메뉴 건너뛰기




Volumn 14, Issue 4, 2007, Pages 295-300

Structural basis for autoinhibition of Notch

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEINASE; NOTCH RECEPTOR; NOTCH1 RECEPTOR; NOTCH2 RECEPTOR;

EID: 34247189534     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1227     Document Type: Article
Times cited : (295)

References (42)
  • 1
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: A simple pathway becomes complex
    • Bray, S.J. Notch signalling: a simple pathway becomes complex. Nat. Rev. Mol. Cell Biol. 7, 678-689 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 678-689
    • Bray, S.J.1
  • 2
    • 5044225888 scopus 로고    scopus 로고
    • Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia
    • Weng, A.P. et al. Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia. Science 306, 269-271 (2004).
    • (2004) Science , vol.306 , pp. 269-271
    • Weng, A.P.1
  • 3
    • 0030877659 scopus 로고    scopus 로고
    • Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane
    • Blaumueller, C.M., Qi, H., Zagouras, P. & Artavanis-Tsakonas, S. Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane. Cell 90, 281-291 (1997).
    • (1997) Cell , vol.90 , pp. 281-291
    • Blaumueller, C.M.1    Qi, H.2    Zagouras, P.3    Artavanis-Tsakonas, S.4
  • 4
    • 0032493302 scopus 로고    scopus 로고
    • The Notch1 receptor is cleaved constitutively by a furin-like convertase
    • Logeat, F. et al. The Notch1 receptor is cleaved constitutively by a furin-like convertase. Proc. Natl. Acad. Sci. USA 95, 8108-8112 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8108-8112
    • Logeat, F.1
  • 5
    • 6344251643 scopus 로고    scopus 로고
    • Notch subunit heterodimerization and prevention of ligand-independent proteolytic activation depend, respectively, on a novel domain and the LNR repeats
    • Sanchez-Irizarry, C. et al. Notch subunit heterodimerization and prevention of ligand-independent proteolytic activation depend, respectively, on a novel domain and the LNR repeats. Mol. Cell. Biol. 24, 9265-9273 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9265-9273
    • Sanchez-Irizarry, C.1
  • 6
    • 0025277746 scopus 로고
    • Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila
    • Fehon, R.G. et al. Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila. Cell 61, 523-534 (1990).
    • (1990) Cell , vol.61 , pp. 523-534
    • Fehon, R.G.1
  • 7
    • 0030748716 scopus 로고    scopus 로고
    • The ins and outs of notch signaling
    • Weinmaster, G. The ins and outs of notch signaling. Mol. Cell. Neurosci. 9, 91-102 (1997).
    • (1997) Mol. Cell. Neurosci , vol.9 , pp. 91-102
    • Weinmaster, G.1
  • 8
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • Brou, C. et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol. Cell 5, 207-216 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 207-216
    • Brou, C.1
  • 9
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1
    • Mumm, J.S. et al. A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1. Mol. Cell 5, 197-206 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1
  • 10
    • 0034669031 scopus 로고    scopus 로고
    • A common enzyme connects notch signaling and Alzheimer's disease
    • Kopan, R. & Goate, A. A common enzyme connects notch signaling and Alzheimer's disease. Genes Dev. 14, 2799-2806 (2000).
    • (2000) Genes Dev , vol.14 , pp. 2799-2806
    • Kopan, R.1    Goate, A.2
  • 11
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E.H., Kisslinger, J.A. & Kopan, R. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393, 382-386 (1998).
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 12
    • 0032524325 scopus 로고    scopus 로고
    • Nuclear access and action of notch in vivo
    • Struhl, G. & Adachi, A. Nuclear access and action of notch in vivo. Cell 93, 649-660 (1998).
    • (1998) Cell , vol.93 , pp. 649-660
    • Struhl, G.1    Adachi, A.2
  • 13
    • 0027219557 scopus 로고
    • Intrinsic activity of the Lin-12 and Notch intracellular domains in vivo
    • Struhl, G., Fitzgerald, K. & Greenwald, I. Intrinsic activity of the Lin-12 and Notch intracellular domains in vivo. Cell 74, 331-345 (1993).
    • (1993) Cell , vol.74 , pp. 331-345
    • Struhl, G.1    Fitzgerald, K.2    Greenwald, I.3
  • 14
    • 0030003538 scopus 로고    scopus 로고
    • Signal transduction by activated mNotch: Importance of proteolytic processing and its regulation by the extracellular domain
    • Kopan, R., Schroeter, E.H., Weintraub, H. & Nye, J.S. Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain. Proc. Natl. Acad. Sci. USA 93, 1683-1688 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1683-1688
    • Kopan, R.1    Schroeter, E.H.2    Weintraub, H.3    Nye, J.S.4
  • 15
    • 0027386233 scopus 로고
    • Antineurogenic phenotypes induced by truncated Notch proteins indicate a role in signal transduction and may point to a novel function for Notch in nuclei
    • Lieber, T., Kidd, S., Alcamo, E., Corbin, V. & Young, M.W. Antineurogenic phenotypes induced by truncated Notch proteins indicate a role in signal transduction and may point to a novel function for Notch in nuclei. Genes Dev. 7, 1949-1965 (1993).
    • (1993) Genes Dev , vol.7 , pp. 1949-1965
    • Lieber, T.1    Kidd, S.2    Alcamo, E.3    Corbin, V.4    Young, M.W.5
  • 16
    • 0027306001 scopus 로고
    • Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor
    • Rebay, I., Fehon, R.G. & Artavanis-Tsakonas, S. Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor. Cell 74, 319-329 (1993).
    • (1993) Cell , vol.74 , pp. 319-329
    • Rebay, I.1    Fehon, R.G.2    Artavanis-Tsakonas, S.3
  • 17
    • 0031030361 scopus 로고    scopus 로고
    • Germ-line tumor formation caused by activation of glp-1, a Caenorhabditis elegans member of the Notch family of receptors
    • Berry, L.W., Westlund, B. & Schedl, T. Germ-line tumor formation caused by activation of glp-1, a Caenorhabditis elegans member of the Notch family of receptors. Development 124, 925-936 (1997).
    • (1997) Development , vol.124 , pp. 925-936
    • Berry, L.W.1    Westlund, B.2    Schedl, T.3
  • 18
    • 0025316499 scopus 로고
    • Analysis of gain-of-function mutations of the lin-12 gene of Caenorhabditis elegans
    • Greenwald, I. & Seydoux, G. Analysis of gain-of-function mutations of the lin-12 gene of Caenorhabditis elegans. Nature 346, 197-199 (1990).
    • (1990) Nature , vol.346 , pp. 197-199
    • Greenwald, I.1    Seydoux, G.2
  • 19
    • 0038808602 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1
    • Vardar, D., North, C.L., Sanchez-Irizarry, C., Aster, J.C. & Blacklow, S.C. Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1. Biochemistry 42, 7061-7067 (2003).
    • (2003) Biochemistry , vol.42 , pp. 7061-7067
    • Vardar, D.1    North, C.L.2    Sanchez-Irizarry, C.3    Aster, J.C.4    Blacklow, S.C.5
  • 20
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L. & Sander, C. Mapping the protein universe. Science 273, 595-603 (1996).
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 21
    • 11144357605 scopus 로고    scopus 로고
    • Solution structure of the SEA Domain from the murine homologue of ovarian cancer antigen CA125 (MUC16)
    • Maeda, T. et al. Solution structure of the SEA Domain from the murine homologue of ovarian cancer antigen CA125 (MUC16). J. Biol. Chem. 279, 13174-13182 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 13174-13182
    • Maeda, T.1
  • 22
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao, B., Johansson, D.G.A., Hansson, G.C. & Hard, T. Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat. Struct. Mol. Biol. 13, 71-76 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 71-76
    • Macao, B.1    Johansson, D.G.A.2    Hansson, G.C.3    Hard, T.4
  • 23
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: From the outside in
    • Mumm, J.S. & Kopan, R. Notch signaling: from the outside in. Dev. Biol. 228, 151-165 (2000).
    • (2000) Dev. Biol , vol.228 , pp. 151-165
    • Mumm, J.S.1    Kopan, R.2
  • 24
    • 0037238008 scopus 로고    scopus 로고
    • Mind bomb is a ubiquitin ligase that is essential for efficient activation of Notch signaling by Delta
    • Itoh, M. et al. Mind bomb is a ubiquitin ligase that is essential for efficient activation of Notch signaling by Delta. Dev. Cell 4, 67-82 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 67-82
    • Itoh, M.1
  • 25
    • 18844414504 scopus 로고    scopus 로고
    • The roles of receptor and ligand endocytosis in regulating Notch signaling
    • Le Borgne, R., Bardin, A. & Schweisguth, F. The roles of receptor and ligand endocytosis in regulating Notch signaling. Development 132, 1751-1762 (2005).
    • (2005) Development , vol.132 , pp. 1751-1762
    • Le Borgne, R.1    Bardin, A.2    Schweisguth, F.3
  • 26
    • 9444297354 scopus 로고    scopus 로고
    • Drosophila Epsin mediates a select endocytic pathway that DSL ligands must enter to activate Notch
    • Wang, W. & Struhl, G. Drosophila Epsin mediates a select endocytic pathway that DSL ligands must enter to activate Notch. Development 131, 5367-5380 (2004).
    • (2004) Development , vol.131 , pp. 5367-5380
    • Wang, W.1    Struhl, G.2
  • 27
    • 21644462494 scopus 로고    scopus 로고
    • Distinct roles for Mind bomb, Neuralized and Epsin in mediating DSL endocytosis and signaling in Drosophila
    • Wang, W. & Struhl, G. Distinct roles for Mind bomb, Neuralized and Epsin in mediating DSL endocytosis and signaling in Drosophila. Development 132, 2883-2894 (2005).
    • (2005) Development , vol.132 , pp. 2883-2894
    • Wang, W.1    Struhl, G.2
  • 28
    • 0242558207 scopus 로고    scopus 로고
    • Neurogenic phenotype of mind bomb mutants leads to severe patterning defects in the zebrafish hindbrain
    • Bingham, S. et al. Neurogenic phenotype of mind bomb mutants leads to severe patterning defects in the zebrafish hindbrain. Dev. Dyn. 228, 451-463 (2003).
    • (2003) Dev. Dyn , vol.228 , pp. 451-463
    • Bingham, S.1
  • 29
    • 18844429102 scopus 로고    scopus 로고
    • The ubiquitin ligase Drosophila Mind bomb promotes Notch signaling by regulating the localization and activity of Serrate and Delta
    • Lai, E.C., Roegiers, F., Qin, X., Jan, Y.N. & Rubin, G.M. The ubiquitin ligase Drosophila Mind bomb promotes Notch signaling by regulating the localization and activity of Serrate and Delta. Development 132, 2319-2332 (2005).
    • (2005) Development , vol.132 , pp. 2319-2332
    • Lai, E.C.1    Roegiers, F.2    Qin, X.3    Jan, Y.N.4    Rubin, G.M.5
  • 30
    • 18844452750 scopus 로고    scopus 로고
    • Two distinct E3 ubiquitin ligases have complementary functions in the regulation of delta and serrate signaling in Drosophila
    • Le Borgne, R., Remaud, S., Hamel, S. & Schweisguth, F. Two distinct E3 ubiquitin ligases have complementary functions in the regulation of delta and serrate signaling in Drosophila. PLoS Biol. 3, 688-696 (2005).
    • (2005) PLoS Biol , vol.3 , pp. 688-696
    • Le Borgne, R.1    Remaud, S.2    Hamel, S.3    Schweisguth, F.4
  • 31
    • 0038686503 scopus 로고    scopus 로고
    • Unequal segregation of Neuralized biases Notch activation during asymmetric cell division
    • Le Borgne, R. & Schweisguth, F. Unequal segregation of Neuralized biases Notch activation during asymmetric cell division. Dev. Cell 5, 139-148 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 139-148
    • Le Borgne, R.1    Schweisguth, F.2
  • 32
    • 0035653308 scopus 로고    scopus 로고
    • neuralized encodes a peripheral membrane protein involved in delta signaling and endocytosis
    • Pavlopoulos, E. et al. neuralized encodes a peripheral membrane protein involved in delta signaling and endocytosis. Dev. Cell 1, 807-816 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 807-816
    • Pavlopoulos, E.1
  • 33
    • 0031573944 scopus 로고    scopus 로고
    • Requirement for dynamin during Notch signaling in Drosophila neurogenesis
    • Seugnet, L., Simpson, P. & Haenlin, M. Requirement for dynamin during Notch signaling in Drosophila neurogenesis. Dev. Biol. 192, 585-598 (1997).
    • (1997) Dev. Biol , vol.192 , pp. 585-598
    • Seugnet, L.1    Simpson, P.2    Haenlin, M.3
  • 34
    • 0034051852 scopus 로고    scopus 로고
    • Ligand endocytosis drives receptor dissociation and activation in the Notch pathway
    • Parks, A.L., Klueg, K.M., Stout, J.R. & Muskavitch, M.A. Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. Development 127, 1373-1385 (2000).
    • (2000) Development , vol.127 , pp. 1373-1385
    • Parks, A.L.1    Klueg, K.M.2    Stout, J.R.3    Muskavitch, M.A.4
  • 35
    • 11244321993 scopus 로고    scopus 로고
    • The adhesion force of Notch with Delta and the rate of Notch signaling
    • Ahimou, F., Mok, L.P., Bardot, B. & Wesley, C. The adhesion force of Notch with Delta and the rate of Notch signaling. J. Cell Biol. 167, 1217-1229 (2004).
    • (2004) J. Cell Biol , vol.167 , pp. 1217-1229
    • Ahimou, F.1    Mok, L.P.2    Bardot, B.3    Wesley, C.4
  • 36
    • 0344019404 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme
    • Maskos, K. et al. Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proc. Natl. Acad. Sci. USA 95, 3408-3412 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3408-3412
    • Maskos, K.1
  • 37
    • 33745045658 scopus 로고    scopus 로고
    • Leukemia-associated mutations within the NOTCH1 heterodimerization domain fall into at least two distinct mechanistic classes
    • Malecki, M.J. et al. Leukemia-associated mutations within the NOTCH1 heterodimerization domain fall into at least two distinct mechanistic classes. Mol. Cell. Biol. 26, 4642-4651 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 4642-4651
    • Malecki, M.J.1
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsk, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowsk, Z.1    Minor, W.2
  • 39
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. & Lazmin, V. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463 (1999).
    • (1999) Nat. Struct. Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lazmin, V.3
  • 40
  • 41
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T., Adams, P. & Clore, G. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr D Biol. Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.2    Clore, G.3
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G., Vagin, A. & Dodson, E. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240-245 (1997).
    • (1997) Acta Crystallogr. D Biol. Crystallogr , vol.53 , pp. 240-245
    • Murshudov, G.1    Vagin, A.2    Dodson, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.