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Volumn 17, Issue 1, 2016, Pages 221-232

MALT1 Protease Activation Triggers Acute Disruption of Endothelial Barrier Integrity via CYLD Cleavage

Author keywords

Bcl10; CARD10; CARMA3; CYLD; endothelial permeability; G protein coupled receptor (GPCR); MALT1 protease; NF B; Protease activated receptor 1 (PAR1); thrombin

Indexed keywords

CYLD PROTEIN; DEUBIQUITINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MALT1 PROTEIN; PROTEINASE; THROMBIN; UNCLASSIFIED DRUG; CARD10 PROTEIN, MOUSE; CASPASE; CASPASE RECRUITMENT DOMAIN SIGNALING PROTEIN; CYLD PROTEIN, MOUSE; CYSTEINE PROTEINASE; I KAPPA B KINASE; MALT1 PROTEIN, MOUSE; PROTEINASE ACTIVATED RECEPTOR 1; TUMOR PROTEIN;

EID: 84989917883     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2016.08.080     Document Type: Article
Times cited : (31)

References (62)
  • 1
    • 84940724626 scopus 로고    scopus 로고
    • MALT1–a universal soldier: multiple strategies to ensure NF-κB activation and target gene expression
    • Afonina, I.S., Elton, L., Carpentier, I., Beyaert, R., MALT1–a universal soldier: multiple strategies to ensure NF-κB activation and target gene expression. FEBS J. 282 (2015), 3286–3297.
    • (2015) FEBS J. , vol.282 , pp. 3286-3297
    • Afonina, I.S.1    Elton, L.2    Carpentier, I.3    Beyaert, R.4
  • 2
    • 84948115174 scopus 로고    scopus 로고
    • Control of microtubule organization and dynamics: two ends in the limelight
    • Akhmanova, A., Steinmetz, M.O., Control of microtubule organization and dynamics: two ends in the limelight. Nat. Rev. Mol. Cell Biol. 16 (2015), 711–726.
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 711-726
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 3
    • 80053384105 scopus 로고    scopus 로고
    • plusTipTracker: Quantitative image analysis software for the measurement of microtubule dynamics
    • Applegate, K.T., Besson, S., Matov, A., Bagonis, M.H., Jaqaman, K., Danuser, G., plusTipTracker: Quantitative image analysis software for the measurement of microtubule dynamics. J. Struct. Biol. 176 (2011), 168–184.
    • (2011) J. Struct. Biol. , vol.176 , pp. 168-184
    • Applegate, K.T.1    Besson, S.2    Matov, A.3    Bagonis, M.H.4    Jaqaman, K.5    Danuser, G.6
  • 4
    • 1642564595 scopus 로고    scopus 로고
    • Microtubule depolymerization rapidly collapses capillary tube networks in vitro and angiogenic vessels in vivo through the small GTPase Rho
    • Bayless, K.J., Davis, G.E., Microtubule depolymerization rapidly collapses capillary tube networks in vitro and angiogenic vessels in vivo through the small GTPase Rho. J. Biol. Chem. 279 (2004), 11686–11695.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11686-11695
    • Bayless, K.J.1    Davis, G.E.2
  • 5
    • 34249794861 scopus 로고    scopus 로고
    • Microtubule-associated proteins as targets in cancer chemotherapy
    • Bhat, K.M., Setaluri, V., Microtubule-associated proteins as targets in cancer chemotherapy. Clin. Cancer Res. 13 (2007), 2849–2854.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 2849-2854
    • Bhat, K.M.1    Setaluri, V.2
  • 7
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp, T.R., Nijman, S.M., Dirac, A.M., Bernards, R., Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424 (2003), 797–801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 9
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin, S.R., Thrombin signalling and protease-activated receptors. Nature 407 (2000), 258–264.
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 10
    • 78650648858 scopus 로고    scopus 로고
    • Thrombin-dependent NF-κB activation and monocyte/endothelial adhesion are mediated by the CARMA3·Bcl10·MALT1 signalosome
    • Delekta, P.C., Apel, I.J., Gu, S., Siu, K., Hattori, Y., McAllister-Lucas, L.M., Lucas, P.C., Thrombin-dependent NF-κB activation and monocyte/endothelial adhesion are mediated by the CARMA3·Bcl10·MALT1 signalosome. J. Biol. Chem. 285 (2010), 41432–41442.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41432-41442
    • Delekta, P.C.1    Apel, I.J.2    Gu, S.3    Siu, K.4    Hattori, Y.5    McAllister-Lucas, L.M.6    Lucas, P.C.7
  • 11
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek, S.M., Garcia, J.G., Cytoskeletal regulation of pulmonary vascular permeability. J. Appl. Physiol. 91 (2001), 1487–1500.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 14
    • 44049088740 scopus 로고    scopus 로고
    • The tumor suppressor CYLD regulates microtubule dynamics and plays a role in cell migration
    • Gao, J., Huo, L., Sun, X., Liu, M., Li, D., Dong, J.T., Zhou, J., The tumor suppressor CYLD regulates microtubule dynamics and plays a role in cell migration. J. Biol. Chem. 283 (2008), 8802–8809.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8802-8809
    • Gao, J.1    Huo, L.2    Sun, X.3    Liu, M.4    Li, D.5    Dong, J.T.6    Zhou, J.7
  • 15
    • 77953284316 scopus 로고    scopus 로고
    • CYLD regulates angiogenesis by mediating vascular endothelial cell migration
    • Gao, J., Sun, L., Huo, L., Liu, M., Li, D., Zhou, J., CYLD regulates angiogenesis by mediating vascular endothelial cell migration. Blood 115 (2010), 4130–4137.
    • (2010) Blood , vol.115 , pp. 4130-4137
    • Gao, J.1    Sun, L.2    Huo, L.3    Liu, M.4    Li, D.5    Zhou, J.6
  • 16
    • 84937526813 scopus 로고    scopus 로고
    • Microtubule-associated protein EB3 regulates IP3 receptor clustering and Ca(2+) signaling in endothelial cells
    • Geyer, M., Huang, F., Sun, Y., Vogel, S.M., Malik, A.B., Taylor, C.W., Komarova, Y.A., Microtubule-associated protein EB3 regulates IP3 receptor clustering and Ca(2+) signaling in endothelial cells. Cell Rep. 12 (2015), 79–89.
    • (2015) Cell Rep. , vol.12 , pp. 79-89
    • Geyer, M.1    Huang, F.2    Sun, Y.3    Vogel, S.M.4    Malik, A.B.5    Taylor, C.W.6    Komarova, Y.A.7
  • 20
    • 84945496884 scopus 로고    scopus 로고
    • Inflammation and plaque vulnerability
    • Hansson, G.K., Libby, P., Tabas, I., Inflammation and plaque vulnerability. J. Intern. Med. 278 (2015), 483–493.
    • (2015) J. Intern. Med. , vol.278 , pp. 483-493
    • Hansson, G.K.1    Libby, P.2    Tabas, I.3
  • 21
    • 33847725166 scopus 로고    scopus 로고
    • The roles of proteinase-activated receptors in the vascular physiology and pathophysiology
    • Hirano, K., The roles of proteinase-activated receptors in the vascular physiology and pathophysiology. Arterioscler. Thromb. Vasc. Biol. 27 (2007), 27–36.
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 27-36
    • Hirano, K.1
  • 22
    • 84964727060 scopus 로고    scopus 로고
    • Role of the CARMA1/BCL10/MALT1 complex in lymphoid malignancies
    • Juilland, M., Thome, M., Role of the CARMA1/BCL10/MALT1 complex in lymphoid malignancies. Curr. Opin. Hematol. 23 (2016), 402–409.
    • (2016) Curr. Opin. Hematol. , vol.23 , pp. 402-409
    • Juilland, M.1    Thome, M.2
  • 24
    • 84941691131 scopus 로고    scopus 로고
    • Cytoskeletal mechanisms regulating vascular endothelial barrier function in response to acute lung injury
    • Kása, A., Csortos, C., Verin, A.D., Cytoskeletal mechanisms regulating vascular endothelial barrier function in response to acute lung injury. Tissue Barriers, 3, 2015, e974448.
    • (2015) Tissue Barriers , vol.3 , pp. e974448
    • Kása, A.1    Csortos, C.2    Verin, A.D.3
  • 25
    • 33846083165 scopus 로고    scopus 로고
    • Bcl10 and Malt1 control lysophosphatidic acid-induced NF-kappaB activation and cytokine production
    • Klemm, S., Zimmermann, S., Peschel, C., Mak, T.W., Ruland, J., Bcl10 and Malt1 control lysophosphatidic acid-induced NF-kappaB activation and cytokine production. Proc. Natl. Acad. Sci. USA 104 (2007), 134–138.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 134-138
    • Klemm, S.1    Zimmermann, S.2    Peschel, C.3    Mak, T.W.4    Ruland, J.5
  • 26
    • 0036228955 scopus 로고    scopus 로고
    • Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton
    • Krendel, M., Zenke, F.T., Bokoch, G.M., Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nat. Cell Biol. 4 (2002), 294–301.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 294-301
    • Krendel, M.1    Zenke, F.T.2    Bokoch, G.M.3
  • 27
    • 84897968714 scopus 로고    scopus 로고
    • CYLD coordinates with EB1 to regulate microtubule dynamics and cell migration
    • Li, D., Gao, J., Yang, Y., Sun, L., Suo, S., Luo, Y., Shui, W., Zhou, J., Liu, M., CYLD coordinates with EB1 to regulate microtubule dynamics and cell migration. Cell Cycle 13 (2014), 974–983.
    • (2014) Cell Cycle , vol.13 , pp. 974-983
    • Li, D.1    Gao, J.2    Yang, Y.3    Sun, L.4    Suo, S.5    Luo, Y.6    Shui, W.7    Zhou, J.8    Liu, M.9
  • 28
    • 65249179023 scopus 로고    scopus 로고
    • CXCL8/IL8 stimulates vascular endothelial growth factor (VEGF) expression and the autocrine activation of VEGFR2 in endothelial cells by activating NFkappaB through the CBM (Carma3/Bcl10/Malt1) complex
    • Martin, D., Galisteo, R., Gutkind, J.S., CXCL8/IL8 stimulates vascular endothelial growth factor (VEGF) expression and the autocrine activation of VEGFR2 in endothelial cells by activating NFkappaB through the CBM (Carma3/Bcl10/Malt1) complex. J. Biol. Chem. 284 (2009), 6038–6042.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6038-6042
    • Martin, D.1    Galisteo, R.2    Gutkind, J.S.3
  • 35
    • 33644839612 scopus 로고    scopus 로고
    • Signaling mechanisms regulating endothelial permeability
    • Mehta, D., Malik, A.B., Signaling mechanisms regulating endothelial permeability. Physiol. Rev. 86 (2006), 279–367.
    • (2006) Physiol. Rev. , vol.86 , pp. 279-367
    • Mehta, D.1    Malik, A.B.2
  • 38
    • 0026553098 scopus 로고
    • Evans blue dye as a marker of albumin clearance in cultured endothelial monolayer and isolated lung
    • Patterson, C.E., Rhoades, R.A., Garcia, J.G., Evans blue dye as a marker of albumin clearance in cultured endothelial monolayer and isolated lung. J. Appl. Physiol. 72 (1992), 865–873.
    • (1992) J. Appl. Physiol. , vol.72 , pp. 865-873
    • Patterson, C.E.1    Rhoades, R.A.2    Garcia, J.G.3
  • 39
    • 85027937448 scopus 로고    scopus 로고
    • Genetic errors of the human caspase recruitment domain-B-cell lymphoma 10-mucosa-associated lymphoid tissue lymphoma-translocation gene 1 (CBM) complex: Molecular, immunologic, and clinical heterogeneity
    • Pérez de Diego, R., Sánchez-Ramón, S., López-Collazo, E., Martínez-Barricarte, R., Cubillos-Zapata, C., Ferreira Cerdán, A., Casanova, J.L., Puel, A., Genetic errors of the human caspase recruitment domain-B-cell lymphoma 10-mucosa-associated lymphoid tissue lymphoma-translocation gene 1 (CBM) complex: Molecular, immunologic, and clinical heterogeneity. J. Allergy Clin. Immunol. 136 (2015), 1139–1149.
    • (2015) J. Allergy Clin. Immunol. , vol.136 , pp. 1139-1149
    • Pérez de Diego, R.1    Sánchez-Ramón, S.2    López-Collazo, E.3    Martínez-Barricarte, R.4    Cubillos-Zapata, C.5    Ferreira Cerdán, A.6    Casanova, J.L.7    Puel, A.8
  • 43
    • 0141751697 scopus 로고    scopus 로고
    • Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase
    • Somlyo, A.P., Somlyo, A.V., Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83 (2003), 1325–1358.
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 45
    • 44449177553 scopus 로고    scopus 로고
    • A20 is a negative regulator of BCL10- and CARMA3-mediated activation of NF-kappaB
    • Stilo, R., Varricchio, E., Liguoro, D., Leonardi, A., Vito, P., A20 is a negative regulator of BCL10- and CARMA3-mediated activation of NF-kappaB. J. Cell Sci. 121 (2008), 1165–1171.
    • (2008) J. Cell Sci. , vol.121 , pp. 1165-1171
    • Stilo, R.1    Varricchio, E.2    Liguoro, D.3    Leonardi, A.4    Vito, P.5
  • 46
    • 84941422122 scopus 로고    scopus 로고
    • Impedance analysis of GPCR-mediated changes in endothelial barrier function: overview and fundamental considerations for stable and reproducible measurements
    • Stolwijk, J.A., Matrougui, K., Renken, C.W., Trebak, M., Impedance analysis of GPCR-mediated changes in endothelial barrier function: overview and fundamental considerations for stable and reproducible measurements. Pflugers Arch. 467 (2015), 2193–2218.
    • (2015) Pflugers Arch. , vol.467 , pp. 2193-2218
    • Stolwijk, J.A.1    Matrougui, K.2    Renken, C.W.3    Trebak, M.4
  • 47
    • 85026337518 scopus 로고    scopus 로고
    • Mechanisms regulating endothelial permeability
    • Sukriti, S., Tauseef, M., Yazbeck, P., Mehta, D., Mechanisms regulating endothelial permeability. Pulm. Circ. 4 (2014), 535–551.
    • (2014) Pulm. Circ. , vol.4 , pp. 535-551
    • Sukriti, S.1    Tauseef, M.2    Yazbeck, P.3    Mehta, D.4
  • 48
    • 77449150629 scopus 로고    scopus 로고
    • CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
    • Sun, S.C., CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes. Cell Death Differ. 17 (2010), 25–34.
    • (2010) Cell Death Differ. , vol.17 , pp. 25-34
    • Sun, S.C.1
  • 49
    • 2442612540 scopus 로고    scopus 로고
    • CARMA1, BCL-10 and MALT1 in lymphocyte development and activation
    • Thome, M., CARMA1, BCL-10 and MALT1 in lymphocyte development and activation. Nat. Rev. Immunol. 4 (2004), 348–359.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 348-359
    • Thome, M.1
  • 55
    • 33846034844 scopus 로고    scopus 로고
    • Bcl10 plays a critical role in NF-kappaB activation induced by G protein-coupled receptors
    • Wang, D., You, Y., Lin, P.C., Xue, L., Morris, S.W., Zeng, H., Wen, R., Lin, X., Bcl10 plays a critical role in NF-kappaB activation induced by G protein-coupled receptors. Proc. Natl. Acad. Sci. USA 104 (2007), 145–150.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 145-150
    • Wang, D.1    You, Y.2    Lin, P.C.3    Xue, L.4    Morris, S.W.5    Zeng, H.6    Wen, R.7    Lin, X.8
  • 56
    • 81255188900 scopus 로고    scopus 로고
    • Atherosclerosis: current pathogenesis and therapeutic options
    • Weber, C., Noels, H., Atherosclerosis: current pathogenesis and therapeutic options. Nat. Med. 17 (2011), 1410–1422.
    • (2011) Nat. Med. , vol.17 , pp. 1410-1422
    • Weber, C.1    Noels, H.2
  • 57
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S., Weber, K., Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 4 (2003), 938–947.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 58
    • 75649119696 scopus 로고    scopus 로고
    • CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin
    • Wickström, S.A., Masoumi, K.C., Khochbin, S., Fässler, R., Massoumi, R., CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin. EMBO J. 29 (2010), 131–144.
    • (2010) EMBO J. , vol.29 , pp. 131-144
    • Wickström, S.A.1    Masoumi, K.C.2    Khochbin, S.3    Fässler, R.4    Massoumi, R.5
  • 60
    • 84976486955 scopus 로고    scopus 로고
    • CYLD - a deubiquitylase that acts to fine-tune microtubule properties and functions
    • Yang, Y., Zhou, J., CYLD - a deubiquitylase that acts to fine-tune microtubule properties and functions. J. Cell Sci. 129 (2016), 2289–2295.
    • (2016) J. Cell Sci. , vol.129 , pp. 2289-2295
    • Yang, Y.1    Zhou, J.2
  • 61
    • 84893848639 scopus 로고    scopus 로고
    • CYLD regulates spindle orientation by stabilizing astral microtubules and promoting dishevelled-NuMA-dynein/dynactin complex formation
    • Yang, Y., Liu, M., Li, D., Ran, J., Gao, J., Suo, S., Sun, S.C., Zhou, J., CYLD regulates spindle orientation by stabilizing astral microtubules and promoting dishevelled-NuMA-dynein/dynactin complex formation. Proc. Natl. Acad. Sci. USA 111 (2014), 2158–2163.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 2158-2163
    • Yang, Y.1    Liu, M.2    Li, D.3    Ran, J.4    Gao, J.5    Suo, S.6    Sun, S.C.7    Zhou, J.8


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