메뉴 건너뛰기




Volumn 20, Issue 20, 2011, Pages 3986-3996

The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALPHA TUBULIN; HYDROLASE; SIRTUIN 2; SIRTUIN 2 MICROTUBULE DEACETYLASE; TUBULIN ACETYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 80053137033     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr326     Document Type: Article
Times cited : (159)

References (47)
  • 1
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G. and Guarente, L. (2004) The Sir2 family of protein deacetylases. Annu. Rev. Biochem., 73, 417-435.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 2
    • 25144496904 scopus 로고    scopus 로고
    • The Sir 2 family of protein deacetylases
    • Denu, J.M. (2005) The Sir 2 family of protein deacetylases. Curr. Opin. Chem. Biol., 9, 431-440.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 431-440
    • Denu, J.M.1
  • 3
    • 77953257025 scopus 로고    scopus 로고
    • Aging and disease: connections to sirtuins
    • Donmez, G. and Guarente, L. (2010) Aging and disease: connections to sirtuins. Aging Cell, 9, 285-290.
    • (2010) Aging Cell , vol.9 , pp. 285-290
    • Donmez, G.1    Guarente, L.2
  • 4
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M. and Guarente, L. (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev., 13, 2570-2580.
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 5
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina, B. and Helfand, S.L. (2004) Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl Acad. Sci. USA, 101, 15998-16003.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 6
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • Michan, S. and Sinclair, D. (2007) Sirtuins in mammals: insights into their biological function. Biochem. J., 404, 1-13.
    • (2007) Biochem. J. , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 8
    • 77149172855 scopus 로고    scopus 로고
    • SIRT2-mediated protein deacetylation: an emerging key regulator in brain physiology and pathology
    • Harting, K. and Knoll, B. (2010) SIRT2-mediated protein deacetylation: an emerging key regulator in brain physiology and pathology. Eur. J. Cell. Biol., 89, 262-269.
    • (2010) Eur. J. Cell. Biol. , vol.89 , pp. 262-269
    • Harting, K.1    Knoll, B.2
  • 9
    • 58149339917 scopus 로고    scopus 로고
    • Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity
    • Pfister, J.A., Ma, C., Morrison, B.E. and D'Mello, S.R. (2008) Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity. PLoS One, 3, e4090.
    • (2008) PLoS One , vol.3
    • Pfister, J.A.1    Ma, C.2    Morrison, B.E.3    D'Mello, S.R.4
  • 10
    • 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. and Koike, T. (2007) 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) Neuroscience , vol.147 , pp. 599-612
    • Suzuki, K.1    Koike, T.2
  • 14
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden, S.C., Nahhas, F.A., Nowak, J.E., Goustin, A.S. and Tainsky, M.A. (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol., 23, 3173-3185.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.S.4    Tainsky, M.A.5
  • 16
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alphα-tubulin
    • Li, W., Zhang, B., Tang, J., Cao, Q., Wu, Y., Wu, C., Guo, J., Ling, E.A. and Liang, F. (2007) Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alphα-tubulin. J. Neurosci., 27, 2606-2616.
    • (2007) J. Neurosci. , vol.27 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6    Guo, J.7    Ling, E.A.8    Liang, F.9
  • 19
    • 77955272733 scopus 로고    scopus 로고
    • Tubulin post-translational modifications: encoding functions on the neuronal microtubule cytoskeleton
    • Janke, C. and Kneussel, M. (2010) Tubulin post-translational modifications: encoding functions on the neuronal microtubule cytoskeleton. Trends Neurosci., 33, 362-372.
    • (2010) Trends Neurosci , vol.33 , pp. 362-372
    • Janke, C.1    Kneussel, M.2
  • 20
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: more than just a post-translational modification?
    • Perdiz, D., Mackeh, R., Pous, 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    Pous, C.3    Baillet, A.4
  • 22
    • 73449139095 scopus 로고    scopus 로고
    • Elongator -an emerging role in neurological disorders
    • Nguyen, L., Humbert, S., Saudou, F. and Chariot, A. (2010) Elongator -an emerging role in neurological disorders. Trends Mol. Med., 16, 1-6.
    • (2010) Trends Mol. Med. , vol.16 , pp. 1-6
    • Nguyen, L.1    Humbert, S.2    Saudou, F.3    Chariot, A.4
  • 23
    • 79952211581 scopus 로고    scopus 로고
    • Elongator: an ancestral complex driving transcription and migration through protein acetylation
    • Creppe, C. and Buschbeck, M. (2011) Elongator: an ancestral complex driving transcription and migration through protein acetylation. J. Biomed. Biotechnol., 2011, 924898.
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 924898
    • Creppe, C.1    Buschbeck, M.2
  • 24
    • 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., Cordelieres, 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    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 25
    • 77958569746 scopus 로고    scopus 로고
    • Impaired function of HDAC6 slows down axonal growth and interferes with axon initial segment development
    • Tapia, M., Wandosell, F. and Garrido, J.J. (2010) Impaired function of HDAC6 slows down axonal growth and interferes with axon initial segment development. PLoS One, 5, e12908.
    • (2010) PLoS One , vol.5
    • Tapia, M.1    Wandosell, F.2    Garrido, J.J.3
  • 26
    • 77956525855 scopus 로고    scopus 로고
    • HDAC6 regulates mitochondrial transport in hippocampal neurons
    • Chen, S., Owens, G.C., Makarenkova, H. and Edelman, D.B. (2010) HDAC6 regulates mitochondrial transport in hippocampal neurons. PLoS One, 5, e10848.
    • (2010) PLoS One , vol.5
    • Chen, S.1    Owens, G.C.2    Makarenkova, H.3    Edelman, D.B.4
  • 29
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S. and Matthias, P. (2003) HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J., 22, 1168-1179.
    • (2003) EMBO J , vol.22 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 31
    • 34547920351 scopus 로고    scopus 로고
    • Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin
    • Nahhas, F., Dryden, S.C., Abrams, J. and Tainsky, M.A. (2007) Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin. Mol. Cell. Biochem., 303, 221-230.
    • (2007) Mol. Cell. Biochem. , vol.303 , pp. 221-230
    • Nahhas, F.1    Dryden, S.C.2    Abrams, J.3    Tainsky, M.A.4
  • 33
    • 33846930889 scopus 로고    scopus 로고
    • Microtubule deacetylases, SirT2 and HDAC6, in the nervous system
    • Southwood, C.M., Peppi, M., Dryden, S., Tainsky, M.A. and Gow, A. (2007) Microtubule deacetylases, SirT2 and HDAC6, in the nervous system. Neurochem. Res., 32, 187-195.
    • (2007) Neurochem. Res. , vol.32 , pp. 187-195
    • Southwood, C.M.1    Peppi, M.2    Dryden, S.3    Tainsky, M.A.4    Gow, A.5
  • 34
    • 84873376098 scopus 로고    scopus 로고
    • Evaluation of histone deacetylases as drug targets in Huntington's disease models. Study of HDACs in brain tissues from R6/2 and CAG140 knock-in HD mouse models and human patients and in a neuronal HD cell model
    • Quinti, L., Chopra, V., Rotili, D., Valente, S., Amore, A., Franci, G., Meade, S., Valenza, M., Altucci, L., Maxwell, M.M. et al. (2010) Evaluation of histone deacetylases as drug targets in Huntington's disease models. Study of HDACs in brain tissues from R6/2 and CAG140 knock-in HD mouse models and human patients and in a neuronal HD cell model. PLoS Curr., 2, RRN1172.
    • (2010) PLoS Curr , vol.2
    • Quinti, L.1    Chopra, V.2    Rotili, D.3    Valente, S.4    Amore, A.5    Franci, G.6    Meade, S.7    Valenza, M.8    Altucci, L.9    Maxwell, M.M.10
  • 36
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation
    • Jing, E., Gesta, S. and Kahn, C.R. (2007) SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab., 6, 105-114.
    • (2007) Cell Metab , vol.6 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 37
    • 64049089450 scopus 로고    scopus 로고
    • SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma
    • Wang, F. and Tong, Q. (2009) SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma. Mol. Biol. Cell, 20, 801-808.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 801-808
    • Wang, F.1    Tong, Q.2
  • 38
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang, F., Nguyen, M., Qin, F.X. and Tong, Q. (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell, 6, 505-514.
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 40
    • 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
  • 41
    • 33645299025 scopus 로고    scopus 로고
    • Ageing and neuronal vulnerability
    • Mattson, M.P. and Magnus, T. (2006) Ageing and neuronal vulnerability. Nat. Rev. Neurosci., 7, 278-294.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 278-294
    • Mattson, M.P.1    Magnus, T.2
  • 45
    • 34547839586 scopus 로고    scopus 로고
    • Potential role of tubulin acetylation and microtubule-based protein trafficking in familial dysautonomia
    • Gardiner, J., Barton, D., Marc, J. and Overall, R. (2007) Potential role of tubulin acetylation and microtubule-based protein trafficking in familial dysautonomia. Traffic, 8, 1145-1149.
    • (2007) Traffic , vol.8 , pp. 1145-1149
    • Gardiner, J.1    Barton, D.2    Marc, J.3    Overall, R.4
  • 46
    • 1542267797 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of mutant superoxide dismutase rescues cyclosporin A-induced death in cultured neuroblastoma cells
    • Maxwell, M.M., Pasinelli, P., Kazantsev, A.G. and Brown, R.H. Jr. (2004) RNA interference-mediated silencing of mutant superoxide dismutase rescues cyclosporin A-induced death in cultured neuroblastoma cells. Proc. Natl Acad. Sci. USA, 101, 3178-3183.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3178-3183
    • Maxwell, M.M.1    Pasinelli, P.2    Kazantsev, A.G.3    Brown Jr., R.H.4
  • 47
    • 73949155373 scopus 로고    scopus 로고
    • Mutant huntingtin and glycogen synthase kinase 3-beta accumulate in neuronal lipid rafts of a presymptomatic knock-in mouse model of Huntington's disease
    • Valencia, A., Reeves, P.B., Sapp, E., Li, X., Alexander, J., Kegel, K.B., Chase, K., Aronin, N. and DiFiglia, M. (2010) Mutant huntingtin and glycogen synthase kinase 3-beta accumulate in neuronal lipid rafts of a presymptomatic knock-in mouse model of Huntington's disease. J. Neurosci. Res., 88, 179-190.
    • (2010) J. Neurosci. Res. , vol.88 , pp. 179-190
    • Valencia, A.1    Reeves, P.B.2    Sapp, E.3    Li, X.4    Alexander, J.5    Kegel, K.B.6    Chase, K.7    Aronin, N.8    DiFiglia, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.