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Volumn 289, Issue 17, 2014, Pages 11816-11828

Reactive oxygen species, amp-Activated protein kinase, and the transcription cofactor p300 regulate α-Tubulin acetyltransferase-1 (αtat-1/mec-17)-Dependent microtubule hyperacetylation during cell stress

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION;

EID: 84899444482     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.507400     Document Type: Article
Times cited : (75)

References (53)
  • 1
    • 77955965172 scopus 로고    scopus 로고
    • Cellular stress responses: Cell survival and cell death
    • 2010
    • Fulda, S., Gorman, A. M., Hori, O., and Samali, A. (2010) Cellular stress responses: cell survival and cell death. Int. J. Cell Biol. 2010, 214074
    • (2010) Int. J. Cell Biol. , pp. 214074
    • Fulda, S.1    Gorman, A.M.2    Hori, O.3    Samali, A.4
  • 2
    • 78649344442 scopus 로고    scopus 로고
    • Cellular stress responses: A balancing act
    • Chen, F., Evans, A., Pham, J., and Plosky, B. (2010) Cellular stress responses: a balancing act. Mol. Cell 40, 175
    • (2010) Mol. Cell , vol.40 , pp. 175
    • Chen, F.1    Evans, A.2    Pham, J.3    Plosky, B.4
  • 3
    • 75749155892 scopus 로고    scopus 로고
    • From signaling pathways to microtubule dynamics: The key players
    • Etienne-Manneville, S. (2010) From signaling pathways to microtubule dynamics: the key players. Curr. Opin. Cell Biol. 22, 104-111
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 104-111
    • Etienne-Manneville, S.1
  • 5
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T., and Kirschner, M. (1984) Dynamic instability of microtubule growth. Nature 312, 237-242
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 8
    • 84862658847 scopus 로고    scopus 로고
    • Posttranslational acetylation of α-Tubulin constrains protofilament number in native microtubules
    • Cueva, J. G., Hsin, J., Huang, K. C., and Goodman, M. B. (2012) Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules. Curr. Biol. 22, 1066-1074
    • (2012) Curr. Biol. , vol.22 , pp. 1066-1074
    • Cueva, J.G.1    Hsin, J.2    Huang, K.C.3    Goodman, M.B.4
  • 10
    • 84868146124 scopus 로고    scopus 로고
    • Luminal localization of α-Tubulin K40 acetylation by cryo-EM analysis of fablabeled microtubules
    • Soppina, V., Herbstman, J. F., Skiniotis, G., and Verhey, K. J. (2012) Luminal localization of α-tubulin K40 acetylation by cryo-EM analysis of fablabeled microtubules. PLoS One 7, e48204
    • (2012) PLoS One , vol.7
    • Soppina, V.1    Herbstman, J.F.2    Skiniotis, G.3    Verhey, K.J.4
  • 11
    • 84864746082 scopus 로고    scopus 로고
    • Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro
    • Walter, W. J., Beránek, V., Fischermeier, E., and Diez, S. (2012) Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. PLoS One 7, e42218
    • (2012) PLoS One , vol.7
    • Walter, W.J.1    Beránek, V.2    Fischermeier, E.3    Diez, S.4
  • 13
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelières, F. P., King, S. J., Humbert, S., and Saudou, F. (2007) Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelières, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 14
    • 76649143069 scopus 로고    scopus 로고
    • Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons
    • Hammond, J. W., Huang, C. F., Kaech, S., Jacobson, C., Banker, G., and Verhey, K. J. (2010) Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons. Mol. Biol. Cell 21, 572-583
    • (2010) Mol. Biol. Cell , vol.21 , pp. 572-583
    • Hammond, J.W.1    Huang, C.F.2    Kaech, S.3    Jacobson, C.4    Banker, G.5    Verhey, K.J.6
  • 15
    • 70350501513 scopus 로고    scopus 로고
    • Single molecule imaging reveals differences in microtubule track selection between kinesin motors
    • Cai, D., McEwen, D. P., Martens, J. R., Meyhofer, E., and Verhey, K. J. (2009) Single molecule imaging reveals differences in microtubule track selection between kinesin motors. PLoS Biol. 7, e1000216
    • (2009) PLoS Biol. , vol.7
    • Cai, D.1    McEwen, D.P.2    Martens, J.R.3    Meyhofer, E.4    Verhey, K.J.5
  • 16
    • 70449724841 scopus 로고    scopus 로고
    • Basal endothelial nicric oxide synthase (eNOS) phosphorylation on ser 1177 occurs in a stable microtubule- and tubulin acetylation-Dependent manner
    • Giustiniani, J., Couloubaly, S., Baillet, A., Pourci, M. L., Cantaloube, I., Fourniat, C., Paul, J. L., and Poüs, C. (2009) Basal endothelial nicric oxide synthase (eNOS) phosphorylation on Ser 1177 occurs in a stable microtubule- and tubulin acetylation-dependent manner. Exp. Cell Res. 315, 3509-3520
    • (2009) Exp. Cell Res. , vol.315 , pp. 3509-3520
    • Giustiniani, J.1    Couloubaly, S.2    Baillet, A.3    Pourci, M.L.4    Cantaloube, I.5    Fourniat, C.6    Paul, J.L.7    Poüs, C.8
  • 19
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: More than just a post-Translational modification?
    • Perdiz, D., Mackeh, R., Poüs, C., and Baillet, A. (2011) The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell. Signal. 23, 763-771
    • (2011) Cell. Signal. , vol.23 , pp. 763-771
    • Perdiz, D.1    Mackeh, R.2    Poüs, C.3    Baillet, A.4
  • 21
    • 78650731392 scopus 로고    scopus 로고
    • The major α-Tubulin K40 acetyltransferase αtAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B., and Nachury, M. V. (2010) The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. U.S.A. 107, 21517-21522
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 22
    • 0024094432 scopus 로고
    • Dynamic instability of individualmicrotubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker, R. A., O'Brien, E. T., Pryer, N. K., Soboeiro, M. F., Voter, W. A., Erickson, H. P., and Salmon, E. D. (1988) Dynamic instability of individualmicrotubules analyzed by video light microscopy: rate constants and transition frequencies. J. Cell Biol. 107, 1437-1448
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Soboeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6    Salmon, E.D.7
  • 23
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., and Elazar, Z. (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 26, 1749-1760
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 24
    • 24944450290 scopus 로고    scopus 로고
    • Superiority of combination of thiazide with angiotensin-Converting enzyme inhibitor or AT1-Receptor blocker over thiazide alone on renoprotection in L-NAME/SHR
    • Zhou, X., Matavelli, L. C., Ono, H., and Frohlich, E. D. (2005) Superiority of combination of thiazide with angiotensin-converting enzyme inhibitor or AT1-receptor blocker over thiazide alone on renoprotection in L-NAME/SHR. Am. J. Physiol. Renal. Physiol. 289, F871-F879
    • (2005) Am. J. Physiol. Renal. Physiol. , vol.289
    • Zhou, X.1    Matavelli, L.C.2    Ono, H.3    Frohlich, E.D.4
  • 26
    • 0035895888 scopus 로고    scopus 로고
    • Selective targeting of a redox-active ubiquinone to mitochondria within cells: Antioxidant and antiapoptotic properties
    • Kelso, G. F. (2001) Selective targeting of a redox-active ubiquinone to mitochondria within cells: antioxidant and antiapoptotic properties. J. Biol. Chem. 276, 4588-4596
    • (2001) J. Biol. Chem. , vol.276 , pp. 4588-4596
    • Kelso, G.F.1
  • 28
    • 84855182851 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) controls the aging process via an integrated signaling network
    • Salminen, A., and Kaarniranta, K. (2012) AMP-activated protein kinase (AMPK) controls the aging process via an integrated signaling network. Ageing Res. Rev. 11, 230-241
    • (2012) Ageing Res. Rev. , vol.11 , pp. 230-241
    • Salminen, A.1    Kaarniranta, K.2
  • 29
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • Codogno, P., and Meijer, A. J. (2005) Autophagy and signaling: their role in cell survival and cell death. Cell Death Differ. 12, 1509-1518
    • (2005) Cell Death Differ. , vol.12 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 31
    • 38349195601 scopus 로고    scopus 로고
    • HDAC6 a new cellular stress surveillance factor
    • Matthias, P., Yoshida, M., and Khochbin, S. (2008) HDAC6 a new cellular stress surveillance factor. Cell Cycle 7, 7-10
    • (2008) Cell Cycle , vol.7 , pp. 7-10
    • Matthias, P.1    Yoshida, M.2    Khochbin, S.3
  • 32
    • 0026002792 scopus 로고
    • Analysis with specific polyclonal antiserum indicates that the E1A-Associated 300-KDa product is a stable nuclear phosphoprotein that undergoes cell cycle phase-Specific modification
    • Yaciuk, P., and Moran, E. (1991) Analysis with specific polyclonal antiserum indicates that the E1A-associated 300-kDa product is a stable nuclear phosphoprotein that undergoes cell cycle phase-specific modification. Mol. Cell. Biol. 11, 5389-5397
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5389-5397
    • Yaciuk, P.1    Moran, E.2
  • 39
    • 0025095542 scopus 로고
    • Transition metals as catalysts of " autoxidation" reactions
    • Miller, D. M., Buettner, G. R., and Aust, S. D. (1990) Transition metals as catalysts of " autoxidation" reactions. Free Radic. Biol. Med. 8, 95-108
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 95-108
    • Miller, D.M.1    Buettner, G.R.2    Aust, S.D.3
  • 40
    • 29344446328 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria: A new therapeutic direction
    • Sheu, S. S., Nauduri, D., and Anders, M. W. (2006) Targeting antioxidants to mitochondria: a new therapeutic direction. Biochim. Biophys. Acta 1762, 256-265
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 256-265
    • Sheu, S.S.1    Nauduri, D.2    Anders, M.W.3
  • 41
    • 35648982347 scopus 로고    scopus 로고
    • Cellular response to hyperosmotic stresses
    • Burg, M. B., Ferraris, J. D., and Dmitrieva, N. I. (2007) Cellular response to hyperosmotic stresses. Physiol. Rev. 87, 1441-1474
    • (2007) Physiol. Rev. , vol.87 , pp. 1441-1474
    • Burg, M.B.1    Ferraris, J.D.2    Dmitrieva, N.I.3
  • 43
    • 84862849835 scopus 로고    scopus 로고
    • Redox implications of AMPK-Mediated signal transduction beyond energetic clues
    • Cardaci, S., Filomeni, G., and Ciriolo, M. R. (2012) Redox implications of AMPK-mediated signal transduction beyond energetic clues. J. Cell Sci. 125, 2115-2125
    • (2012) J. Cell Sci. , vol.125 , pp. 2115-2125
    • Cardaci, S.1    Filomeni, G.2    Ciriolo, M.R.3
  • 44
    • 33947602679 scopus 로고    scopus 로고
    • Differential modulation of AMPK signaling pathways by low or high levels of exogenous reactive oxygen species in colon cancer cells
    • Park, I. J., Hwang, J. T., Kim, Y. M., Ha, J., and Park, O. J. (2006) Differential modulation of AMPK signaling pathways by low or high levels of exogenous reactive oxygen species in colon cancer cells. Ann. N.Y. Acad. Sci. 1091, 102-109
    • (2006) Ann. N.Y. Acad. Sci. , vol.1091 , pp. 102-109
    • Park, I.J.1    Hwang, J.T.2    Kim, Y.M.3    Ha, J.4    Park, O.J.5
  • 45
    • 84867602835 scopus 로고    scopus 로고
    • Starvation-Induced autophagy is regulated by mitochondrial reactive oxygen species leading to AMPK activation
    • Li, L., Chen, Y., and Gibson, S. B. (2013) Starvation-induced autophagy is regulated by mitochondrial reactive oxygen species leading to AMPK activation. Cell. Signal. 25, 50-65
    • (2013) Cell. Signal. , vol.25 , pp. 50-65
    • Li, L.1    Chen, Y.2    Gibson, S.B.3
  • 46
    • 84884905298 scopus 로고    scopus 로고
    • Role of AMPK activation in oxidative cell damage: Implications for alcohol-Induced liver disease
    • Sid, B., Verrax, J., and Calderon, P. B. (2013) Role of AMPK activation in oxidative cell damage: implications for alcohol-induced liver disease. Biochem. Pharmacol. 86, 200-209
    • (2013) Biochem. Pharmacol. , vol.86 , pp. 200-209
    • Sid, B.1    Verrax, J.2    Calderon, P.B.3
  • 47
    • 84892547110 scopus 로고    scopus 로고
    • Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
    • Howes, S. C., Alushin, G. M., Shida, T., Nachury, M. V., and Nogales, E. (2014) Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. Mol. Biol. Cell 25, 257-266
    • (2014) Mol. Biol. Cell , vol.25 , pp. 257-266
    • Howes, S.C.1    Alushin, G.M.2    Shida, T.3    Nachury, M.V.4    Nogales, E.5
  • 49
    • 77957681100 scopus 로고    scopus 로고
    • ROS-Mediated mechanisms of autophagy stimulation and their relevance in cancer therapy
    • Dewaele, M., Maes, H., and Agostinis, P. (2010) ROS-mediated mechanisms of autophagy stimulation and their relevance in cancer therapy. Autophagy 6, 838-854
    • (2010) Autophagy , vol.6 , pp. 838-854
    • Dewaele, M.1    Maes, H.2    Agostinis, P.3
  • 50
    • 84877909895 scopus 로고    scopus 로고
    • Autophagy and microtubules: New story, old players
    • Mackeh, R., Perdiz, D., Lorin, S., Codogno, P., and Poüs, C. (2013) Autophagy and microtubules: new story, old players. J. Cell Sci. 126, 1071-1080
    • (2013) J. Cell Sci. , vol.126 , pp. 1071-1080
    • Mackeh, R.1    Perdiz, D.2    Lorin, S.3    Codogno, P.4    Poüs, C.5
  • 52
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αTAT1 Tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G., and Downing, K. H. (1998) Structure of the αTAT1 tubulin dimer by electron crystallography. Nature 391, 199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 53
    • 84870342617 scopus 로고    scopus 로고
    • Structure of the α-tubulin acetyltransferase, αtAT1, and implications for tubulin-Specific acetylation
    • Friedmann, D. R., Aguilar, A., Fan, J., Nachury, M. V., and Marmorstein, R. (2012) Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. U.S.A. 109, 19655-19660
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 19655-19660
    • Friedmann, D.R.1    Aguilar, A.2    Fan, J.3    Nachury, M.V.4    Marmorstein, R.5


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