메뉴 건너뛰기




Volumn 21, Issue 13, 2010, Pages 2150-2160

P38 mitogen-activated protein kinase activity is required during mitosis for timely satisfaction of the mitotic checkpoint but not for the fidelity of chromosome segregation

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE P38; MOLECULAR MOTOR;

EID: 77954179458     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E10-02-0125     Document Type: Article
Times cited : (27)

References (52)
  • 3
    • 70450176266 scopus 로고    scopus 로고
    • Deviant kinetochore microtubule dynamics underlie chromosomal instability
    • Bakhoum, S. F., Genovese, G., and Compton, D. A. (2009). Deviant kinetochore microtubule dynamics underlie chromosomal instability. Curr. Biol. 19, 1937-1942.
    • (2009) Curr. Biol. , vol.19 , pp. 1937-1942
    • Bakhoum, S.F.1    Genovese, G.2    Compton, D.A.3
  • 4
    • 0032563807 scopus 로고    scopus 로고
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
    • Ben-Levy, R., Hooper, S., Wilson, R., Patterson, H. F., and Marshall, C. J. (1998). Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr. Biol. 8, 1049-1057.
    • (1998) Curr. Biol. , vol.8 , pp. 1049-1057
    • Ben-Levy, R.1    Hooper, S.2    Wilson, R.3    Patterson, H.F.4    Marshall, C.J.5
  • 5
    • 0036848491 scopus 로고    scopus 로고
    • The role of MAPK pathways in the action of chemotherapeutic drugs
    • Boldt, S., Weidle, U. H., and Kolch, W. (2002). The role of MAPK pathways in the action of chemotherapeutic drugs. Carcinogenesis 23, 1831-1838. (Pubitemid 35355933)
    • (2002) Carcinogenesis , vol.23 , Issue.11 , pp. 1831-1838
    • Boldt, S.1    Weidle, U.H.2    Kolch, W.3
  • 7
    • 0027531645 scopus 로고
    • An osmosensing signal transduction pathway in yeast
    • Brewster, J. L., de Valoir, T., Dwyer, N. D., Winter, E., and Gustin, M. C. (1993). An osmosensing signal transduction pathway in yeast. Science 259, 1760-1763. (Pubitemid 23114664)
    • (1993) Science , vol.259 , Issue.5102 , pp. 1760-1763
    • Brewster, J.L.1    De Valoir, T.2    Dwyer, N.D.3    Winter, E.4    Gustin, M.C.5
  • 8
    • 67749147567 scopus 로고    scopus 로고
    • The ability to survive mitosis in the presence of microtubule poisons differs significantly between human nontransformed (RPE-1) and cancer (U2OS, HeLa) cells
    • Brito, D., and Rieder, C. L. (2008). The ability to survive mitosis in the presence of microtubule poisons differs significantly between human nontransformed (RPE-1) and cancer (U2OS, HeLa) cells. Cell Motil. Cytoskelet. 66, 437-447.
    • (2008) Cell Motil. Cytoskelet. , vol.66 , pp. 437-447
    • Brito, D.1    Rieder, C.L.2
  • 12
    • 0037025073 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase during normal mitosis in the developing retina
    • Campos, C.B.L., Bedard, P. A., and Linden, R. (2002). Activation of p38 mitogen-activated protein kinase during normal mitosis in the developing retina. Neuroscience 112, 583-591.
    • (2002) Neuroscience , vol.112 , pp. 583-591
    • Campos, C.B.L.1    Bedard, P.A.2    Linden, R.3
  • 13
    • 34547942911 scopus 로고    scopus 로고
    • A functional role for p38 MAPK in modulating mitotic transit in the absence of stress
    • Cha, H., Wang, X., Li, H., and Fornace, A. J. (2007). A functional role for p38 MAPK in modulating mitotic transit in the absence of stress. J. Biol. Chem. 282, 22984-22992.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22984-22992
    • Cha, H.1    Wang, X.2    Li, H.3    Fornace, A.J.4
  • 15
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M., and Cohen, P. (2000). Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 16
    • 0038247837 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase mediates cell death and p21-activated kinase mediates cell survival during chemotherapeutic drug-induced mitotic arrest
    • Deacon, K., Mistry, P., Chernoff, J., Blank, J. L., and Patel, R. (2003). p38 mitogen-activated protein kinase mediates cell death and p21-activated kinase mediates cell survival during chemotherapeutic drug-induced mitotic arrest. Mol. Biol. Cell 14, 2071-2087.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2071-2087
    • Deacon, K.1    Mistry, P.2    Chernoff, J.3    Blank, J.L.4    Patel, R.5
  • 17
    • 0034677067 scopus 로고    scopus 로고
    • Activation of the p38 mitogen-activated protein kinase pathway arrests cell cycle progression and differentiation of immature thymocytes in vitro
    • Diehl, N. L., Enslen, H., Fortner, K. A., Merritt, C., Stetson, N., Charland, C., Flavell, R. A., Davis, R. J., and Rincon, M. (2000). Activation of the p38 mitogen-activated protein kinase pathway arrests cell cycle progression and differentiation of immature thymocytes in vitro. J. Exp. Med. 191, 321-334.
    • (2000) J. Exp. Med. , vol.191 , pp. 321-334
    • Diehl, N.L.1    Enslen, H.2    Fortner, K.A.3    Merritt, C.4    Stetson, N.5    Charland, C.6    Flavell, R.A.7    Davis, R.J.8    Rincon, M.9
  • 18
    • 67649834504 scopus 로고    scopus 로고
    • Compression regulates mitotic spindle length by a mechanochemical switch at the poles
    • Dumont, S., and Mitchison, T. J. (2009). Compression regulates mitotic spindle length by a mechanochemical switch at the poles. Curr. Biol. 19, 1086-1095.
    • (2009) Curr. Biol. , vol.19 , pp. 1086-1095
    • Dumont, S.1    Mitchison, T.J.2
  • 19
    • 0032961833 scopus 로고    scopus 로고
    • Cell cycle arrest and reversion of Ras-induced transformation by a conditionally activated form of mitogen-activated protein kinase kinase kinase 3
    • Ellinger-Ziegelbauer, H., Kelly, K., and Siebenlist, U. (1999). Cell cycle arrest and reversion of Ras-induced transformation by a conditionally activated form of mitogen-activated protein kinase kinase kinase 3. Mol. Biol. Cell 19, 3857-3868.
    • (1999) Mol. Biol. Cell , vol.19 , pp. 3857-3868
    • Ellinger-Ziegelbauer, H.1    Kelly, K.2    Siebenlist, U.3
  • 20
    • 34548436939 scopus 로고    scopus 로고
    • Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore microtubule interactions
    • Elowe, S., Hummer, S., Li, X., and Nigg, E. A. (2007). Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore microtubule interactions. Genes Dev. 21, 2205-2219.
    • (2007) Genes Dev. , vol.21 , pp. 2205-2219
    • Elowe, S.1    Hummer, S.2    Li, X.3    Nigg, E.A.4
  • 21
    • 33750298315 scopus 로고    scopus 로고
    • FGF1/p38 MAP kinase inhibitor therapy induces cardiomyocyte mitosis, reduces scarring, and rescues function after myocardial infarction
    • Engel, F. B., Hsieh, P.C.H., Lee, R. T., and Keating, M. T. (2006). FGF1/p38 MAP kinase inhibitor therapy induces cardiomyocyte mitosis, reduces scarring, and rescues function after myocardial infarction. Proc. Natl. Acad. Sci. USA 103, 15546-15551.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15546-15551
    • Engel, F.B.1    Hsieh, P.C.H.2    Lee, R.T.3    Keating, M.T.4
  • 22
    • 39049190957 scopus 로고    scopus 로고
    • A novel role of p38α MAPK in mitotic progression independent of its kinase activity
    • Fan, L., Yang, X., Du, J., Marshall, M., Blanchard, K., and Ye, X. (2005). A novel role of p38α MAPK in mitotic progression independent of its kinase activity. Cell Cycle 4, 1616-1624.
    • (2005) Cell Cycle , vol.4 , pp. 1616-1624
    • Fan, L.1    Yang, X.2    Du, J.3    Marshall, M.4    Blanchard, K.5    Ye, X.6
  • 23
    • 14044270858 scopus 로고    scopus 로고
    • Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38γ at Thr50 promotes microtubule assembly
    • Feijoo, C., Campbell, D. G., Jakes, R., Goedert, M., and Cuenda, A. (2005). Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38γ at Thr50 promotes microtubule assembly. J. Cell Sci. 118, 397-408.
    • (2005) J. Cell Sci. , vol.118 , pp. 397-408
    • Feijoo, C.1    Campbell, D.G.2    Jakes, R.3    Goedert, M.4    Cuenda, A.5
  • 24
    • 0029937532 scopus 로고    scopus 로고
    • Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells
    • Gabrielli, B. G., DeSouza, C. P., Tonks, I. D., Clark, J. M., Hayward, N. K., and Ellem, K. A. (1996). Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells. J. Cell Sci. 109, 1081-1093. (Pubitemid 26168260)
    • (1996) Journal of Cell Science , vol.109 , Issue.5 , pp. 1081-1093
    • Gabrielli, B.G.1    De Souza, C.P.C.2    Tonks, I.D.3    Clark, J.M.4    Hayward, N.K.5    Ellem, K.A.O.6
  • 26
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han, J., Lee, J.-D., Bibbs, L., and Ulevitch, R. J. (1994). A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265, 808-811. (Pubitemid 24266145)
    • (1994) Science , vol.265 , Issue.5173 , pp. 808-811
    • Man, J.1    Lee, J.-D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 27
  • 28
    • 0035153295 scopus 로고    scopus 로고
    • Microtubule dependent changes in the assembly of microtubule motor proteins and mitotic spindle checkpoint proteins at kinetochores
    • Hoffman, D. B., Pearson, C. G., Yen, T. J., Howell, B. J., and Salmon, E. D. (2001). Microtubule dependent changes in the assembly of microtubule motor proteins and mitotic spindle checkpoint proteins at kinetochores. Mol. Biol. Cell 12, 1995-2009.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1995-2009
    • Hoffman, D.B.1    Pearson, C.G.2    Yen, T.J.3    Howell, B.J.4    Salmon, E.D.5
  • 29
    • 73849139645 scopus 로고    scopus 로고
    • The p38/MAPK pathway regulates microtubule polymerization through phosphorylation of MAP4 and Op18 in hypoxic cells
    • Hu, J. Y., Chu, Z. G., Han, J., Dang, Y. M., Yan, H., Zhang, Q., Liang, G. P., and Huang, Y. S. (2010). The p38/MAPK pathway regulates microtubule polymerization through phosphorylation of MAP4 and Op18 in hypoxic cells. Cell Mol. Life Sci. 67, 321-333.
    • (2010) Cell Mol. Life Sci. , vol.67 , pp. 321-333
    • Hu, J.Y.1    Chu, Z.G.2    Han, J.3    Dang, Y.M.4    Yan, H.5    Zhang, Q.6    Liang, G.P.7    Huang, Y.S.8
  • 30
    • 0029982565 scopus 로고    scopus 로고
    • Characterization of the structure and function of a new mitogen- Activated protein kinase (p38β)
    • DOI 10.1074/jbc.271.30.17920
    • Jiang, Y., Chen, C., Li, Z., Guo, W., Gegner, J. A., Lin, S., and Han, J. (1996). Characterization of the structure and function of a new mitogen-activated protein kinase (p38β). J. Biol. Chem. 271, 17920-17926. (Pubitemid 26250772)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 17920-17926
    • Jiang, Y.1    Chen, C.2    Li, Z.3    Guo, W.4    Gegner, J.A.5    Lin, S.6    Han, J.7
  • 31
    • 29044441387 scopus 로고    scopus 로고
    • Imaging the division process in living tissue culture cells
    • Khodjakov, A., and Rieder, C. L. (2006). Imaging the division process in living tissue culture cells. Methods 38, 2-16.
    • (2006) Methods , vol.38 , pp. 2-16
    • Khodjakov, A.1    Rieder, C.L.2
  • 32
    • 72949095324 scopus 로고    scopus 로고
    • The nature of cell cycle checkpoints: Facts and fallacies
    • Khodjakov, A., and Rieder, C. L. (2009). The nature of cell cycle checkpoints: facts and fallacies. J. Biol. 8, 88.1- 88.5.
    • (2009) J. Biol. , vol.8
    • Khodjakov, A.1    Rieder, C.L.2
  • 33
    • 4444245218 scopus 로고    scopus 로고
    • Inactivation of the mitotic checkpoint as a determinant of the efficacy of microtubule-targeted drugs in killing human cancer cells
    • Lee, E. A., Keutmann, M. K., Dowling, M. L., Harris, E., Chan, G., and Kao, G. D. (2004). Inactivation of the mitotic checkpoint as a determinant of the efficacy of microtubule-targeted drugs in killing human cancer cells. Mol. Cancer Ther. 3, 661-669.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 661-669
    • Lee, E.A.1    Keutmann, M.K.2    Dowling, M.L.3    Harris, E.4    Chan, G.5    Kao, G.D.6
  • 34
    • 37249023811 scopus 로고    scopus 로고
    • Actin dysfunction activates ERK1/2 and delays entry into mitosis in mammalian cells
    • Lee, K., and Song, K. (2007). Actin dysfunction activates ERK1/2 and delays entry into mitosis in mammalian cells. Cell Cycle 6, 1487-1495.
    • (2007) Cell Cycle , vol.6 , pp. 1487-1495
    • Lee, K.1    Song, K.2
  • 35
    • 4143140977 scopus 로고    scopus 로고
    • Chfr acts with the p38 stress kinase to block entry to mitosis in mammalian cells
    • Matsusaka, T., and Pines, J. (2004). Chfr acts with the p38 stress kinase to block entry to mitosis in mammalian cells. J. Cell Biol. 166, 507-516.
    • (2004) J. Cell Biol. , vol.166 , pp. 507-516
    • Matsusaka, T.1    Pines, J.2
  • 36
    • 4143057046 scopus 로고    scopus 로고
    • Topoisomerase II and histone deacetylase inhibitors delay the G2/M transition by triggering the p38 MAPK pathway
    • Mikhailov, A., Shinohara, M., and Rieder, C. L. (2004). Topoisomerase II and histone deacetylase inhibitors delay the G2/M transition by triggering the p38 MAPK pathway. J. Cell Biol. 166, 517-526.
    • (2004) J. Cell Biol. , vol.166 , pp. 517-526
    • Mikhailov, A.1    Shinohara, M.2    Rieder, C.L.3
  • 37
    • 22844443157 scopus 로고    scopus 로고
    • The p38-mediated stress-activated checkpoint
    • Mikhailov, A., Shinohara, M., and Rieder, C. L. (2005). The p38-mediated stress-activated checkpoint. Cell Cycle 4, 57-62.
    • (2005) Cell Cycle , vol.4 , pp. 57-62
    • Mikhailov, A.1    Shinohara, M.2    Rieder, C.L.3
  • 39
    • 0029089795 scopus 로고
    • Pyp1 and Pyp2 PPTases dephosphorylate an osmosensing MAK kinase controlling cell size at division in fission yeast
    • Millar, J. B., Buck, V., and Wilkinson, M. G. (1995). Pyp1 and Pyp2 PPTases dephosphorylate an osmosensing MAK kinase controlling cell size at division in fission yeast. Genes Dev. 9, 2117-2130.
    • (1995) Genes Dev. , vol.9 , pp. 2117-2130
    • Millar, J.B.1    Buck, V.2    Wilkinson, M.G.3
  • 40
    • 0027413490 scopus 로고
    • Microtubule nucleating activity of centrosomes in cell free extracts from Xenopus eggs: Involvement of phosphorylation and accumulation of pericentriolar material
    • Ohta, K., Shina, N., Okumura, E., Hisanaga, S., Kishimoto, T., Endo, S., Gotoh, Y., Nishida, E., and Sakai, H. (1993). Microtubule nucleating activity of centrosomes in cell free extracts from Xenopus eggs: involvement of phosphorylation and accumulation of pericentriolar material. J. Cell Sci. 104, 125-137.
    • (1993) J. Cell Sci. , vol.104 , pp. 125-137
    • Ohta, K.1    Shina, N.2    Okumura, E.3    Hisanaga, S.4    Kishimoto, T.5    Endo, S.6    Gotoh, Y.7    Nishida, E.8    Sakai, H.9
  • 41
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Hans, J., Ulevitch, R. J., and Davis, R. J. (1995). Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270, 7420-7426.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Hans, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 43
    • 33845807361 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK
    • Ronkina, N., et al. (2007). The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK. Mol. Cell. Biol. 27, 170-181.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 170-181
    • Ronkina, N.1
  • 44
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse, J., Cohen, P., Trigon, S., Morange, M., Alonso-Llamazares, A., Zamanillo, D., Hunt, T., and Nebreda, A. R. (1994). A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78, 1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 45
    • 4444281927 scopus 로고    scopus 로고
    • Drosophila Klp67A is required for proper chromosome congression and segregation during meiosis 1
    • Savoian, M. S., Gatt, M. K., Riparbelli, M. G., Callaini, G., and Glover, D. M. (2004). Drosophila Klp67A is required for proper chromosome congression and segregation during meiosis 1. J. Cell Sci. 117, 3669-3677.
    • (2004) J. Cell Sci. , vol.117 , pp. 3669-3677
    • Savoian, M.S.1    Gatt, M.K.2    Riparbelli, M.G.3    Callaini, G.4    Glover, D.M.5
  • 46
    • 1942474378 scopus 로고    scopus 로고
    • Dependence of paclitaxel sensitivity on a functional spindle assembly checkpoint
    • Sudo, T., Nitta, M., Saya, H., and Ueno, N. T. (2004). Dependence of paclitaxel sensitivity on a functional spindle assembly checkpoint. Cancer Res. 64, 2502-2508.
    • (2004) Cancer Res. , vol.64 , pp. 2502-2508
    • Sudo, T.1    Nitta, M.2    Saya, H.3    Ueno, N.T.4
  • 47
    • 0032562716 scopus 로고    scopus 로고
    • Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest
    • Takenaka, K., Moriguchi, T., and Nishida, E. (1998). Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science 280, 599-602.
    • (1998) Science , vol.280 , pp. 599-602
    • Takenaka, K.1    Moriguchi, T.2    Nishida, E.3
  • 48
    • 56149111920 scopus 로고    scopus 로고
    • Phosphorylation of Plk1 at Ser326 regulates its functions during mitotic progression
    • Tang, J., Yang, X., and Liu, X. (2008). Phosphorylation of Plk1 at Ser326 regulates its functions during mitotic progression. Oncogene 27, 6635-6645.
    • (2008) Oncogene , vol.27 , pp. 6635-6645
    • Tang, J.1    Yang, X.2    Liu, X.3
  • 50
    • 27744493551 scopus 로고    scopus 로고
    • A novel role of p38α MAPK in mitotic progression independent of its kinase activity
    • Yang, X., Du, J., Marshall, M., Blanchard, K., and Ye, X. (2005). A novel role of p38α MAPK in mitotic progression independent of its kinase activity. Cell Cycle 4, e61-e69.
    • (2005) Cell Cycle , vol.4
    • Yang, X.1    Du, J.2    Marshall, M.3    Blanchard, K.4    Ye, X.5
  • 51
    • 69949182313 scopus 로고    scopus 로고
    • Cells satisfy the mitotic checkpoint in Taxol, and do so faster in concentrations that stabilize syntelic attachments
    • Yang, Z., Kenny, A. E., Brito, D. A., and Rieder, C. L. (2009). Cells satisfy the mitotic checkpoint in Taxol, and do so faster in concentrations that stabilize syntelic attachments. J. Cell Biol. 186, 675-684.
    • (2009) J. Cell Biol. , vol.186 , pp. 675-684
    • Yang, Z.1    Kenny, A.E.2    Brito, D.A.3    Rieder, C.L.4
  • 52
    • 77950800323 scopus 로고    scopus 로고
    • Cdc20 proteolysis requires p38 MAPK signaling and Cdh1-independent APC/C ubiquitination during spindle assembly checkpoint activation by cadmium
    • Yen, A. H., and Yang, J. L. (2010). Cdc20 proteolysis requires p38 MAPK signaling and Cdh1-independent APC/C ubiquitination during spindle assembly checkpoint activation by cadmium. J. Cell Physiol. 223, 327-334.
    • (2010) J. Cell Physiol. , vol.223 , pp. 327-334
    • Yen, A.H.1    Yang, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.