메뉴 건너뛰기




Volumn 2, Issue , 2012, Pages

The NAD +-dependent protein deacetylase activity of SIRT1 is regulated by its oligomeric status

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53; SIRT1 PROTEIN, MOUSE; SIRTUIN 1;

EID: 84866116711     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00640     Document Type: Article
Times cited : (36)

References (27)
  • 1
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • DOI 10.1146/annurev.biochem.73.011303.073651
    • Blander, G. & Guarente, L. The Sir2 family of protein deacetylases. Annu Rev Biochem 73, 417-35 (2004). (Pubitemid 39050375)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 2
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • DOI 10.1006/bbrc.2000.3000
    • Frye, R. A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273, 793-8 (2000). (Pubitemid 30599063)
    • (2000) Biochemical and Biophysical Research Communications , vol.273 , Issue.2 , pp. 793-798
    • Frye, R.A.1
  • 3
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis,M. C. & Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol 5, 253-95 (2010).
    • (2010) Annu Rev Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 4
    • 79953898189 scopus 로고    scopus 로고
    • Sirtuin 1 in lipid metabolism and obesity
    • Schug, T. T. & Li, X. Sirtuin 1 in lipid metabolism and obesity. Annals of Medicine 43, 198-211 (2011).
    • (2011) Annals of Medicine , vol.43 , pp. 198-211
    • Schug, T.T.1    Li, X.2
  • 5
    • 54249107873 scopus 로고    scopus 로고
    • The ups and downs of SIRT1
    • Kwon, H. S. & Ott, M. The ups and downs of SIRT1. Trends Biochem Sci 33, 517-25 (2008).
    • (2008) Trends Biochem Sci , vol.33 , pp. 517-525
    • Kwon, H.S.1    Ott, M.2
  • 7
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer?
    • Brooks, C. L. & Gu, W. How does SIRT1 affect metabolism, senescence and cancer? Nat Rev Cancer 9, 123-8 (2009).
    • (2009) Nat Rev Cancer , vol.9 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 10
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • DOI 10.1038/nature06515, PII NATURE06515
    • Zhao, W. et al.Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451, 587-90 (2008). (Pubitemid 351186268)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 587-590
    • Zhao, W.1    Kruse, J.-P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 11
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • DOI 10.1038/nature06500, PII NATURE06500
    • Kim, J. E., Chen, J. & Lou, Z. DBC1 is a negative regulator of SIRT1. Nature 451, 583-6 (2008). (Pubitemid 351186264)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 583-586
    • Kim, J.-E.1    Chen, J.2    Lou, Z.3
  • 12
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim, E. J., Kho, J.H., Kang,M. R. & Um, S. J. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 28, 277-90 (2007).
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 14
    • 58149202185 scopus 로고    scopus 로고
    • Phosphorylation regulates SIRT1 function
    • Sasaki, T. et al. Phosphorylation regulates SIRT1 function. PLoS One 3, e4020 (2008).
    • (2008) PLoS One , vol.3
    • Sasaki, T.1
  • 15
    • 69949138641 scopus 로고    scopus 로고
    • CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNAdamage
    • Kang, H., Jung, J. W., Kim, M. K. & Chung, J. H. CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNAdamage. PLoS One 4, e6611 (2009).
    • (2009) PLoS One , vol.4
    • Kang, H.1    Jung, J.W.2    Kim, M.K.3    Chung, J.H.4
  • 16
    • 77949539030 scopus 로고    scopus 로고
    • JNK1 phosphorylates SIRT1 and promotes its enzymatic activity
    • Nasrin, N. et al. JNK1 phosphorylates SIRT1 and promotes its enzymatic activity. PLoS One 4, e8414 (2009).
    • (2009) PLoS One , vol.4
    • Nasrin, N.1
  • 17
    • 77951225449 scopus 로고    scopus 로고
    • DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1
    • Guo, X.,Williams, J. G., Schug, T. T. & Li, X. DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1. J Biol Chem 285, 13223-32 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 13223-14132
    • Guo, X.1    Williams, J.G.2    Schug, T.T.3    Li, X.4
  • 18
    • 77949363859 scopus 로고    scopus 로고
    • DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping
    • Kurabayashi, N., Hirota, T., Sakai, M., Sanada, K. & Fukada, Y. DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping. Mol Cell Biol 30, 1757-68 (2010).
    • (2010) Mol Cell Biol , vol.30 , pp. 1757-1768
    • Kurabayashi, N.1    Hirota, T.2    Sakai, M.3    Sanada, K.4    Fukada, Y.5
  • 20
    • 82455219091 scopus 로고    scopus 로고
    • Peptide switch is essential for Sirt1 deacetylase activity
    • Kang, H. et al. Peptide switch is essential for Sirt1 deacetylase activity. Mol Cell 44, 203-13 (2011).
    • (2011) Mol Cell , vol.44 , pp. 203-213
    • Kang, H.1
  • 21
    • 0141618441 scopus 로고    scopus 로고
    • Structure and autoregulation of the yeast Hst2 homolog of Sir2
    • DOI 10.1038/nsb978
    • Zhao, K., Chai, X., Clements, A. &Marmorstein, R. Structure and autoregulation of the yeast Hst2 homolog of Sir2. Nat Struct Biol 10, 864-71 (2003). (Pubitemid 37187660)
    • (2003) Nature Structural Biology , vol.10 , Issue.10 , pp. 864-871
    • Zhao, K.1    Chai, X.2    Clements, A.3    Marmorstein, R.4
  • 22
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • DOI 10.1083/jcb.200205057
    • Schwer, B., North, B. J., Frye, R. A., Ott, M. & Verdin, E. The human silent information regulator (Sir)2 homologue hSIRT3 is amitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 158, 647-57 (2002). (Pubitemid 34920104)
    • (2002) Journal of Cell Biology , vol.158 , Issue.4 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 23
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide, S. D., Anckar, J., Stevens, S. M., Jr., Sistonen, L. & Morimoto, R. I. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323, 1063-6 (2009).
    • (2009) Science , vol.323 , pp. 1063-1116
    • Westerheide, S.D.1    Anckar, J.2    Stevens Jr., S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 24
    • 84255198350 scopus 로고    scopus 로고
    • The cAMP/PKA pathway rapidly activates SIRT1 to promote fatty acid oxidation independently of changes in NAD(1)
    • Gerhart-Hines, Z. et al. The cAMP/PKA pathway rapidly activates SIRT1 to promote fatty acid oxidation independently of changes in NAD(1). Mol Cell 44, 851-63 (2011).
    • (2011) Mol Cell , vol.44 , pp. 851-863
    • Gerhart-Hines, Z.1
  • 25
    • 15444379602 scopus 로고    scopus 로고
    • SIRT1 shows no substrate specificity in vitro
    • Blander, G. et al. SIRT1 shows no substrate specificity in vitro. J Biol Chem 280, 9780-5 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 9780-9795
    • Blander, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.