메뉴 건너뛰기




Volumn 113, Issue 33, 2016, Pages E4857-E4866

Site-specific phosphorylation and microtubule dynamics control Pyrin inflammasome activation

Author keywords

FMF; Inflammasome; Phosphorylation; Pyrin; Rho toxins

Indexed keywords

COLCHICINE; INFLAMMASOME; INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEIN 14 3 3; PYRIN INFLAMMASOME; SERINE; SERINE 205; SERINE 241; UNCLASSIFIED DRUG; BACTERIAL TOXIN; ENTEROTOXIN; PYRIN; TCDA PROTEIN, CLOSTRIDIUM DIFFICILE; TUBULIN MODULATOR;

EID: 84982091531     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1601700113     Document Type: Article
Times cited : (186)

References (43)
  • 1
    • 84901310586 scopus 로고    scopus 로고
    • Mechanisms and functions of inflammasomes
    • Lamkanfi M, Dixit VM (2014) Mechanisms and functions of inflammasomes. Cell 157 (5):1013-1022.
    • (2014) Cell , vol.157 , Issue.5 , pp. 1013-1022
    • Lamkanfi, M.1    Dixit, V.M.2
  • 2
    • 84946925072 scopus 로고    scopus 로고
    • Diverse mechanisms for inflammasome sensing of cytosolic bacteria and bacterial virulence
    • Zhao Y, Shao F (2016) Diverse mechanisms for inflammasome sensing of cytosolic bacteria and bacterial virulence. Curr Opin Microbiol 29:37-42.
    • (2016) Curr Opin Microbiol , vol.29 , pp. 37-42
    • Zhao, Y.1    Shao, F.2
  • 5
    • 84942892037 scopus 로고    scopus 로고
    • Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
    • Shi J, et al. (2015) Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 526 (7575):660-665.
    • (2015) Nature , vol.526 , Issue.7575 , pp. 660-665
    • Shi, J.1
  • 6
    • 84942856523 scopus 로고    scopus 로고
    • Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
    • Kayagaki N, et al. (2015) Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526 (7575):666-671.
    • (2015) Nature , vol.526 , Issue.7575 , pp. 666-671
    • Kayagaki, N.1
  • 7
    • 84906571225 scopus 로고    scopus 로고
    • Inflammatory caspases are innate immune receptors for intracellular LPS
    • Shi J, et al. (2014) Inflammatory caspases are innate immune receptors for intracellular LPS. Nature 514 (7521):187-192.
    • (2014) Nature , vol.514 , Issue.7521 , pp. 187-192
    • Shi, J.1
  • 8
    • 84921461716 scopus 로고    scopus 로고
    • Non-canonical activation of inflammatory caspases by cytosolic LPS in innate immunity
    • Yang J, Zhao Y, Shao F (2015) Non-canonical activation of inflammatory caspases by cytosolic LPS in innate immunity. Curr Opin Immunol 32:78-83.
    • (2015) Curr Opin Immunol , vol.32 , pp. 78-83
    • Yang, J.1    Zhao, Y.2    Shao, F.3
  • 9
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J (2002) The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 10 (2):417-426.
    • (2002) Mol Cell , vol.10 , Issue.2 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 10
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed EM, Vance RE (2011) Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 477 (7366):592-595.
    • (2011) Nature , vol.477 , Issue.7366 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 11
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao Y, et al. (2011) The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 477 (7366):596-600.
    • (2011) Nature , vol.477 , Issue.7366 , pp. 596-600
    • Zhao, Y.1
  • 12
    • 84885439494 scopus 로고    scopus 로고
    • Cutting edge: Mouse NAIP1 detects the type III secretion system needle protein
    • Rayamajhi M, Zak DE, Chavarria-Smith J, Vance RE, Miao EA (2013) Cutting edge: Mouse NAIP1 detects the type III secretion system needle protein. J Immunol 191 (8): 3986-3989.
    • (2013) J Immunol , vol.191 , Issue.8 , pp. 3986-3989
    • Rayamajhi, M.1    Zak, D.E.2    Chavarria-Smith, J.3    Vance, R.E.4    Miao, E.A.5
  • 13
    • 84883329029 scopus 로고    scopus 로고
    • Human NAIP and mouse NAIP1 recognize bacterial type III secretion needle protein for inflammasome activation
    • Yang J, Zhao Y, Shi J, Shao F (2013) Human NAIP and mouse NAIP1 recognize bacterial type III secretion needle protein for inflammasome activation. Proc Natl Acad Sci USA 110 (35):14408-14413.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.35 , pp. 14408-14413
    • Yang, J.1    Zhao, Y.2    Shi, J.3    Shao, F.4
  • 14
    • 84898031590 scopus 로고    scopus 로고
    • Molecular basis for specific recognition of bacterial ligands by NAIP/NLRC4 inflammasomes
    • Tenthorey JL, Kofoed EM, Daugherty MD, Malik HS, Vance RE (2014) Molecular basis for specific recognition of bacterial ligands by NAIP/NLRC4 inflammasomes. Mol Cell 54 (1):17-29.
    • (2014) Mol Cell , vol.54 , Issue.1 , pp. 17-29
    • Tenthorey, J.L.1    Kofoed, E.M.2    Daugherty, M.D.3    Malik, H.S.4    Vance, R.E.5
  • 15
    • 84927774890 scopus 로고    scopus 로고
    • The NAIP-NLRC4 inflammasome in innate immune detection of bacterial flagellin and type III secretion apparatus
    • Zhao Y, Shao F (2015) The NAIP-NLRC4 inflammasome in innate immune detection of bacterial flagellin and type III secretion apparatus. Immunol Rev 265 (1):85-102.
    • (2015) Immunol Rev , vol.265 , Issue.1 , pp. 85-102
    • Zhao, Y.1    Shao, F.2
  • 16
    • 80052152283 scopus 로고    scopus 로고
    • The PYHIN protein family as mediators of host defenses
    • Schattgen SA, Fitzgerald KA (2011) The PYHIN protein family as mediators of host defenses. Immunol Rev 243 (1):109-118.
    • (2011) Immunol Rev , vol.243 , Issue.1 , pp. 109-118
    • Schattgen, S.A.1    Fitzgerald, K.A.2
  • 17
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • Anonymous; French FMF Consortium (1997) A candidate gene for familial Mediterranean fever. Nat Genet 17 (1):25-31.
    • (1997) Nat Genet , vol.17 , Issue.1 , pp. 25-31
    • Anonymous1
  • 18
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever
    • Anonymous; The International FMF Consortium (1997) Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. Cell 90 (4):797-807.
    • (1997) Cell , vol.90 , Issue.4 , pp. 797-807
    • Anonymous1
  • 19
    • 69049085064 scopus 로고    scopus 로고
    • Advances in the understanding of familial Mediterranean fever and possibilities for targeted therapy
    • Chae JJ, Aksentijevich I, Kastner DL (2009) Advances in the understanding of familial Mediterranean fever and possibilities for targeted therapy. Br J Haematol 146 (5): 467-478.
    • (2009) Br J Haematol , vol.146 , Issue.5 , pp. 467-478
    • Chae, J.J.1    Aksentijevich, I.2    Kastner, D.L.3
  • 20
    • 30844432876 scopus 로고    scopus 로고
    • Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization
    • Yu JW, et al. (2006) Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization. Cell Death Differ 13 (2):236-249.
    • (2006) Cell Death Differ , vol.13 , Issue.2 , pp. 236-249
    • Yu, J.W.1
  • 21
    • 79956299492 scopus 로고    scopus 로고
    • Gain-of-function Pyrin mutations induce NLRP3 proteinindependent interleukin-1β activation and severe autoinflammation in mice
    • Chae JJ, et al. (2011) Gain-of-function Pyrin mutations induce NLRP3 proteinindependent interleukin-1β activation and severe autoinflammation in mice. Immunity 34 (5):755-768.
    • (2011) Immunity , vol.34 , Issue.5 , pp. 755-768
    • Chae, J.J.1
  • 22
    • 84907270863 scopus 로고    scopus 로고
    • Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome
    • Xu H, et al. (2014) Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature 513 (7517):237-241.
    • (2014) Nature , vol.513 , Issue.7517 , pp. 237-241
    • Xu, H.1
  • 23
    • 84964664672 scopus 로고    scopus 로고
    • A burkholderia type VI effector deamidates rho gtpases to activate the pyrin inflammasome and trigger inflammation
    • Aubert DF, et al. (2016) A Burkholderia Type VI Effector Deamidates Rho GTPases to Activate the Pyrin Inflammasome and Trigger Inflammation. Cell Host Microbe 19 (5): 664-674.
    • (2016) Cell Host Microbe , vol.19 , Issue.5 , pp. 664-674
    • Aubert, D.F.1
  • 24
    • 60549111042 scopus 로고    scopus 로고
    • Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin
    • Waite AL, et al. (2009) Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin. Exp Biol Med (Maywood) 234 (1):40-52.
    • (2009) Exp Biol Med (Maywood , vol.234 , Issue.1 , pp. 40-52
    • Waite, A.L.1
  • 25
    • 84940453310 scopus 로고    scopus 로고
    • Aberrant actin depolymerization triggers the pyrin inflammasome and autoinflammatory disease that is dependent on IL-18, not IL-1β
    • Kim ML, et al. (2015) Aberrant actin depolymerization triggers the pyrin inflammasome and autoinflammatory disease that is dependent on IL-18, not IL-1β. J Exp Med 212 (6):927-938.
    • (2015) J Exp Med , vol.212 , Issue.6 , pp. 927-938
    • Kim, M.L.1
  • 26
    • 0021995801 scopus 로고
    • Effects of Clostridium difficile toxins given intragastrically to animals
    • Lyerly DM, Saum KE, MacDonald DK, Wilkins TD (1985) Effects of Clostridium difficile toxins given intragastrically to animals. Infect Immun 47 (2):349-352.
    • (1985) Infect Immun , vol.47 , Issue.2 , pp. 349-352
    • Lyerly, D.M.1    Saum, K.E.2    MacDonald, D.K.3    Wilkins, T.D.4
  • 27
    • 0029011449 scopus 로고
    • The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins
    • Just I, et al. (1995) The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. J Biol Chem 270 (23):13932-13936.
    • (1995) J Biol Chem , vol.270 , Issue.23 , pp. 13932-13936
    • Just, I.1
  • 28
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: The ABCD model
    • Jank T, Aktories K (2008) Structure and mode of action of clostridial glucosylating toxins: The ABCD model. Trends Microbiol 16 (5):222-229.
    • (2008) Trends Microbiol , vol.16 , Issue.5 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 29
    • 67349114409 scopus 로고    scopus 로고
    • Toxin B is essential for virulence of Clostridium difficile
    • Lyras D, et al. (2009) Toxin B is essential for virulence of Clostridium difficile. Nature 458 (7242):1176-1179.
    • (2009) Nature , vol.458 , Issue.7242 , pp. 1176-1179
    • Lyras, D.1
  • 30
    • 77957988127 scopus 로고    scopus 로고
    • The role of toxin A and toxin B in Clostridium difficile infection
    • Kuehne SA, et al. (2010) The role of toxin A and toxin B in Clostridium difficile infection. Nature 467 (7316):711-713.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 711-713
    • Kuehne, S.A.1
  • 31
    • 77955482224 scopus 로고    scopus 로고
    • Clostridium difficile toxin-induced inflammation and intestinal injury are mediated by the inflammasome
    • Ng J, et al. (2010) Clostridium difficile toxin-induced inflammation and intestinal injury are mediated by the inflammasome. Gastroenterology 139 (2):542-552.
    • (2010) Gastroenterology , vol.139 , Issue.2 , pp. 542-552
    • Ng, J.1
  • 32
    • 20744453230 scopus 로고    scopus 로고
    • Interaction of pyrin with 14.3.3 in an isoform-specific and phosphorylation-dependent manner regulates its translocation to the nucleus
    • Jéru I, et al. (2005) Interaction of pyrin with 14.3.3 in an isoform-specific and phosphorylation-dependent manner regulates its translocation to the nucleus. Arthritis Rheum 52 (6):1848-1857.
    • (2005) Arthritis Rheum , vol.52 , Issue.6 , pp. 1848-1857
    • Jéru, I.1
  • 33
    • 80455154960 scopus 로고    scopus 로고
    • Structural basis of 14-3-3 protein functions
    • Obsil T, Obsilova V (2011) Structural basis of 14-3-3 protein functions. Semin Cell Dev Biol 22 (7):663-672.
    • (2011) Semin Cell Dev Biol , vol.22 , Issue.7 , pp. 663-672
    • Obsil, T.1    Obsilova, V.2
  • 34
    • 33751248527 scopus 로고    scopus 로고
    • Structural basis for protein-protein interactions in the 14-3-3 protein family
    • Yang X, et al. (2006) Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc Natl Acad Sci USA 103 (46):17237-17242.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.46 , pp. 17237-17242
    • Yang, X.1
  • 35
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa C, et al. (1998) 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J Biol Chem 273 (26): 16305-16310.
    • (1998) J Biol Chem , vol.273 , Issue.26 , pp. 16305-16310
    • Petosa, C.1
  • 36
    • 0029046812 scopus 로고
    • Crystal structure of the zeta isoform of the 14-3-3 protein
    • Liu D, et al. (1995) Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 376 (6536):191-194.
    • (1995) Nature , vol.376 , Issue.6536 , pp. 191-194
    • Liu, D.1
  • 37
    • 73349138284 scopus 로고    scopus 로고
    • Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE
    • Kinoshita E, Kinoshita-Kikuta E, Koike T (2009) Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE. Nat Protoc 4 (10):1513-1521.
    • (2009) Nat Protoc , vol.4 , Issue.10 , pp. 1513-1521
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Koike, T.3
  • 38
    • 0035437141 scopus 로고    scopus 로고
    • The familial Mediterranean fever protein, pyrin, associates with microtubules and colocalizes with actin filaments
    • Mansfield E, et al. (2001) The familial Mediterranean fever protein, pyrin, associates with microtubules and colocalizes with actin filaments. Blood 98 (3):851-859.
    • (2001) Blood , vol.98 , Issue.3 , pp. 851-859
    • Mansfield, E.1
  • 39
    • 84876567161 scopus 로고    scopus 로고
    • Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome
    • Misawa T, et al. (2013) Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome. Nat Immunol 14 (5):454-460.
    • (2013) Nat Immunol , vol.14 , Issue.5 , pp. 454-460
    • Misawa, T.1
  • 40
    • 19544393159 scopus 로고    scopus 로고
    • Structural basis for the regulation of tubulin by vinblastine
    • Gigant B, et al. (2005) Structural basis for the regulation of tubulin by vinblastine. Nature 435 (7041):519-522.
    • (2005) Nature , vol.435 , Issue.7041 , pp. 519-522
    • Gigant, B.1
  • 41
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli RB, et al. (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428 (6979):198-202.
    • (2004) Nature , vol.428 , Issue.6979 , pp. 198-202
    • Ravelli, R.B.1
  • 42
    • 84897109910 scopus 로고    scopus 로고
    • The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization
    • Prota AE, et al. (2014) The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization. J Mol Biol 426 (8):1848-1860.
    • (2014) J Mol Biol , vol.426 , Issue.8 , pp. 1848-1860
    • Prota, A.E.1
  • 43
    • 78649819208 scopus 로고    scopus 로고
    • Chemical probing reveals insights into the signaling mechanism of inflammasome activation
    • Gong Y-N, et al. (2010) Chemical probing reveals insights into the signaling mechanism of inflammasome activation. Cell Res 20 (12):1289-1305.
    • (2010) Cell Res , vol.20 , Issue.12 , pp. 1289-1305
    • Gong, Y.-N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.