메뉴 건너뛰기




Volumn 289, Issue 5, 2014, Pages 3080-3093

Polo-like kinase 2, a novel ADAM17 signaling component, regulates tumor necrosis factor α ectodomain shedding

Author keywords

[No Author keywords available]

Indexed keywords

ADAM ADAMTS; ADAM17; METALLOPROTEASE; PHOSPHORYLATION; PLK2; SHEDDING; TUMOR NECROSIS FACTOR (TNF);

EID: 84893474483     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.536847     Document Type: Article
Times cited : (39)

References (64)
  • 2
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs. Key components in EGFR signalling and development
    • Blobel, C. P. (2005) ADAMs. Key components in EGFR signalling and development. Nat Rev. Mol. Cell Biol. 6, 32-43
    • (2005) Nat Rev. Mol. Cell Biol. , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 3
    • 79955470772 scopus 로고    scopus 로고
    • The "a disintegrin and metalloproteases" ADAM10 and ADAM17. Novel drug targets with therapeutic potential?
    • Saftig, P., and Reiss, K. (2011) The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17. Novel drug targets with therapeutic potential? Eur. J. Cell Biol. 90, 527-535
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 527-535
    • Saftig, P.1    Reiss, K.2
  • 6
    • 77949558495 scopus 로고    scopus 로고
    • ADAM-17. The enzyme that does it all
    • Gooz, M. (2010) ADAM-17. The enzyme that does it all. Crit. Rev. Biochem. Mol. Biol. 45, 146-169
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 146-169
    • Gooz, M.1
  • 7
    • 79960923986 scopus 로고    scopus 로고
    • ADAM17. A molecular switch to control inflammation and tissue regeneration
    • Scheller, J., Chalaris, A., Garbers, C, and Rose-John, S. (2011) ADAM17. A molecular switch to control inflammation and tissue regeneration. Trends Immunol. 32, 380-387
    • (2011) Trends Immunol. , vol.32 , pp. 380-387
    • Scheller, J.1    Chalaris, A.2    Garbers, C.3    Rose-John, S.4
  • 9
    • 38449086094 scopus 로고    scopus 로고
    • Cutting edge. TNF-α-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock
    • Horiuchi, K., Kimura, T., Miyamoto, T., Takaishi, H., Okada, Y., Toyama, Y., and Blobel, C. P. (2007) Cutting edge. TNF-α-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock. J. Immunol. 179, 2686-2689
    • (2007) J. Immunol. , vol.179 , pp. 2686-2689
    • Horiuchi, K.1    Kimura, T.2    Miyamoto, T.3    Takaishi, H.4    Okada, Y.5    Toyama, Y.6    Blobel, C.P.7
  • 10
    • 77953989617 scopus 로고    scopus 로고
    • In vivo role of leukocyte ADAM17 in the inflammatory and host responses during E. Coli-mediated peritonitis
    • Long, C, Wang, Y., Herrera, A. H., Horiuchi, K., and Walcheck, B. (2010) In vivo role of leukocyte ADAM17 in the inflammatory and host responses during E. coli-mediated peritonitis. J. Leukocyte Biol. 87, 1097-1101
    • (2010) J. Leukocyte Biol. , vol.87 , pp. 1097-1101
    • Long, C.1    Wang, Y.2    Herrera, A.H.3    Horiuchi, K.4    Walcheck, B.5
  • 11
  • 13
    • 21044444181 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of Thr735 in TNFa-converting enzyme and its potential role in TACE protein trafficking
    • Soond, S. M., Everson, B., Riches, D. W., and Murphy, G. (2005) ERK-mediated phosphorylation of Thr735 in TNFa-converting enzyme and its potential role in TACE protein trafficking. J. Cell Sci. 118, 2371-2380
    • (2005) J. Cell Sci. , vol.118 , pp. 2371-2380
    • Soond, S.M.1    Everson, B.2    Riches, D.W.3    Murphy, G.4
  • 14
    • 84860714018 scopus 로고    scopus 로고
    • TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association
    • Xu, P., Liu, J., Sakaki-Yumoto, M., and Derynck, R. (2012) TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association. Sci. Signal. 5, ra34
    • (2012) Sci. Signal. , vol.5
    • Xu, P.1    Liu, J.2    Sakaki-Yumoto, M.3    Derynck, R.4
  • 16
    • 34548856204 scopus 로고    scopus 로고
    • Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory transsignaling function of neutrophils
    • Chalaris, A., Rabe, B., Paliga, K., Lange, H, Laskay, T., Fielding, C. A., Jones, S. A., Rose-John, S., and Scheller, J. (2007) Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory transsignaling function of neutrophils. Blood 110, 1748-1755
    • (2007) Blood , vol.110 , pp. 1748-1755
    • Chalaris, A.1    Rabe, B.2    Paliga, K.3    Lange, H.4    Laskay, T.5    Fielding, C.A.6    Jones, S.A.7    Rose-John, S.8    Scheller, J.9
  • 17
    • 84867818285 scopus 로고    scopus 로고
    • A role for cGMP in inducible nitric-oxide synthase (iNOS) - Induced tumor necrosis factor (TNF) a-converting enzyme (TACE/ADAM17) activation, translocation, and TNF receptor 1 (TNFR1) shedding in hepatocytes
    • Chanthaphavong, R. S., Loughran, P. A., Lee, T. Y., Scott, M. J., and Billiar, T. R. (2012) A role for cGMP in inducible nitric-oxide synthase (iNOS) - induced tumor necrosis factor (TNF) a-converting enzyme (TACE/ADAM17) activation, translocation, and TNF receptor 1 (TNFR1) shedding in hepatocytes. J. Biol. Chem. 287, 35887-35898
    • (2012) J. Biol. Chem. , vol.287 , pp. 35887-35898
    • Chanthaphavong, R.S.1    Loughran, P.A.2    Lee, T.Y.3    Scott, M.J.4    Billiar, T.R.5
  • 19
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor a-converting enzyme at threonine 735. A potential role in regulated shedding
    • Díaz-Rodríguez, E., Montero, J. C, Esparís-Ogando, A., Yuste, L., and Pandiella, A. (2002) Extracellular signal-regulated kinase phosphorylates tumor necrosis factor a-converting enzyme at threonine 735. A potential role in regulated shedding. Mol. Biol. Cell 13, 2031-2044
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2031-2044
    • Díaz-Rodríguez, E.1    Montero, J.C.2    Esparís-Ogando, A.3    Yuste, L.4    Pandiella, A.5
  • 20
    • 76849107016 scopus 로고    scopus 로고
    • Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation
    • Xu, P., and Derynck, R. (2010) Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation. Mol. Cell 37, 551-566
    • (2010) Mol. Cell , vol.37 , pp. 551-566
    • Xu, P.1    Derynck, R.2
  • 21
    • 79551629449 scopus 로고    scopus 로고
    • A transforming Src mutant increases the bioavailability of EGFR ligands via stimulation of the cell-surface metalloproteinase ADAM17
    • Maretzky, T., Zhou, W., Huang, X. Y., and Blobel, C. P. (2011) A transforming Src mutant increases the bioavailability of EGFR ligands via stimulation of the cell-surface metalloproteinase ADAM17. Oncogene 30, 611-618
    • (2011) Oncogene , vol.30 , pp. 611-618
    • Maretzky, T.1    Zhou, W.2    Huang, X.Y.3    Blobel, C.P.4
  • 24
    • 0027178446 scopus 로고
    • Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila
    • Clay, F. J., McEwen, S. J., Bertoncello, I., Wilks, A. F., and Dunn, A. R. (1993) Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila. Proc. Natl. Acad. Sci. U. S. A. 90, 4882-4886
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 4882-4886
    • Clay, F.J.1    McEwen, S.J.2    Bertoncello, I.3    Wilks, A.F.4    Dunn, A.R.5
  • 25
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • Sunkel, C. E., and Glover, D. M. (1988) polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J. Cell Sci. 89, 25-38
    • (1988) J. Cell Sci. , vol.89 , pp. 25-38
    • Sunkel, C.E.1    Glover, D.M.2
  • 26
    • 0242556820 scopus 로고    scopus 로고
    • The crystal structure of the human Polo-like kinase-1 Polo box domain and its phospho-peptide complex
    • Cheng, K. Y., Lowe, E. D., Sinclair, J., Nigg, E. A., and Johnson, L. N (2003) The crystal structure of the human Polo-like kinase-1 Polo box domain and its phospho-peptide complex. EMBOJ. 22, 5757-5768
    • (2003) EMBOJ , vol.22 , pp. 5757-5768
    • Cheng, K.Y.1    Lowe, E.D.2    Sinclair, J.3    Nigg, E.A.4    Johnson, L.N.5
  • 27
    • 33847680936 scopus 로고    scopus 로고
    • Molecular and structural basis of Polo-like kinase 1 substrate recognition. Implications in centrosomal localization
    • García-Alvarez, B., De Cárcer, G., Ibañez, S., Bragado-Nilsson, E., and Montoya, G. (2007) Molecular and structural basis of Polo-like kinase 1 substrate recognition. Implications in centrosomal localization. Proc. Natl. Acad. Sci. U. S. A. 104, 3107-3112
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 3107-3112
    • García-Alvarez, B.1    De Cárcer, G.2    Ibañez, S.3    Bragado-Nilsson, E.4    Montoya, G.5
  • 30
    • 77957279696 scopus 로고    scopus 로고
    • Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic overexcitation
    • Evers, D. M., Matta, J. A., Hoe, H. S., Zarkowsky, D., Lee, S. H, Isaac, J. T., and Pak, D. T. (2010) Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic overexcitation. Nat. Neurosci. 13, 1199-1207
    • (2010) Nat. Neurosci. , vol.13 , pp. 1199-1207
    • Evers, D.M.1    Matta, J.A.2    Hoe, H.S.3    Zarkowsky, D.4    Lee, S.H.5    Isaac, J.T.6    Pak, D.T.7
  • 31
    • 2942615282 scopus 로고    scopus 로고
    • Polo-like kinases and the orchestration of cell division
    • Barr, F. A., Silljé, H. H., and Nigg, E. A. (2004) Polo-like kinases and the orchestration of cell division. Nat. Rev. Mol. Cell Biol. 5, 429-440
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 429-440
    • Barr, F.A.1    Silljé, H.H.2    Nigg, E.A.3
  • 32
    • 43049151493 scopus 로고    scopus 로고
    • Polo on the rise. From mitotic entry to cytokinesis with Plk1
    • Petronczki, M., Lénárt, P., and Peters, J. M. (2008) Polo on the rise. From mitotic entry to cytokinesis with Plk1. Dev. Cell 14, 646-659
    • (2008) Dev. Cell , vol.14 , pp. 646-659
    • Petronczki, M.1    Lénárt, P.2    Peters, J.M.3
  • 34
    • 0042132030 scopus 로고    scopus 로고
    • Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells
    • Burns, T. F., Fei, P., Scata, K. A., Dicker, D. T., and El-Deiry, W. S. (2003) Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells. Mol. Cell Biol. 23, 5556-5571
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5556-5571
    • Burns, T.F.1    Fei, P.2    Scata, K.A.3    Dicker, D.T.4    El-Deiry, W.S.5
  • 36
    • 84876110045 scopus 로고    scopus 로고
    • ADAM17, shedding, TACE as therapeutic targets
    • Rose-John, S. (2013) ADAM17, shedding, TACE as therapeutic targets. Pharmacol. Res. 71 C, 19-22
    • (2013) Pharmacol. Res. , vol.71 C , pp. 19-22
    • Rose-John, S.1
  • 37
    • 77955106518 scopus 로고    scopus 로고
    • Forced homo- and heterodimerization of all gp130-type receptor complexes leads to constitutive ligand-independent signaling and cytokine-independent growth
    • Suthaus, J., Tillmann, A., Lorenzen, I., Bulanova, E., Rose-John, S., and Scheller, J. (2010) Forced homo- and heterodimerization of all gp130-type receptor complexes leads to constitutive ligand-independent signaling and cytokine-independent growth. Mol. Biol. Cell 21, 2797-2807
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2797-2807
    • Suthaus, J.1    Tillmann, A.2    Lorenzen, I.3    Bulanova, E.4    Rose-John, S.5    Scheller, J.6
  • 38
    • 0026481133 scopus 로고
    • Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor
    • Inaba, K., Inaba, M., Romani, N., Aya, H., Deguchi, M., Ikehara, S., Muramatsu, S., and Steinman, R. M. (1992) Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor. J. Exp. Med. 176, 1693-1702
    • (1992) J. Exp. Med. , vol.176 , pp. 1693-1702
    • Inaba, K.1    Inaba, M.2    Romani, N.3    Aya, H.4    Deguchi, M.5    Ikehara, S.6    Muramatsu, S.7    Steinman, R.M.8
  • 39
    • 80053266748 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases p38 and ERK1/2 regulated control of Mycobacterium avium replication in primary murine macrophages is independent of tumor necrosis factor-A and interleukin-10
    • Klug, K., Ehlers, S., Uhlig, S., and Reiling, N. (2011) Mitogen-activated protein kinases p38 and ERK1/2 regulated control of Mycobacterium avium replication in primary murine macrophages is independent of tumor necrosis factor-a and interleukin-10. Innate Immun. 17, 470-485
    • (2011) Innate Immun. , vol.17 , pp. 470-485
    • Klug, K.1    Ehlers, S.2    Uhlig, S.3    Reiling, N.4
  • 41
    • 84859896499 scopus 로고    scopus 로고
    • The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II
    • Lorenzen, I., Lokau, J., Düsterhöft, S., Trad, A., Garbers, C., Scheller, J., Rose-John, S., and Grötzinger, J. (2012) The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II. FEBSLett. 586, 1093-1100
    • (2012) FEBSLett. , vol.586 , pp. 1093-1100
    • Lorenzen, I.1    Lokau, J.2    Düsterhöft, S.3    Trad, A.4    Garbers, C.5    Scheller, J.6    Rose-John, S.7    Grötzinger, J.8
  • 42
    • 84855863627 scopus 로고    scopus 로고
    • Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain
    • Lorenzen, I., Trad, A., and Grötzinger, J. (2011) Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain. Biochem. Biophys. Res. Commun. 415, 330-336
    • (2011) Biochem. Biophys. Res. Commun. , vol.415 , pp. 330-336
    • Lorenzen, I.1    Trad, A.2    Grötzinger, J.3
  • 43
    • 43649097642 scopus 로고    scopus 로고
    • Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity
    • Seeburg, D. P., Feliu-Mojer, M., Gaiottino, J., Pak, D. T., and Sheng, M. (2008) Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity. Neuron 58, 571-583
    • (2008) Neuron , vol.58 , pp. 571-583
    • Seeburg, D.P.1    Feliu-Mojer, M.2    Gaiottino, J.3    Pak, D.T.4    Sheng, M.5
  • 44
    • 0242515843 scopus 로고    scopus 로고
    • Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates
    • Elia, A. E., Cantley, L. C, and Yaffe, M. B. (2003) Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 299, 1228-1231
    • (2003) Science , vol.299 , pp. 1228-1231
    • Elia, A.E.1    Cantley, L.C.2    Yaffe, M.B.3
  • 45
    • 18844374886 scopus 로고    scopus 로고
    • Chaperone-like properties of the prodomain of TNFa-converting enzyme (TACE) and the functional role of its cysteine switch
    • Leonard, J. D., Lin, F., and Milla, M. E. (2005) Chaperone-like properties of the prodomain of TNFa-converting enzyme (TACE) and the functional role of its cysteine switch. Biochem. J. 387, 797-805
    • (2005) Biochem. J. , vol.387 , pp. 797-805
    • Leonard, J.D.1    Lin, F.2    Milla, M.E.3
  • 46
    • 79952237532 scopus 로고    scopus 로고
    • Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory
    • Lee, K. J., Lee, Y., Rozeboom, A., Lee, J. Y., Udagawa, N., Hoe, H. S., and Pak, D. T. (2011) Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory. Neuron 69, 957-973
    • (2011) Neuron , vol.69 , pp. 957-973
    • Lee, K.J.1    Lee, Y.2    Rozeboom, A.3    Lee, J.Y.4    Udagawa, N.5    Hoe, H.S.6    Pak, D.T.7
  • 47
    • 77955167321 scopus 로고    scopus 로고
    • Multifaceted Polo-like kinases. Drug targets and antitargets for cancer therapy
    • Strebhardt, K. (2010) Multifaceted Polo-like kinases. Drug targets and antitargets for cancer therapy. Nat. Rev. Drug Discov. 9, 643-660
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 643-660
    • Strebhardt, K.1
  • 50
    • 62849123093 scopus 로고    scopus 로고
    • Polo-like kinases. Conservation and divergence in their functions and regulation
    • Archambault, V., and Glover, D. M. (2009) Polo-like kinases. Conservation and divergence in their functions and regulation. Nat. Rev. Mol. Cell Biol. 10, 265-275
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 265-275
    • Archambault, V.1    Glover, D.M.2
  • 51
    • 47249153519 scopus 로고    scopus 로고
    • Role of cytokines in rheumatoid arthritis. An education in pathophysiology and therapeutics
    • Feldmann, M., and Maini, S. R. (2008) Role of cytokines in rheumatoid arthritis. An education in pathophysiology and therapeutics. Immunol. Rev. 223, 7-19
    • (2008) Immunol. Rev. , vol.223 , pp. 7-19
    • Feldmann, M.1    Maini, S.R.2
  • 53
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K., and Tschopp, J. (2010) The inflammasomes. Cell 140, 821-832
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 54
    • 0141781074 scopus 로고    scopus 로고
    • Role of Plk2 (Snk) in mouse development and cell proliferation
    • Ma, S., Charron, J., and Erikson, R. L. (2003) Role of Plk2 (Snk) in mouse development and cell proliferation. Mol. Cell Biol. 23, 6936-6943
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6936-6943
    • Ma, S.1    Charron, J.2    Erikson, R.L.3
  • 56
    • 80053927932 scopus 로고    scopus 로고
    • Reactive oxygen species and p38 mitogen-activated protein kinase mediate tumor necrosis factor a-converting enzyme (TACE/ADAM-17) activation in primary human monocytes
    • Scott, A. J., O'Dea, K. P., O'Callaghan, D., Williams, L., Dokpesi, J. O., Tatton, L., Handy, J. M., Hogg, P. J., and Takata, M. (2011) Reactive oxygen species and p38 mitogen-activated protein kinase mediate tumor necrosis factor a-converting enzyme (TACE/ADAM-17) activation in primary human monocytes. J. Biol. Chem. 286, 35466-35476
    • (2011) J. Biol. Chem. , vol.286 , pp. 35466-35476
    • Scott, A.J.1    O'Dea, K.P.2    O'Callaghan, D.3    Williams, L.4    Dokpesi, J.O.5    Tatton, L.6    Handy, J.M.7    Hogg, P.J.8    Takata, M.9
  • 60
    • 0032482986 scopus 로고    scopus 로고
    • Mutation of the Polo-box disrupts localization and mitotic functions of the mammalian Polo kinase Plk
    • Lee, K. S., Grenfell, T. Z., Yarm, F. R., and Erikson, R. L. (1998) Mutation of the Polo-box disrupts localization and mitotic functions of the mammalian Polo kinase Plk. Proc. Natl. Acad. Sci. U. S. A. 95, 9301-9306
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9301-9306
    • Lee, K.S.1    Grenfell, T.Z.2    Yarm, F.R.3    Erikson, R.L.4
  • 61
    • 84857597018 scopus 로고    scopus 로고
    • Interleukin-1 stimulates ADAM17 through a mechanism independent of its cytoplasmic domain or phosphorylation at threonine 735
    • Hall, K. C, and Blobel, C. P. (2012) Interleukin-1 stimulates ADAM17 through a mechanism independent of its cytoplasmic domain or phosphorylation at threonine 735. PLoS One 7, e31600
    • (2012) PLoS One , vol.7
    • Hall, K.C.1    Blobel, C.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.