Structure of the Notch1 Negative Regulatory Region: Implications for Normal Activation and Pathogenic Signaling in TALL (original) (raw)

Abstract

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The study explores the structure of the Notch1 negative regulatory region (NRR) and its implications for both normal receptor activation and pathogenic signaling, particularly in the context of T cell acute lymphocytic leukemia (T-ALL). Notch proteins play a vital role in cell fate decisions during development and tissue homeostasis. The paper discusses how mutations and aberrant signaling pathways associated with Notch1 contribute to T-ALL, emphasizing the importance of understanding the structural mechanisms that govern Notch signaling for potential therapeutic interventions.

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References (43)

  1. Bray SJ. Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol. 2006;7:678-689
  2. Blaumueller CM, Qi H, Zagouras P, Artavanis-Tsakonas S. Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane. Cell. 1997;90:281-291
  3. Logeat F, Bessia C, Brou C, LeBail O, Jarriault S, Seidah NG, Israel A. The Notch1 receptor is cleaved constitutively by a furin-like convertase. Proc Natl Acad Sci U S A. 1998;95:8108-8112
  4. Kopan R, Schroeter EH, Weintraub H, Nye JS. Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain. Proc Natl Acad Sci U S A. 1996;93:1683-1688
  5. Sanchez-Irizarry C, Carpenter AC, Weng AP, Pear WS, Aster JC, Blacklow SC. Notch subunit heterodimerization and prevention of ligand-independent proteolytic activation depend, respectively, on a novel domain and the LNR repeats. Mol Cell Biol. 2004;24:9265-9273
  6. Fehon R, Kooh P, Rebay I, Regan C, Xu T, Muskavitch M, Artavanis- Tsakonas S. Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila. Cell. 1990;61:523-534
  7. Brou C, Logeat F, Gupta N, Bessia C, LeBail O, Doedens JR, Cumano A, Roux P, Black RA, Israel A. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell. 2000;5:207-216
  8. Mumm JS, Schroeter EH, Saxena MT, Griesemer A, Tian X, Pan DJ, Ray WJ, Kopan R. A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1. Mol Cell. 2000;5:197-206
  9. De Strooper B, Annaert W, Cupers P, Saftig P, Craessaerts K, Mumm JS, Schroeter EH, Schrijvers V, Wolfe MS, Ray WJ, Goate A, Kopan R. A presenilin-1- dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature. 1999;398:518-522
  10. Selkoe D, Kopan R. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu Rev Neurosci. 2003;26:565-597
  11. Struhl G, Greenwald I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature. 1999;398:522-525
  12. Struhl G, Greenwald I. Presenilin-mediated transmembrane cleavage is required for Notch signal transduction in Drosophila. Proc Natl Acad Sci U S A. 2001;98:229-234
  13. Yu G, Nishimura M, Arawaka S, Levitan D, Zhang L, Tandon A, Song YQ, Rogaeva E, Chen F, Kawarai T, Supala A, Levesque L, Yu H, Yang DS, Holmes E, Milman P, Liang Y, Zhang DM, Xu DH, Sato C, Rogaev E, Smith M, Janus C, Zhang Y, Aebersold R, Farrer LS, Sorbi S, Bruni A, Fraser P, St George-Hyslop P. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing. Nature. 2000;407:48-54
  14. Nam Y, Sliz P, Song L, Aster JC, Blacklow SC. Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Cell. 2006;124:973-983 For personal use only. by guest on June 8, 2013. bloodjournal.hematologylibrary.org From 15. Schroeter EH, Kisslinger JA, Kopan R. Notch-1 signalling requires ligand- induced proteolytic release of intracellular domain. Nature. 1998;393:382-386
  15. Wilson JJ, Kovall RA. Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA. Cell. 2006;124:985-996
  16. Ellisen LW, Bird J, West DC, Soreng AL, Reynolds TC, Smith SD, Sklar J. TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell. 1991;66:649-661
  17. Weng AP, Ferrando AA, Lee W, Morris JPt, Silverman LB, Sanchez-Irizarry C, Blacklow SC, Look AT, Aster JC. Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia. Science. 2004;306:269-271
  18. Breit S, Stanulla M, Flohr T, Schrappe M, Ludwig WD, Tolle G, Happich M, Muckenthaler MU, Kulozik AE. Activating NOTCH1 mutations predict favorable early treatment response and long-term outcome in childhood precursor T-cell lymphoblastic leukemia. Blood. 2006;108:1151-1157
  19. De Keersmaecker K, Lahortiga I, Mentens N, Folens C, Van Neste L, Bekaert S, Vandenberghe P, Odero MD, Marynen P, Cools J. In vitro validation of gamma- secretase inhibitors alone or in combination with other anti-cancer drugs for the treatment of T-cell acute lymphoblastic leukemia. Haematologica. 2008;93:533-542
  20. Mansour MR, Duke V, Foroni L, Patel B, Allen CG, Ancliff PJ, Gale RE, Linch DC. Notch-1 mutations are secondary events in some patients with T-cell acute lymphoblastic leukemia. Clin Cancer Res. 2007;13:6964-6969
  21. Mansour MR, Linch DC, Foroni L, Goldstone AH, Gale RE. High incidence of Notch-1 mutations in adult patients with T-cell acute lymphoblastic leukemia. Leukemia. 2006;20:537-539
  22. Sulis ML, Williams O, Palomero T, Tosello V, Pallikuppam S, Real PJ, Barnes K, Zuurbier L, Meijerink JP, Ferrando AA. NOTCH1 extracellular juxtamembrane expansion mutations in T-ALL. Blood. 2008;112:733-740
  23. Zhu YM, Zhao WL, Fu JF, Shi JY, Pan Q, Hu J, Gao XD, Chen B, Li JM, Xiong SM, Gu LJ, Tang JY, Liang H, Jiang H, Xue YQ, Shen ZX, Chen Z, Chen SJ. NOTCH1 mutations in T-cell acute lymphoblastic leukemia: prognostic significance and implication in multifactorial leukemogenesis. Clin Cancer Res. 2006;12:3043-3049 25. Aster JC, Pear WS, Blacklow SC. Notch signaling in leukemia. Annu Rev Pathol. 2008;3:587-613
  24. Chiang MY, Xu ML, Histen G, Shestova O, Roy M, Nam Y, Blacklow SC, Sacks DB, Pear WS, Aster JC. Identification of a conserved negative regulatory sequence that influences the leukemogenic activity of NOTCH1. Mol Cell Biol. 2006;26:6261- 6271
  25. Malecki MJ, Sanchez-Irizarry C, Mitchell JL, Histen G, Xu ML, Aster JC, Blacklow SC. Leukemia-associated mutations within the NOTCH1 heterodimerization domain fall into at least two distinct mechanistic classes. Mol Cell Biol. 2006;26:4642- 4651
  26. Gordon WR, Vardar-Ulu D, Histen G, Sanchez-Irizarry C, Aster JC, Blacklow SC. Structural basis for autoinhibition of Notch. Nat Struct Mol Biol. 2007;14:295-300
  27. Otwinowsk Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology. 1997;276:307-326 For personal use only. by guest on June 8, 2013. bloodjournal.hematologylibrary.org From 30. McCoy A, Grosse-Kunstleve R, Adams P, Winn M, Storoni L, Read R. Phaser crystallographic software. . J. Appl. Cryst. 2007;40:658-674.
  28. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics.
  29. Acta Crystallogr. D Biol. Crystallogr. 2004;60:2126-2132
  30. Brunger A, Adams P, Clore G. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D. 1998;54:905-921
  31. Murshudov G, Vagin A, Dodson E. Refinement of macromolecular structures by the maximum-liklihood method. Acta Crystallogr. D. 1997;53:240-245
  32. Holm L, J P, . DaliLite workbench for protein structure comparison. Bioinformatics. 2000;16:566-567
  33. Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. . 2007;372:774--797
  34. Miller S, Janin J, Lesk AM, Chothia C. Interior and surface of monomeric proteins. J Mol Biol. 1987;196:641-656
  35. Aster JC, Xu L, Karnell FG, Patriub V, Pui JC, Pear WS. Essential roles for ankyrin repeat and transactivation domains in induction of T-cell leukemia by notch1. Mol Cell Biol. 2000;20:7505-7515
  36. Macao B, Johansson DGA, Hansson GC, Hard T. Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nature Structural and Molecular Biology. 2006;13:71-76
  37. Maeda T, Inoue M, Koshiba S, Yabuki T, Aoki M, Nunokawa E, Seki E, Matsuda T, Motoda Y, Kobayashi A, Hiroyasu F, al. e. Solution structure of the SEA Domain from the murine homologue of ovarian cancer antigen CA125 (MUC16). J. Biol. Chem. 2004;279:13174-13182
  38. Maris C, Dominguez C, Allain FH. The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression. Febs J. 2005;272:2118-2131
  39. Primo ME, Klinke S, Sica MP, Goldbaum FA, Jakoncic J, Poskus E, Ermacora MR. Structure of the mature ectodomain of the human receptor-type protein- tyrosine phosphatase IA-2. J Biol Chem. 2008;283:4674-4681
  40. Vooijs M, Schroeter EH, Pan Y, Blandford M, Kopan R. Ectodomain shedding and intramembrane cleavage of mammalian Notch proteins is not regulated through oligomerization. J Biol Chem. 2004;279:50864-50873
  41. Nichols JT, Miyamoto A, Olsen SL, D'Souza B, Yao C, Weinmaster G. DSL ligand endocytosis physically dissociates Notch1 heterodimers before activating proteolysis can occur. J Cell Biol. 2007;176:445-458
  42. Parks AL, Klueg KM, Stout JR, Muskavitch MA. Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. Development. 2000;127:1373- 1385 45. Maskos K, Fernandez-Catalan C, Huber R, Bourenkov GP, Bartunik H, Ellestad GA, Reddy P, Wolfson MF, Rauch CT, Castner BJ, Davis R, Clarke HRG, Peterson M, Fitzner JN, Cerretti DP, March CJ, Paxton RJ, Black RA, Bode W. Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proc. Natl. Acad. Sci. USA. 1998;95:3408-3412 For personal use only. by guest on June 8, 2013. bloodjournal.hematologylibrary.org From 46. Li K, Li Y, Wu W, Gordon WR, Chang DW, Lu M, Scoggin S, Fu T, Vien L, Histen G, Zheng J, Martin-Hollister R, Duensing T, Singh S, Blacklow SC, Yao Z, Aster JC, Zhou BB. Modulation of Notch signaling by antibodies specific for the extracellular negative regulatory region of NOTCH3. J Biol Chem. 2008;283:8046-8054
  43. Gordon WR, Arnett KL, Blacklow SC. The molecular logic of Notch signaling -a structural and biochemical perspective. J Cell Sci. 2008;121:3109-3119 For personal use only. by guest on June 8, 2013.