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Volumn 288, Issue 19, 2013, Pages 13225-13235

Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly

Author keywords

[No Author keywords available]

Indexed keywords

AUTOINHIBITION; HYDROPHOBIC PATCH; INFLAMMASOME; PYRIN DOMAINS;

EID: 84877692253     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.468033     Document Type: Article
Times cited : (135)

References (60)
  • 2
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., and Alnemri, E. S. (2009) AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 458, 509-513
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.-W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 7
    • 77955294800 scopus 로고    scopus 로고
    • Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol
    • Sauer, J.-D., Witte, C. E., Zemansky, J., Hanson, B., Lauer, P., and Portnoy, D. A. (2010) Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol. Cell Host Microbe 7, 412-419
    • (2010) Cell Host Microbe , vol.7 , pp. 412-419
    • Sauer, J.-D.1    Witte, C.E.2    Zemansky, J.3    Hanson, B.4    Lauer, P.5    Portnoy, D.A.6
  • 9
    • 84859945146 scopus 로고    scopus 로고
    • Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking
    • Ge, J., Gong, Y.-N., Xu, Y., and Shao, F. (2012) Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking. Proc. Natl. Acad. Sci. U.S.A. 109, 6193-6198
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 6193-6198
    • Ge, J.1    Gong, Y.-N.2    Xu, Y.3    Shao, F.4
  • 12
    • 22144490446 scopus 로고    scopus 로고
    • The HIN-200 family: More than interferon-inducible genes?
    • Ludlow, L. E., Johnstone, R. W., and Clarke, C. J. (2005) The HIN-200 family: more than interferon-inducible genes? Exp. Cell Res. 308, 1-17
    • (2005) Exp. Cell Res. , vol.308 , pp. 1-17
    • Ludlow, L.E.1    Johnstone, R.W.2    Clarke, C.J.3
  • 13
    • 84860202518 scopus 로고    scopus 로고
    • A comprehensive manually curated protein-protein interaction database for the death domain superfamily
    • Kwon, D., Yoon, J. H., Shin, S. Y., Jang, T. H., Kim, H. G., So, I., Jeon, J. H., and Park, H. H. (2012) A comprehensive manually curated protein-protein interaction database for the death domain superfamily. Nucleic Acids Res. 40, D331-D336
    • (2012) Nucleic Acids Res , vol.40
    • Kwon, D.1    Yoon, J.H.2    Shin, S.Y.3    Jang, T.H.4    Kim, H.G.5    So, I.6    Jeon, J.H.7    Park, H.H.8
  • 15
    • 0034520137 scopus 로고    scopus 로고
    • The PYRIN domain: A novel motif found in apoptosis and inflammation proteins
    • Bertin, J., and DiStefano, P. S. (2000) The PYRIN domain: a novel motif found in apoptosis and inflammation proteins. Cell Death Differ. 7, 1273-1274
    • (2000) Cell Death Differ , vol.7 , pp. 1273-1274
    • Bertin, J.1    Distefano, P.S.2
  • 16
    • 0035916324 scopus 로고    scopus 로고
    • The pyrin domain: A possible member of the death domain-fold family implicated in apoptosis and inflammation
    • Martinon, F., Hofmann, K., and Tschopp, J. (2001) The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. Curr. Biol. 11, R118-20
    • (2001) Curr. Biol , vol.11
    • Martinon, F.1    Hofmann, K.2    Tschopp, J.3
  • 17
    • 0035253022 scopus 로고    scopus 로고
    • The DAPIN family: A novel domain links apoptotic and interferon response proteins
    • Staub, E., Dahl, E., and Rosenthal, A. (2001) The DAPIN family: a novel domain links apoptotic and interferon response proteins. Trends Biochem. Sci. 26, 83-85
    • (2001) Trends Biochem. Sci , vol.26 , pp. 83-85
    • Staub, E.1    Dahl, E.2    Rosenthal, A.3
  • 18
    • 0035253123 scopus 로고    scopus 로고
    • PAAD-A new protein domain associated with apoptosis, cancer and autoimmune diseases
    • Pawłowski, K., Pio, F., Chu, Z., Reed, J. C., and Godzik, A. (2001) PAAD-a new protein domain associated with apoptosis, cancer and autoimmune diseases. Trends Biochem. Sci. 26, 85-87
    • (2001) Trends Biochem. Sci , vol.26 , pp. 85-87
    • Pawłowski, K.1    Pio, F.2    Chu, Z.3    Reed, J.C.4    Godzik, A.5
  • 20
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park, H. H., Logette, E., Raunser, S., Cuenin, S., Walz, T., Tschopp, J., and Wu, H. (2007) Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 128, 533-546
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3    Cuenin, S.4    Walz, T.5    Tschopp, J.6    Wu, H.7
  • 21
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin, S.-C., Lo, Y.-C., and Wu, H. (2010) Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 465, 885-890
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.-C.1    Lo, Y.-C.2    Wu, H.3
  • 22
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan, D., Jiang, X., Morgan, D. G., Heuser, J. E., Wang, X., and Akey, C. W. (2002) Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 9, 423-432
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 24
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β
    • Martinon, F., Burns, K., and Tschopp, J. (2002) The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10, 417-426
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 25
    • 0042386425 scopus 로고    scopus 로고
    • The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition
    • Liepinsh, E., Barbals, R., Dahl, E., Sharipo, A., Staub, E., and Otting, G. (2003) The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition. J. Mol. Biol. 332, 1155-1163
    • (2003) J. Mol. Biol , vol.332 , pp. 1155-1163
    • Liepinsh, E.1    Barbals, R.2    Dahl, E.3    Sharipo, A.4    Staub, E.5    Otting, G.6
  • 26
    • 70450250064 scopus 로고    scopus 로고
    • Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC)
    • de Alba, E. (2009) Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC). J. Biol. Chem. 284, 32932-32941
    • (2009) J. Biol. Chem , vol.284 , pp. 32932-32941
    • De Alba, E.1
  • 28
    • 80655144737 scopus 로고    scopus 로고
    • Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly
    • Bae, J. Y., and Park, H. H. (2011) Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly. J. Biol. Chem. 286, 39528-39536
    • (2011) J. Biol. Chem , vol.286 , pp. 39528-39536
    • Bae, J.Y.1    Park, H.H.2
  • 30
    • 77956254738 scopus 로고    scopus 로고
    • Three-dimensional structure of the NLRP7 pyrin domain: Insight into pyrin-pyrin-mediated effector domain signaling in innate immunity
    • Pinheiro, A. S., Proell, M., Eibl, C., Page, R., Schwarzenbacher, R., and Peti, W. (2010) Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity. J. Biol. Chem. 285, 27402-27410
    • (2010) J. Biol. Chem , vol.285 , pp. 27402-27410
    • Pinheiro, A.S.1    Proell, M.2    Eibl, C.3    Page, R.4    Schwarzenbacher, R.5    Peti, W.6
  • 32
    • 33845966052 scopus 로고    scopus 로고
    • Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling
    • Natarajan, A., Ghose, R., and Hill, J. M. (2006) Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling. J. Biol. Chem. 281, 31863-31875
    • (2006) J. Biol. Chem , vol.281 , pp. 31863-31875
    • Natarajan, A.1    Ghose, R.2    Hill, J.M.3
  • 36
    • 77951587361 scopus 로고    scopus 로고
    • A synergistic approach to protein crystallization: Combination of a fixedarm carrier with surface entropy reduction
    • Moon, A. F., Mueller, G. A., Zhong, X., and Pedersen, L. C. (2010) A synergistic approach to protein crystallization: combination of a fixedarm carrier with surface entropy reduction. Protein Sci. 19, 901-913
    • (2010) Protein Sci , vol.19 , pp. 901-913
    • Moon, A.F.1    Mueller, G.A.2    Zhong, X.3    Pedersen, L.C.4
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 44
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and Nicholls, A. (1995) Classical electrostatics in biology and chemistry. Science 268, 1144-1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 45
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and Richards, F. M. (1971) The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400
    • (1971) J. Mol. Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 46
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., and Kumar, S. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 28, 2731-2739
    • (2011) Mol. Biol. Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 47
    • 77954257799 scopus 로고    scopus 로고
    • Con-Surf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) Con-Surf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 48
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: Cluspro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov, D., Hall, D. R., Beglov, D., Brenke, R., Comeau, S. R., Shen, Y., Li, K., Zheng, J., Vakili, P., Paschalidis, I. Ch., and Vajda, S. (2010) Achieving reliability and high accuracy in automated protein docking: Cluspro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78, 3124-3130
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5    Shen, Y.6    Li, K.7    Zheng, J.8    Vakili, P.9    Paschalidis, C.I.10    Vajda, S.11
  • 49
    • 77957242885 scopus 로고    scopus 로고
    • Ultra-fast FFT protein docking on graphics processors
    • Ritchie, D. W., and Venkatraman, V. (2010) Ultra-fast FFT protein docking on graphics processors. Bioinformatics 26, 2398-2405
    • (2010) Bioinformatics , vol.26 , pp. 2398-2405
    • Ritchie, D.W.1    Venkatraman, V.2
  • 50
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman, B., Dantas, G., Ireton, G. C., Varani, G., Stoddard, B. L., and Baker, D. (2003) Design of a novel globular protein fold with atomic-level accuracy. Science 302, 1364-1368
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 51
    • 41849132440 scopus 로고    scopus 로고
    • Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain
    • Potter, J. A., Randall, R. E., and Taylor, G. L. (2008) Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain. BMC Struct. Biol. 8, 11
    • (2008) BMC Struct. Biol , vol.8 , pp. 11
    • Potter, J.A.1    Randall, R.E.2    Taylor, G.L.3
  • 52
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2
  • 53
    • 29144463250 scopus 로고    scopus 로고
    • Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition
    • Yang, J. K., Wang, L., Zheng, L., Wan, F., Ahmed, M., Lenardo, M. J., and Wu, H. (2005) Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition. Mol. Cell 20, 939-949
    • (2005) Mol. Cell , vol.20 , pp. 939-949
    • Yang, J.K.1    Wang, L.2    Zheng, L.3    Wan, F.4    Ahmed, M.5    Lenardo, M.J.6    Wu, H.7
  • 54
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • Qin, H., Srinivasula, S. M., Wu, G., Fernandes-Alnemri, T., Alnemri, E. S., and Shi, Y. (1999) Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Nature 399, 549-557
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 56
    • 0035896406 scopus 로고    scopus 로고
    • Adocking model of key components of the DISC complex: Death domain superfamily interactions redefined
    • Weber, C. H., and Vincenz, C. (2001)Adocking model of key components of the DISC complex: death domain superfamily interactions redefined. FEBS Lett. 492, 171-176
    • (2001) FEBS Lett. , vol.492 , pp. 171-176
    • Weber, C.H.1    Vincenz, C.2
  • 57
    • 0033601077 scopus 로고    scopus 로고
    • Threedimensional structure of a complex between the death domains of Pelle and Tube
    • Xiao, T., Towb, P., Wasserman, S. A., and Sprang, S. R. (1999) Threedimensional structure of a complex between the death domains of Pelle and Tube. Cell 99, 545-555
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 58
    • 84865753053 scopus 로고    scopus 로고
    • Crystallographic characterization of mouse AIM2 HIN-200 domain bound to a 15 bp and an 18 bp doublestranded DNA
    • Sung, M. W., Watts, T., and Li, P. (2012) Crystallographic characterization of mouse AIM2 HIN-200 domain bound to a 15 bp and an 18 bp doublestranded DNA. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 1081-1084
    • (2012) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.68 , pp. 1081-1084
    • Sung, M.W.1    Watts, T.2    Li, P.3
  • 59
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski, E., Lunardi, T., McCarthy, A. A., Louber, J., Brunel, J., Grigorov, B., Gerlier, D., and Cusack, S. (2011) Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 147, 423-435
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1    Lunardi, T.2    McCarthy, A.A.3    Louber, J.4    Brunel, J.5    Grigorov, B.6    Gerlier, D.7    Cusack, S.8
  • 60
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl, S. J., Li, W., Chao, Y., Schwarzenbacher, R., and Shi, Y. (2005) Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434, 926-933
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5


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