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Volumn 5, Issue , 2015, Pages

New HDAC6-mediated deacetylation sites of tubulin in the mouse brain identified by quantitative mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

HDAC6 PROTEIN, MOUSE; HISTONE DEACETYLASE; LYSINE; PEPTIDE; TUBULIN;

EID: 84947792534     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep16869     Document Type: Article
Times cited : (26)

References (66)
  • 1
    • 34548830425 scopus 로고    scopus 로고
    • The tubulin code
    • Verhey, K. J. & Gaertig, J. The tubulin code. Cell Cycle 6, 2152-2160 (2007).
    • (2007) Cell Cycle , vol.6 , pp. 2152-2160
    • Verhey, K.J.1    Gaertig, J.2
  • 2
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu, F., Zhang, K. & Grunstein, M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121, 375-385 (2005).
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 3
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y. et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953 (2004).
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 4
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • Wang, H. et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol. Cell 22, 383-394 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 383-394
    • Wang, H.1
  • 5
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M. & Schreiber, S. L. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. USA 100, 4389-4394 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 6
    • 43149106461 scopus 로고    scopus 로고
    • Differential trafficking of Kif5c on tyrosinated and detyrosinated microtubules in live cells
    • Dunn, S. et al. Differential trafficking of Kif5c on tyrosinated and detyrosinated microtubules in live cells. J. Cell Sci. 121 1085-1095, (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 1085-1095
    • Dunn, S.1
  • 7
    • 33847688915 scopus 로고    scopus 로고
    • Loss of alpha-tubulin polyglutamylation in ROSA22 mice is associated with abnormal targeting of KIF1A and modulated synaptic function
    • Ikegami, K. et al. Loss of alpha-tubulin polyglutamylation in ROSA22 mice is associated with abnormal targeting of KIF1A and modulated synaptic function. Proc. Natl. Acad. Sci. USA 104, 3213-3218 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3213-3218
    • Ikegami, K.1
  • 8
    • 0034743675 scopus 로고    scopus 로고
    • Structural insight into microtubule function
    • Nogales, E. Structural insight into microtubule function. Annu. Rev. Biophys. Biomol. Struct. 30, 397-420 (2001).
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 397-420
    • Nogales, E.1
  • 9
    • 18844475127 scopus 로고
    • Microtubules are acetylated in domains that turn over slowly
    • Webster, D. R. & Borisy, G. G. Microtubules are acetylated in domains that turn over slowly. J. Cell Sci. 92 (Pt 1), 57-65 (1989).
    • (1989) J. Cell Sci. , vol.92 , pp. 57-65
    • Webster, D.R.1    Borisy, G.G.2
  • 10
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • Piperno, G., LeDizet, M. & Chang, X. J. Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J. Cell Biol. 104, 289-302 (1987).
    • (1987) J. Cell Biol. , vol.104 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.J.3
  • 11
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • Reed, N. A. et al. Microtubule acetylation promotes kinesin-1 binding and transport. Curr. Biol. 16, 2166-2172 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 2166-2172
    • Reed, N.A.1
  • 12
    • 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. et al. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1
  • 13
    • 0021993649 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine
    • L'Hernault, S. W. & Rosenbaum, J. L. Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine. Biochemistry 24, 473-478 (1985).
    • (1985) Biochemistry , vol.24 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 14
    • 0034536319 scopus 로고    scopus 로고
    • Exposure of lumenal microtubule sites after mild fixation
    • Draberova, E., Viklicky, V. & Draber, P. Exposure of lumenal microtubule sites after mild fixation. Eur. J. Cell Biol. 79, 982-985 (2000).
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 982-985
    • Draberova, E.1    Viklicky, V.2    Draber, P.3
  • 15
    • 0033214537 scopus 로고    scopus 로고
    • A structural view of microtubule dynamics
    • Nogales, E. A structural view of microtubule dynamics. Cell. Mol. Life Sci. 56, 133-142 (1999).
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 133-142
    • Nogales, E.1
  • 16
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta, H., Greer, K. & Rosenbaum, J. L. The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103, 571-579 (1986).
    • (1986) J. Cell Biol. , vol.103 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 17
    • 34248213405 scopus 로고    scopus 로고
    • HDAC6 deacetylation of tubulin modulates dynamics of cellular adhesions
    • Tran, A. D. et al. HDAC6 deacetylation of tubulin modulates dynamics of cellular adhesions. J. Cell Sci. 120, 1469-1479 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 1469-1479
    • Tran, A.D.1
  • 18
    • 70350359874 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6
    • Zilberman, Y. et al. Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6. J. Cell Sci. 122, 3531-3541 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3531-3541
    • Zilberman, Y.1
  • 19
    • 76649143069 scopus 로고    scopus 로고
    • Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons
    • Hammond, J. W. et al. Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons. Mol. Biol. Cell 21, 572-583 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 572-583
    • Hammond, J.W.1
  • 20
    • 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. & Verhey, K. J. Single molecule imaging reveals differences in microtubule track selection between Kinesin motors. PLoS Biol. 7, e1000216 (2009).
    • (2009) PLoS Biol. , vol.7
    • Cai, D.1    McEwen, D.P.2    Martens, J.R.3    Meyhofer, E.4    Verhey, K.J.5
  • 21
    • 79951819919 scopus 로고    scopus 로고
    • A novel acetylation of beta-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation
    • Chu, C. W. et al. A novel acetylation of beta-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation.Mol. Biol. Cell 22, 448-456 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 448-456
    • Chu, C.W.1
  • 23
    • 77955459468 scopus 로고    scopus 로고
    • ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules
    • Friedman, J. R., Webster, B. M., Mastronarde, D. N., Verhey, K. J. & Voeltz, G. K. ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules. J. Cell Biol. 190, 363-375 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 363-375
    • Friedman, J.R.1    Webster, B.M.2    Mastronarde, D.N.3    Verhey, K.J.4    Voeltz, G.K.5
  • 24
    • 80054844842 scopus 로고    scopus 로고
    • ER tubules mark sites of mitochondrial division
    • Friedman, J. R. et al. ER tubules mark sites of mitochondrial division. Science 334, 358-362 (2011).
    • (2011) Science , vol.334 , pp. 358-362
    • Friedman, J.R.1
  • 25
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro, T. F. et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317, 516-519 (2007).
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1
  • 26
    • 34250848194 scopus 로고    scopus 로고
    • Mammalian Sir2-related protein (SIRT) 2-mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: A crucial role of tubulin deacetylation
    • Suzuki, K. & Koike, T. Mammalian Sir2-related protein (SIRT) 2-mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: a crucial role of tubulin deacetylation. Neuroscience 147, 599-612 (2007).
    • (2007) Neuroscience , vol.147 , pp. 599-612
    • Suzuki, K.1    Koike, T.2
  • 27
    • 0024511885 scopus 로고
    • Differential localisation of tyrosinated, detyrosinated, and acetylated alpha-tubulins in neurites and growth cones of dorsal root ganglion neurons
    • Robson, S. J. & Burgoyne, R. D. Differential localisation of tyrosinated, detyrosinated, and acetylated alpha-tubulins in neurites and growth cones of dorsal root ganglion neurons. Cell Motil. Cytoskeleton 12, 273-282 (1989).
    • (1989) Cell Motil. Cytoskeleton , vol.12 , pp. 273-282
    • Robson, S.J.1    Burgoyne, R.D.2
  • 28
    • 77956525850 scopus 로고    scopus 로고
    • MEC-17 is an alpha-tubulin acetyltransferase
    • Akella, J. S. et al. MEC-17 is an alpha-tubulin acetyltransferase. Nature 467, 218-222 (2010).
    • (2010) Nature , vol.467 , pp. 218-222
    • Akella, J.S.1
  • 29
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B. & Nachury, M. V. The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 107, 21517-21522 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 30
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin
    • Creppe, C. et al. Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin. Cell 136, 551-564 (2009).
    • (2009) Cell , vol.136 , pp. 551-564
    • Creppe, C.1
  • 31
    • 76749123484 scopus 로고    scopus 로고
    • The Caenorhabditis elegans Elongator complex regulates neuronal alpha-tubulin acetylation
    • Solinger, J. A. et al. The Caenorhabditis elegans Elongator complex regulates neuronal alpha-tubulin acetylation. PLoS Genet. 6, e1000820 (2010).
    • (2010) PLoS Genet. , vol.6
    • Solinger, J.A.1
  • 32
    • 77955330151 scopus 로고    scopus 로고
    • Myc-nick: A cytoplasmic cleavage product of Myc that promotes alpha-tubulin acetylation and cell differentiation
    • Conacci-Sorrell, M., Ngouenet, C. & Eisenman, R. N. Myc-nick: a cytoplasmic cleavage product of Myc that promotes alpha-tubulin acetylation and cell differentiation. Cell 142, 480-493 (2010).
    • (2010) Cell , vol.142 , pp. 480-493
    • Conacci-Sorrell, M.1    Ngouenet, C.2    Eisenman, R.N.3
  • 33
    • 84880066266 scopus 로고    scopus 로고
    • Mice lacking alpha-tubulin acetyltransferase 1 are viable but display alpha-tubulin acetylation deficiency and dentate gyrus distortion
    • Kim, G. W., Li, L., Gorbani, M., You, L. & Yang, X. J. Mice lacking alpha-tubulin acetyltransferase 1 are viable but display alpha-tubulin acetylation deficiency and dentate gyrus distortion. J. Biol. Chem. 288, 20334-20350 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 20334-20350
    • Kim, G.W.1    Li, L.2    Gorbani, M.3    You, L.4    Yang, X.J.5
  • 34
    • 84891620677 scopus 로고    scopus 로고
    • AlphaTAT1 is the major alpha-tubulin acetyltransferase in mice
    • Kalebic, N. et al. alphaTAT1 is the major alpha-tubulin acetyltransferase in mice. Nat. Commun. 4, 1962 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1962
    • Kalebic, N.1
  • 35
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert, C. et al. HDAC6 is a microtubule-associated deacetylase. Nature 417, 455-458 (2002).
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1
  • 36
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • Matsuyama, A. et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J. 21, 6820-6831 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6820-6831
    • Matsuyama, A.1
  • 37
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • Zhang, Y. et al. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168-1179 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1168-1179
    • Zhang, Y.1
  • 39
    • 40749161986 scopus 로고    scopus 로고
    • Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally
    • Zhang, Y. et al. Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally. Mol. Cell. Biol. 28, 1688-1701 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1688-1701
    • Zhang, Y.1
  • 40
    • 79961168180 scopus 로고    scopus 로고
    • HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease
    • d'Ydewalle, C. et al. HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease. Nat. Med. 17, 968-974 (2011).
    • (2011) Nat. Med. , vol.17 , pp. 968-974
    • D'Ydewalle, C.1
  • 41
    • 84856643478 scopus 로고    scopus 로고
    • Loss of deacetylation activity of Hdac6 affects emotional behavior in mice
    • Fukada, M. et al. Loss of deacetylation activity of Hdac6 affects emotional behavior in mice. PLoS One 7, e30924 (2012).
    • (2012) PLoS One , vol.7
    • Fukada, M.1
  • 42
    • 84871946821 scopus 로고    scopus 로고
    • Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease
    • Govindarajan, N. et al. Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease. EMBO Mol. Med. 5, 52-63 (2013).
    • (2013) EMBO Mol. Med. , vol.5 , pp. 52-63
    • Govindarajan, N.1
  • 43
    • 84890546642 scopus 로고    scopus 로고
    • Antidepressant-like properties of novel HDAC6-selective inhibitors with improved brain bioavailability
    • Jochems, J. et al. Antidepressant-like properties of novel HDAC6-selective inhibitors with improved brain bioavailability. Neuropsychopharmacology 39, 389-400 (2014).
    • (2014) Neuropsychopharmacology , vol.39 , pp. 389-400
    • Jochems, J.1
  • 44
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali, P. et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 280, 26729-26734 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 26729-26734
    • Bali, P.1
  • 45
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs, J. J. et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol. Cell 18, 601-607 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1
  • 46
    • 34447315270 scopus 로고    scopus 로고
    • HDAC6 modulates cell motility by altering the acetylation level of cortactin
    • Zhang, X. et al. HDAC6 modulates cell motility by altering the acetylation level of cortactin. Mol. Cell 27, 197-213, (2007).
    • (2007) Mol. Cell , vol.27 , pp. 197-213
    • Zhang, X.1
  • 47
    • 47749156827 scopus 로고    scopus 로고
    • HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation
    • Parmigiani, R. B. et al. HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation. Proc. Natl. Acad. Sci. USA 105, 9633-9638, (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9633-9638
    • Parmigiani, R.B.1
  • 48
    • 45149089913 scopus 로고    scopus 로고
    • HDAC6 is required for epidermal growth factor-induced beta-catenin nuclear localization
    • Li, Y., Zhang, X., Polakiewicz, R. D., Yao, T. P. & Comb, M. J. HDAC6 is required for epidermal growth factor-induced beta-catenin nuclear localization. J. Biol. Chem. 283, 12686-12690 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 12686-12690
    • Li, Y.1    Zhang, X.2    Polakiewicz, R.D.3    Yao, T.P.4    Comb, M.J.5
  • 49
    • 79953203531 scopus 로고    scopus 로고
    • Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6
    • Huo, L. et al. Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6. J. Biol. Chem. 286, 9280-9286 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 9280-9286
    • Huo, L.1
  • 50
  • 51
    • 84859508081 scopus 로고    scopus 로고
    • Histone deacetylase 6 (HDAC6) deacetylates survivin for its nuclear export in breast cancer
    • Riolo, M. T. et al. Histone deacetylase 6 (HDAC6) deacetylates survivin for its nuclear export in breast cancer. J. Biol. Chem. 287, 10885-10893 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 10885-10893
    • Riolo, M.T.1
  • 52
    • 84922080063 scopus 로고    scopus 로고
    • Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity
    • Zhang, L. et al. Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity. Protein Cell 6, 42-54 (2015).
    • (2015) Protein Cell , vol.6 , pp. 42-54
    • Zhang, L.1
  • 53
    • 79953219078 scopus 로고    scopus 로고
    • Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner
    • Li, D. et al. Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner. Protein Cell 2, 150-160 (2011).
    • (2011) Protein Cell , vol.2 , pp. 150-160
    • Li, D.1
  • 54
    • 84898599000 scopus 로고    scopus 로고
    • Histone deacetylase 6 and cytoplasmic linker protein 170 function together to regulate the motility of pancreatic cancer cells
    • Li, D. et al. Histone deacetylase 6 and cytoplasmic linker protein 170 function together to regulate the motility of pancreatic cancer cells. Protein Cell 5, 214-223 (2014).
    • (2014) Protein Cell , vol.5 , pp. 214-223
    • Li, D.1
  • 55
    • 37449030154 scopus 로고    scopus 로고
    • The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response
    • Kwon, S., Zhang, Y. & Matthias, P. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev. 21, 3381-3394 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 3381-3394
    • Kwon, S.1    Zhang, Y.2    Matthias, P.3
  • 56
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C. et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834-840 (2009).
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 57
    • 84903900696 scopus 로고    scopus 로고
    • Assessment of BAK1 activity in different plant receptor-like kinase complexes by quantitative profiling of phosphorylation patterns
    • Wang, Y. et al. Assessment of BAK1 activity in different plant receptor-like kinase complexes by quantitative profiling of phosphorylation patterns. J. Proteomics 108, 484-493 (2014).
    • (2014) J. Proteomics , vol.108 , pp. 484-493
    • Wang, Y.1
  • 58
    • 84887546676 scopus 로고    scopus 로고
    • Identification and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1
    • Xu, J. et al. Identification and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1. Protein Cell 4, 771-781 (2013).
    • (2013) Protein Cell , vol.4 , pp. 771-781
    • Xu, J.1
  • 59
    • 77955296287 scopus 로고    scopus 로고
    • Methods in tubulin proteomics
    • Miller, L. M. et al. Methods in tubulin proteomics. Methods Cell Biol. 95, 105-126 (2010).
    • (2010) Methods Cell Biol. , vol.95 , pp. 105-126
    • Miller, L.M.1
  • 60
    • 0015520152 scopus 로고
    • Microtubule formation in vitro in solutions containing low calcium concentrations
    • Weisenberg, R. C. Microtubule formation in vitro in solutions containing low calcium concentrations. Science 177, 1104-1105 (1972).
    • (1972) Science , vol.177 , pp. 1104-1105
    • Weisenberg, R.C.1
  • 61
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G. & Downing, K. H. Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391, 199-203 (1998).
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 62
    • 0025758171 scopus 로고
    • A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity
    • Edde, B. et al. A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity. J. Cell. Biochem. 46, 134-142 (1991).
    • (1991) J. Cell. Biochem. , vol.46 , pp. 134-142
    • Edde, B.1
  • 63
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas alpha-tubulin
    • LeDizet, M. & Piperno, G. Identification of an acetylation site of Chlamydomonas alpha-tubulin. Proc. Natl. Acad. Sci. USA 84, 5720-5724 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5720-5724
    • LeDizet, M.1    Piperno, G.2
  • 64
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger, C. M., Hassig, C. A. & Schreiber, S. L. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl. Acad. Sci. USA 96, 4868-4873 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 65
    • 37549010715 scopus 로고    scopus 로고
    • Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis
    • Gao, Y. S. et al. Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis. Mol. Cell. Biol. 27, 8637-8647 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8637-8647
    • Gao, Y.S.1
  • 66
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V. & Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860 (2006).
    • (2006) Nat. Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.