메뉴 건너뛰기




Volumn 20, Issue 2, 2012, Pages 340-349

Conformational locking upon cooperative assembly of notch transcription complexes

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; DNA; MASTERMIND LIKE 1 PROTEIN; NOTCH RECEPTOR; RAM PROTEIN; UNCLASSIFIED DRUG;

EID: 84863012561     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.12.011     Document Type: Article
Times cited : (54)

References (46)
  • 3
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • DOI 10.1126/science.284.5415.770
    • S. Artavanis-Tsakonas, M.D. Rand, and R.J. Lake Notch signaling: cell fate control and signal integration in development Science 284 1999 770 776 (Pubitemid 29291335)
    • (1999) Science , vol.284 , Issue.5415 , pp. 770-776
    • Artavanis-Tsakonas, S.1    Rand, M.D.2    Lake, R.J.3
  • 4
    • 33644764891 scopus 로고    scopus 로고
    • The Notch transcription activation complex makes its move
    • DOI 10.1016/j.cell.2006.02.028, PII S0092867406002455
    • D. Barrick, and R. Kopan The Notch transcription activation complex makes its move Cell 124 2006 883 885 (Pubitemid 43344226)
    • (2006) Cell , vol.124 , Issue.5 , pp. 883-885
    • Barrick, D.1    Kopan, R.2
  • 5
    • 42449123135 scopus 로고    scopus 로고
    • The effects of conformational heterogeneity on the binding of the Notch intracellular domain to effector proteins: A case of biologically tuned disorder
    • DOI 10.1042/BST0360157
    • A. Bertagna, D. Toptygin, L. Brand, and D. Barrick The effects of conformational heterogeneity on the binding of the Notch intracellular domain to effector proteins: a case of biologically tuned disorder Biochem. Soc. Trans. 36 2008 157 166 (Pubitemid 351570585)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.2 , pp. 157-166
    • Bertagna, A.1    Toptygin, D.2    Brand, L.3    Barrick, D.4
  • 6
    • 33746841062 scopus 로고    scopus 로고
    • The Notch Ankyrin Domain Folds via a Discrete, Centralized Pathway
    • DOI 10.1016/j.str.2006.06.013, PII S0969212606002966
    • C.M. Bradley, and D. Barrick The notch ankyrin domain folds via a discrete, centralized pathway Structure 14 2006 1303 1312 (Pubitemid 44176374)
    • (2006) Structure , vol.14 , Issue.8 , pp. 1303-1312
    • Bradley, C.M.1    Barrick, D.2
  • 7
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: A simple pathway becomes complex
    • DOI 10.1038/nrm2009, PII NRM2009
    • S.J. Bray Notch signalling: a simple pathway becomes complex Nat. Rev. Mol. Cell Biol. 7 2006 678 689 (Pubitemid 44268213)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.9 , pp. 678-689
    • Bray, S.J.1
  • 9
    • 38049018580 scopus 로고    scopus 로고
    • Mutational and energetic studies of Notch 1 transcription complexes
    • C. Del Bianco, J.C. Aster, and S.C. Blacklow Mutational and energetic studies of Notch 1 transcription complexes J. Mol. Biol. 376 2008 131 140
    • (2008) J. Mol. Biol. , vol.376 , pp. 131-140
    • Del Bianco, C.1    Aster, J.C.2    Blacklow, S.C.3
  • 10
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • S.W. Englander, and L. Mayne Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR Annu. Rev. Biophys. Biomol. Struct. 21 1992 243 265
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 11
    • 47249090444 scopus 로고    scopus 로고
    • RAM-induced allostery facilitates assembly of a notch pathway active transcription complex
    • D.R. Friedmann, J.J. Wilson, and R.A. Kovall RAM-induced allostery facilitates assembly of a notch pathway active transcription complex J. Biol. Chem. 283 2008 14781 14791
    • (2008) J. Biol. Chem. , vol.283 , pp. 14781-14791
    • Friedmann, D.R.1    Wilson, J.J.2    Kovall, R.A.3
  • 12
    • 0036606776 scopus 로고    scopus 로고
    • Mastermind mediates chromatin-specific transcription and turnover of the notch enhancer complex
    • DOI 10.1101/gad.991602
    • C.J. Fryer, E. Lamar, I. Turbachova, C. Kintner, and K.A. Jones Mastermind mediates chromatin-specific transcription and turnover of the Notch enhancer complex Genes Dev. 16 2002 1397 1411 (Pubitemid 34615092)
    • (2002) Genes and Development , vol.16 , Issue.11 , pp. 1397-1411
    • Fryer, C.J.1    Lamar, E.2    Turbachova, I.3    Kintner, C.4    Jones, K.A.5
  • 13
    • 8844229536 scopus 로고    scopus 로고
    • Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover
    • DOI 10.1016/j.molcel.2004.10.014, PII S1097276504006409
    • C.J. Fryer, J.B. White, and K.A. Jones Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover Mol. Cell 16 2004 509 520 (Pubitemid 39531875)
    • (2004) Molecular Cell , vol.16 , Issue.4 , pp. 509-520
    • Fryer, C.J.1    White, J.B.2    Jones, K.A.3
  • 14
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • D. Houde, S.A. Berkowitz, and J.R. Engen The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies J. Pharm. Sci. 100 2011 2071 2086
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 15
    • 0000277207 scopus 로고
    • Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions
    • A. Hvidt, and K. Linderstrøm-Lang Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions Biochim. Biophys. Acta 14 1954 574 575
    • (1954) Biochim. Biophys. Acta , vol.14 , pp. 574-575
    • Hvidt, A.1    Linderstrøm-Lang, K.2
  • 16
    • 0028609035 scopus 로고
    • Mass spectrometric measurement of protein amide hydrogen exchange rates of apo-and holo-myoglobin
    • R.S. Johnson, and K.A. Walsh Mass spectrometric measurement of protein amide hydrogen exchange rates of apo-and holo-myoglobin Protein Sci. 3 1994 2411 2418
    • (1994) Protein Sci. , vol.3 , pp. 2411-2418
    • Johnson, R.S.1    Walsh, K.A.2
  • 17
    • 77949893098 scopus 로고    scopus 로고
    • Thermodynamic analysis of the CSL x Notch interaction: Distribution of binding energy of the Notch RAM region to the CSL beta-trefoil domain and the mode of competition with the viral transactivator EBNA2
    • S.E. Johnson, M.X. Ilagan, R. Kopan, and D. Barrick Thermodynamic analysis of the CSL x Notch interaction: distribution of binding energy of the Notch RAM region to the CSL beta-trefoil domain and the mode of competition with the viral transactivator EBNA2 J. Biol. Chem. 285 2010 6681 6692
    • (2010) J. Biol. Chem. , vol.285 , pp. 6681-6692
    • Johnson, S.E.1    Ilagan, M.X.2    Kopan, R.3    Barrick, D.4
  • 18
    • 0026134908 scopus 로고
    • Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry
    • V. Katta, and B.T. Chait Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry Rapid Commun. Mass Spectrom. 5 1991 214 217
    • (1991) Rapid Commun. Mass Spectrom. , vol.5 , pp. 214-217
    • Katta, V.1    Chait, B.T.2
  • 19
    • 79954629044 scopus 로고    scopus 로고
    • MSTools-Web based application for visualization and presentation of HXMS data
    • D. Kavan, and P. Man MSTools-Web based application for visualization and presentation of HXMS data Int. J. Mass Spectrom. 302 2011 53 58
    • (2011) Int. J. Mass Spectrom. , vol.302 , pp. 53-58
    • Kavan, D.1    Man, P.2
  • 21
    • 64249172203 scopus 로고    scopus 로고
    • The canonical Notch signaling pathway: Unfolding the activation mechanism
    • R. Kopan, and M.X. Ilagan The canonical Notch signaling pathway: unfolding the activation mechanism Cell 137 2009 216 233
    • (2009) Cell , vol.137 , pp. 216-233
    • Kopan, R.1    Ilagan, M.X.2
  • 22
    • 4644317278 scopus 로고    scopus 로고
    • Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA
    • DOI 10.1038/sj.emboj.7600349
    • R.A. Kovall, and W.A. Hendrickson Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA EMBO J. 23 2004 3441 3451 (Pubitemid 39265534)
    • (2004) EMBO Journal , vol.23 , Issue.17 , pp. 3441-3451
    • Kovall, R.A.1    Hendrickson, W.A.2
  • 23
    • 77956300942 scopus 로고    scopus 로고
    • Mechanistic insights into Notch receptor signaling from structural and biochemical studies
    • R.A. Kovall, and S.C. Blacklow Mechanistic insights into Notch receptor signaling from structural and biochemical studies Curr. Top. Dev. Biol. 92 2010 31 71
    • (2010) Curr. Top. Dev. Biol. , vol.92 , pp. 31-71
    • Kovall, R.A.1    Blacklow, S.C.2
  • 24
    • 17744366374 scopus 로고    scopus 로고
    • The crystal structure of a partial mouse Notch-1 ankyrin domain: Repeats 4 through 7 preserve an ankyrin fold
    • DOI 10.1110/ps.041184105
    • O.Y. Lubman, R. Kopan, G. Waksman, and S. Korolev The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold Protein Sci. 14 2005 1274 1281 (Pubitemid 40577807)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1274-1281
    • Lubman, O.Y.1    Kopan, R.2    Waksman, G.3    Korolev, S.4
  • 25
    • 33845683490 scopus 로고    scopus 로고
    • Quantitative Dissection of the Notch:CSL Interaction: Insights into the Notch-mediated Transcriptional Switch
    • DOI 10.1016/j.jmb.2006.09.071, PII S0022283606012952
    • O.Y. Lubman, M.X. Ilagan, R. Kopan, and D. Barrick Quantitative dissection of the Notch:CSL interaction: insights into the Notch-mediated transcriptional switch J. Mol. Biol. 365 2007 577 589 (Pubitemid 44960348)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.3 , pp. 577-589
    • Lubman, O.Y.1    Ilagan, Ma.X.G.2    Kopan, R.3    Barrick, D.4
  • 28
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
    • J.S. Mumm, E.H. Schroeter, M.T. Saxena, A. Griesemer, X. Tian, D.J. Pan, W.J. Ray, and R. Kopan A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1 Mol. Cell 5 2000 197 206 (Pubitemid 30628079)
    • (2000) Molecular Cell , vol.5 , Issue.2 , pp. 197-206
    • Mumm, J.S.1    Schroeter, E.H.2    Saxena, M.T.3    Griesemer, A.4    Tian, X.5    Pan, D.J.6    Ray, W.J.7    Kopan, R.8
  • 30
    • 33644749306 scopus 로고    scopus 로고
    • Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes
    • DOI 10.1016/j.cell.2005.12.037, PII S009286740600122X
    • Y. Nam, P. Sliz, L. Song, J.C. Aster, and S.C. Blacklow Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes Cell 124 2006 973 983 (Pubitemid 43344237)
    • (2006) Cell , vol.124 , Issue.5 , pp. 973-983
    • Nam, Y.1    Sliz, P.2    Song, L.3    Aster, J.C.4    Blacklow, S.C.5
  • 31
    • 0038079817 scopus 로고    scopus 로고
    • Structural requirements for assembly of the CSL·intracellular Notch1·Mastermind-like 1 transcriptional activation complex
    • DOI 10.1074/jbc.M301567200
    • Y. Nam, A.P. Weng, J.C. Aster, and S.C. Blacklow Structural requirements for assembly of the CSL.intracellular Notch1.Mastermind-like 1 transcriptional activation complex J. Biol. Chem. 278 2003 21232 21239 (Pubitemid 36806438)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 21232-21239
    • Nam, Y.1    Weng, A.P.2    Aster, J.C.3    Blacklow, S.C.4
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 36749078686 scopus 로고    scopus 로고
    • Combining Efficient Conformational Sampling with a Deformable Elastic Network Model Facilitates Structure Refinement at Low Resolution
    • DOI 10.1016/j.str.2007.09.021, PII S096921260700411X
    • G.F. Schröder, A.T. Brunger, and M. Levitt Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution Structure 15 2007 1630 1641 (Pubitemid 350213409)
    • (2007) Structure , vol.15 , Issue.12 , pp. 1630-1641
    • Schroder, G.F.1    Brunger, A.T.2    Levitt, M.3
  • 36
    • 77951623055 scopus 로고    scopus 로고
    • Super-resolution biomolecular crystallography with low-resolution data
    • G.F. Schröder, M. Levitt, and A.T. Brunger Super-resolution biomolecular crystallography with low-resolution data Nature 464 2010 1218 1222
    • (2010) Nature , vol.464 , pp. 1218-1222
    • Schröder, G.F.1    Levitt, M.2    Brunger, A.T.3
  • 38
    • 79955429963 scopus 로고    scopus 로고
    • Transcriptional repression in the Notch pathway: Thermodynamic characterization of CSL-MINT (Msx2-interacting nuclear target protein) complexes
    • B.D. VanderWielen, Z. Yuan, D.R. Friedmann, and R.A. Kovall Transcriptional repression in the Notch pathway: thermodynamic characterization of CSL-MINT (Msx2-interacting nuclear target protein) complexes J. Biol. Chem. 286 2011 14892 14902
    • (2011) J. Biol. Chem. , vol.286 , pp. 14892-14902
    • Vanderwielen, B.D.1    Yuan, Z.2    Friedmann, D.R.3    Kovall, R.A.4
  • 39
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • T.E. Wales, and J.R. Engen Hydrogen exchange mass spectrometry for the analysis of protein dynamics Mass Spectrom. Rev. 25 2006 158 170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 40
    • 51549121010 scopus 로고    scopus 로고
    • High-speed and high-resolution UPLC separation at zero degrees Celsius
    • T.E. Wales, K.E. Fadgen, G.C. Gerhardt, and J.R. Engen High-speed and high-resolution UPLC separation at zero degrees Celsius Anal. Chem. 80 2008 6815 6820
    • (2008) Anal. Chem. , vol.80 , pp. 6815-6820
    • Wales, T.E.1    Fadgen, K.E.2    Gerhardt, G.C.3    Engen, J.R.4
  • 41
    • 0036840497 scopus 로고    scopus 로고
    • P300 and PCAF act cooperatively to mediate transcriptional activation from chromatin templates by Notch intracellular domains in vitro
    • DOI 10.1128/MCB.22.22.7812-7819.2002
    • A.E. Wallberg, K. Pedersen, U. Lendahl, and R.G. Roeder p300 and PCAF act cooperatively to mediate transcriptional activation from chromatin templates by notch intracellular domains in vitro Mol. Cell. Biol. 22 2002 7812 7819 (Pubitemid 35217292)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.22 , pp. 7812-7819
    • Wallberg, A.E.1    Pedersen, K.2    Lendahl, U.3    Roeder, R.G.4
  • 42
    • 33751337111 scopus 로고    scopus 로고
    • Semi-Automated Data Processing of Hydrogen Exchange Mass Spectra Using HX-Express
    • DOI 10.1016/j.jasms.2006.07.025, PII S1044030506006891
    • D.D. Weis, J.R. Engen, and I.J. Kass Semi-automated data processing of hydrogen exchange mass spectra using HX-Express J. Am. Soc. Mass Spectrom. 17 2006 1700 1703 (Pubitemid 44809951)
    • (2006) Journal of the American Society for Mass Spectrometry , vol.17 , Issue.12 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 43
    • 0037218811 scopus 로고    scopus 로고
    • Growth suppression of pre-T acute lymphoblastic leukemia cells by inhibition of NOTCH signaling
    • DOI 10.1128/MCB.23.2.655-664.2003
    • A.P. Weng, Y. Nam, M.S. Wolfe, W.S. Pear, J.D. Griffin, S.C. Blacklow, and J.C. Aster Growth suppression of pre-T acute lymphoblastic leukemia cells by inhibition of notch signaling Mol. Cell. Biol. 23 2003 655 664 (Pubitemid 36050558)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.2 , pp. 655-664
    • Weng, A.P.1    Nam, Y.2    Wolfe, M.S.3    Pear, W.S.4    Griffin, J.D.5    Blacklow, S.C.6    Aster, J.C.7
  • 45
    • 33644761961 scopus 로고    scopus 로고
    • Crystal structure of the CSL-Notch-Mastermind Ternary complex bound to DNA
    • DOI 10.1016/j.cell.2006.01.035, PII S009286740600170X
    • J.J. Wilson, and R.A. Kovall Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA Cell 124 2006 985 996 (Pubitemid 43344238)
    • (2006) Cell , vol.124 , Issue.5 , pp. 985-996
    • Wilson, J.J.1    Kovall, R.A.2
  • 46
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Z. Zhang, and D.L. Smith Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation Protein Sci. 2 1993 522 531 (Pubitemid 23119303)
    • (1993) Protein Science , vol.2 , Issue.4 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.