
  • 14
    • 0034598830 scopus 로고    scopus 로고
    • Tandem-duplicated Flt3 constitutively activates STAT5 and MAP kinase and introduces autonomous cell growth in IL-3-dependent cell lines
    • Hayakawa F., Towatari M., Kiyoi H., Tanimoto M., Kitamura T., Saito H., Naoe T. Tandem-duplicated Flt3 constitutively activates STAT5 and MAP kinase and introduces autonomous cell growth in IL-3-dependent cell lines. Oncogene. 19:2000;624-631.
    • (2000) Oncogene , vol.19 , pp. 624-631
    • Hayakawa, F.1    Towatari, M.2    Kiyoi, H.3    Tanimoto, M.4    Kitamura, T.5    Saito, H.6    Naoe, T.7
  • 15
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin C.H. Dimerization of cell surface receptors in signal transduction. Cell. 80:1995;213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 17
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard S.R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16:1997;5572-5581.
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 18
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard S.R., Wei L., Ellis L., Hendrickson W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372:1994;746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 19
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., Kuriyan J. The conformational plasticity of protein kinases. Cell. 109:2002;275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 20
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • Huse M., Chen Y.G., Massague J., Kuriyan J. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell. 96:1999;425-436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 21
    • 0037064087 scopus 로고    scopus 로고
    • Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor β receptor
    • Irusta P.M., Luo Y., Bakht O., Lai C., Smith S.O., DiMaio D. Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor β receptor. J. Biol. Chem. 277:2002;38627-38634.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38627-38634
    • Irusta, P.M.1    Luo, Y.2    Bakht, O.3    Lai, C.4    Smith, S.O.5    Dimaio, D.6
  • 25
    • 0029294896 scopus 로고
    • Biology and potential clinical applications of flt3 ligand
    • Lyman S.D., Williams D.E. Biology and potential clinical applications of flt3 ligand. Curr. Opin. Hematol. 2:1995;177-181.
    • (1995) Curr. Opin. Hematol. , vol.2 , pp. 177-181
    • Lyman, S.D.1    Williams, D.E.2
  • 27
    • 0027461751 scopus 로고
    • Biochemical characterization and analysis of the transforming potential of the FLT3/FLK2 receptor tyrosine kinase
    • Maroc N., Rottapel R., Rosnet O., Marchetto S., Lavezzi C., Mannoni P., Birnbaum D., Dubreuil P. Biochemical characterization and analysis of the transforming potential of the FLT3/FLK2 receptor tyrosine kinase. Oncogene. 8:1993;909-918.
    • (1993) Oncogene , vol.8 , pp. 909-918
    • Maroc, N.1    Rottapel, R.2    Rosnet, O.3    Marchetto, S.4    Lavezzi, C.5    Mannoni, P.6    Birnbaum, D.7    Dubreuil, P.8
  • 28
    • 0025770646 scopus 로고
    • A receptor tyrosine kinase specific to hematopoietic stem and progenitor cell-enriched populations
    • Matthews W., Jordan C.T., Wiegand G.W., Pardoll D., Lemischka I.R. A receptor tyrosine kinase specific to hematopoietic stem and progenitor cell-enriched populations. Cell. 65:1991;1143-1152.
    • (1991) Cell , vol.65 , pp. 1143-1152
    • Matthews, W.1    Jordan, C.T.2    Wiegand, G.W.3    Pardoll, D.4    Lemischka, I.R.5
  • 30
    • 0034554796 scopus 로고    scopus 로고
    • Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways
    • Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C., Gruning W., Kratz-Albers K., Serve S., Steur C.et al. Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways. Blood. 96:2000;3907-3914.
    • (2000) Blood , vol.96 , pp. 3907-3914
    • Mizuki, M.1    Fenski, R.2    Halfter, H.3    Matsumura, I.4    Schmidt, R.5    Muller, C.6    Gruning, W.7    Kratz-Albers, K.8    Serve, S.9    Steur, C.10
  • 34
    • 0037064032 scopus 로고    scopus 로고
    • Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity
    • Munshi S., Kornienko M., Hall D.L., Reid J.C., Waxman L., Stirdivant S.M., Darke P.L., Kuo L.C. Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity. J. Biol. Chem. 277:2002;38797-38802.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38797-38802
    • Munshi, S.1    Kornienko, M.2    Hall, D.L.3    Reid, J.C.4    Waxman, L.5    Stirdivant, S.M.6    Darke, P.L.7    Kuo, L.C.8
  • 36
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza J. AmoRe. an automated package for molecular replacement Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 37
    • 0037200045 scopus 로고    scopus 로고
    • Deletion of the carboxyl terminus of Tie2 enhances kinase activity, signaling, and function. Evidence for an autoinhibitory mechanism
    • Niu X.L., Peters K.G., Kontos C.D. Deletion of the carboxyl terminus of Tie2 enhances kinase activity, signaling, and function. Evidence for an autoinhibitory mechanism. J. Biol. Chem. 277:2002;31768-31773.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31768-31773
    • Niu, X.L.1    Peters, K.G.2    Kontos, C.D.3
  • 39
    • 0027130517 scopus 로고
    • Hematopoietic receptors of class III receptor-type tyrosine kinases
    • Rosnet O., Birnbaum D. Hematopoietic receptors of class III receptor-type tyrosine kinases. Crit. Rev. Oncog. 4:1993;595-613.
    • (1993) Crit. Rev. Oncog. , vol.4 , pp. 595-613
    • Rosnet, O.1    Birnbaum, D.2
  • 40
    • 0025870946 scopus 로고
    • Murine Flt3, a gene encoding a novel tyrosine kinase receptor of the PDGFR/CSF1R family
    • a
    • Rosnet O., Marchetto S., deLapeyriere O., Birnbaum D. Murine Flt3, a gene encoding a novel tyrosine kinase receptor of the PDGFR/CSF1R family. Oncogene. 6:1991;1641-1650. a.
    • (1991) Oncogene , vol.6 , pp. 1641-1650
    • Rosnet, O.1    Marchetto, S.2    Delapeyriere, O.3    Birnbaum, D.4
  • 41
    • 0025969518 scopus 로고
    • Isolation and chromosomal localization of a novel FMS-like tyrosine kinase gene
    • b
    • Rosnet O., Mattei M.G., Marchetto S., Birnbaum D. Isolation and chromosomal localization of a novel FMS-like tyrosine kinase gene. Genomics. 9:1991;380-385. b.
    • (1991) Genomics , vol.9 , pp. 380-385
    • Rosnet, O.1    Mattei, M.G.2    Marchetto, S.3    Birnbaum, D.4
  • 44
    • 0034124850 scopus 로고    scopus 로고
    • Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots
    • Savvides S.N., Boone T., Andrew Karplus P. Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots. Nat. Struct. Biol. 7:2000;486-491.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 486-491
    • Savvides, S.N.1    Boone, T.2    Andrew Karplus, P.3
  • 45
    • 0036595322 scopus 로고    scopus 로고
    • Finding the next Gleevec: FLT3 targeted kinase inhibitor therapy for acute myeloid leukemia
    • Sawyers C.L. Finding the next Gleevec. FLT3 targeted kinase inhibitor therapy for acute myeloid leukemia Cancer Cell. 1:2002;413-415.
    • (2002) Cancer Cell , vol.1 , pp. 413-415
    • Sawyers, C.L.1
  • 46
    • 0037071418 scopus 로고    scopus 로고
    • Tyrosine kinase oncogenes in normal hematopoiesis and hematological disease
    • Scheijen B., Griffin J.D. Tyrosine kinase oncogenes in normal hematopoiesis and hematological disease. Oncogene. 21:2002;3314-3333.
    • (2002) Oncogene , vol.21 , pp. 3314-3333
    • Scheijen, B.1    Griffin, J.D.2
  • 47
    • 0038418059 scopus 로고    scopus 로고
    • Signal transduction. Autoinhibition control
    • Schlessinger J. Signal transduction. Autoinhibition control. Science. 300:2003;750-752.
    • (2003) Science , vol.300 , pp. 750-752
    • Schlessinger, J.1
  • 48
    • 0037441745 scopus 로고    scopus 로고
    • The protein tyrosine kinase inhibitor SU5614 inhibits FLT3 and induces growth arrest and apoptosis in AML-derived cell lines expressing a constitutively activated FLT3
    • Spiekermann K., Dirschinger R.J., Schwab R., Bagrintseva K., Faber F., Buske C., Schnittger S., Kelly L.M., Gilliland D.G., Hiddemann W. The protein tyrosine kinase inhibitor SU5614 inhibits FLT3 and induces growth arrest and apoptosis in AML-derived cell lines expressing a constitutively activated FLT3. Blood. 101:2003;1494-1504.
    • (2003) Blood , vol.101 , pp. 1494-1504
    • Spiekermann, K.1    Dirschinger, R.J.2    Schwab, R.3    Bagrintseva, K.4    Faber, F.5    Buske, C.6    Schnittger, S.7    Kelly, L.M.8    Gilliland, D.G.9    Hiddemann, W.10
  • 49
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos J., Sliwkowski M.X., Eigenbrot C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277:2002;46265-46272.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 50
    • 0141465061 scopus 로고    scopus 로고
    • The role of FLT3 in haematopoietic malignancies
    • Stirewalt D.L., Radich J.P. The role of FLT3 in haematopoietic malignancies. Nat. Rev. Cancer. 3:2003;650-665.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 650-665
    • Stirewalt, D.L.1    Radich, J.P.2
  • 51
    • 0037097716 scopus 로고    scopus 로고
    • Analysis of FLT3-activating mutations in 979 patients with acute myelogenous leukemia: Association with FAB subtypes and identification of subgroups with poor prognosis
    • Thiede C., Steudel C., Mohr B., Schaich M., Schakel U., Platzbecker U., Wermke M., Bornhauser M., Ritter M., Neubauer A.et al. Analysis of FLT3-activating mutations in 979 patients with acute myelogenous leukemia. association with FAB subtypes and identification of subgroups with poor prognosis Blood. 99:2002;4326-4335.
    • (2002) Blood , vol.99 , pp. 4326-4335
    • Thiede, C.1    Steudel, C.2    Mohr, B.3    Schaich, M.4    Schakel, U.5    Platzbecker, U.6    Wermke, M.7    Bornhauser, M.8    Ritter, M.9    Neubauer, A.10
  • 53
    • 0029998037 scopus 로고    scopus 로고
    • FLT3 receptor expression on the surface of normal and malignant human hematopoietic cells
    • Turner A.M., Lin N.L., Issarachai S., Lyman S.D., Broudy V.C. FLT3 receptor expression on the surface of normal and malignant human hematopoietic cells. Blood. 88:1996;3383-3390.
    • (1996) Blood , vol.88 , pp. 3383-3390
    • Turner, A.M.1    Lin, N.L.2    Issarachai, S.3    Lyman, S.D.4    Broudy, V.C.5
  • 55
    • 0035929146 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region
    • Wybenga-Groot L.E., Baskin B., Ong S.H., Tong J., Pawson T., Sicheri F. Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell. 106:2001;745-757.
    • (2001) Cell , vol.106 , pp. 745-757
    • Wybenga-Groot, L.E.1    Baskin, B.2    Ong, S.H.3    Tong, J.4    Pawson, T.5    Sicheri, F.6
  • 57
    • 16944365287 scopus 로고    scopus 로고
    • Internal tandem duplication of the FLT3 gene is preferentially seen in acute myeloid leukemia and myelodysplastic syndrome among various hematological malignancies. A study on a large series of patients and cell lines
    • Yokota S., Kiyoi H., Nakao M., Iwai T., Misawa S., Okuda T., Sonoda Y., Abe T., Kahsima K., Matsuo Y.et al. Internal tandem duplication of the FLT3 gene is preferentially seen in acute myeloid leukemia and myelodysplastic syndrome among various hematological malignancies. A study on a large series of patients and cell lines. Leukemia. 11:1997;1605-1609.
    • (1997) Leukemia , vol.11 , pp. 1605-1609
    • Yokota, S.1    Kiyoi, H.2    Nakao, M.3    Iwai, T.4    Misawa, S.5    Okuda, T.6    Sonoda, Y.7    Abe, T.8    Kahsima, K.9    Matsuo, Y.10
  • 58
    • 0034605042 scopus 로고    scopus 로고
    • Essential role of signal transducer and activator of transcription (Stat)5a but not Stat5b for Flt3-dependent signaling
    • Zhang S., Fukuda S., Lee Y., Hangoc G., Cooper S., Spolski R., Leonard W.J., Broxmeyer H.E. Essential role of signal transducer and activator of transcription (Stat)5a but not Stat5b for Flt3-dependent signaling. J. Exp. Med. 192:2000;719-728.
    • (2000) J. Exp. Med. , vol.192 , pp. 719-728
    • Zhang, S.1    Fukuda, S.2    Lee, Y.3    Hangoc, G.4    Cooper, S.5    Spolski, R.6    Leonard, W.J.7    Broxmeyer, H.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.