메뉴 건너뛰기




Volumn 287, Issue 16, 2012, Pages 12750-12758

Silent information regulator 2 (Sir2) and forkhead box O (FOXO) complement mitochondrial dysfunction and dopaminergic neuron loss in Drosophila PTEN-induced kinase 1 (PINK1) null mutant

Author keywords

[No Author keywords available]

Indexed keywords

DELETERIOUS EFFECTS; DOPAMINERGIC NEURONS; DOWNSTREAM TARGET; ECTOPIC EXPRESSIONS; FORKHEAD BOX O; GENETIC ANALYSIS; GENETIC SCREENING; MITOCHONDRIAL DEFECTS; MITOCHONDRIAL DYSFUNCTION; MITOCHONDRIAL FUNCTION; NULL MUTANT; OVER-EXPRESSION; PARKINSON DISEASE;

EID: 84859759299     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.337907     Document Type: Article
Times cited : (51)

References (55)
  • 1
    • 0032497504 scopus 로고    scopus 로고
    • Parkinson disease: First of two parts
    • Lang, A. E., and Lozano, A. M. (1998) Parkinson disease: first of two parts. N. Engl. J. Med. 339, 1044-1053
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1044-1053
    • Lang, A.E.1    Lozano, A.M.2
  • 8
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • DOI 10.1038/nature04788, PII N04788
    • Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J. M., and Chung, J. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441, 1157-1161 (Pubitemid 43990737)
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.-M.10    Chung, J.11
  • 9
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • DOI 10.1038/nature04779, PII N04779
    • Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., and Guo, M. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441, 1162-1166 (Pubitemid 43990738)
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 11
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai, Y., Soda, M., and Takahashi, R. (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275, 35661-35664
    • (2000) J. Biol. Chem. , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 13
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang, Y., Gao, J., Chung, K. K., Huang, H., Dawson, V. L., and Dawson, T. M. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. U.S.A. 97, 13354-13359
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 17
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng, H., Dodson, M. W., Huang, H., and Guo, M. (2008) The Parkinson disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105, 14503-14508
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 19
    • 57749194390 scopus 로고    scopus 로고
    • The PINK1-Parkin pathway is involved in the regulation of mitochondrial remodeling process
    • Park, J., Lee, G., and Chung, J. (2009) The PINK1-Parkin pathway is involved in the regulation of mitochondrial remodeling process. Biochem. Biophys. Res. Commun. 378, 518-523
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 518-523
    • Park, J.1    Lee, G.2    Chung, J.3
  • 20
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon, J. W., Olzmann, J. A., Chin, L. S., and Li, L. (2007) PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. Plos Biol. 5, e172
    • (2007) Plos Biol. , vol.5
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 24
    • 77953084081 scopus 로고    scopus 로고
    • DJ-1 is critical for mitochondrial function and rescues PINK1 loss of function
    • Hao, L. Y., Giasson, B. I., and Bonini, N. M. (2010) DJ-1 is critical for mitochondrial function and rescues PINK1 loss of function. Proc. Natl. Acad. Sci. U.S.A. 107, 9747-9752
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9747-9752
    • Hao, L.Y.1    Giasson, B.I.2    Bonini, N.M.3
  • 25
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • DOI 10.1126/science.1098014
    • Araki, T., Sasaki, Y., and Milbrandt, J. (2004) Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305, 1010-1013 (Pubitemid 39071777)
    • (2004) Science , vol.305 , Issue.5686 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 33
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • DOI 10.1016/S0092-8674(04)00452-0, PII S0092867404004520
    • Accili, D., and Arden, K. C. (2004) FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell 117, 421-426 (Pubitemid 38610228)
    • (2004) Cell , vol.117 , Issue.4 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 35
    • 0042161896 scopus 로고    scopus 로고
    • Control of cell number by Drosophila FOXO: Downstream and feedback regulation of the insulin receptor pathway
    • DOI 10.1101/gad.1098703
    • Puig, O., Marr, M. T., Ruhf, M. L., and Tjian, R. (2003) Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway. Genes Dev. 17, 2006-2020 (Pubitemid 36999327)
    • (2003) Genes and Development , vol.17 , Issue.16 , pp. 2006-2020
    • Puig, O.1    Marr, M.T.2    Ruhf, M.L.3    Tjian, R.4
  • 36
    • 0242539698 scopus 로고    scopus 로고
    • The Drosophila forkhead transcription factor FOXO mediates the reduction in cell number associated with reduced insulin signaling
    • Jünger, M. A., Rintelen, F., Stocker, H., Wasserman, J. D., Végh, M., Radimerski, T., Greenberg, M. E., and Hafen, E. (2003) The Drosophila forkhead transcription factor FOXO mediates the reduction in cell number associated with reduced insulin signaling. J. Biol. 2, 20
    • (2003) J. Biol. , vol.2 , pp. 20
    • Jünger, M.A.1    Rintelen, F.2    Stocker, H.3    Wasserman, J.D.4    Végh, M.5    Radimerski, T.6    Greenberg, M.E.7    Hafen, E.8
  • 37
    • 66049087696 scopus 로고    scopus 로고
    • The coordination of nuclear and mitochondrial communication during aging and calorie restriction
    • Finley, L. W., and Haigis, M. C. (2009) The coordination of nuclear and mitochondrial communication during aging and calorie restriction. Ageing Res. Rev. 8, 173-188
    • (2009) Ageing Res. Rev. , vol.8 , pp. 173-188
    • Finley, L.W.1    Haigis, M.C.2
  • 41
    • 69949138641 scopus 로고    scopus 로고
    • CK2 is the regulator of SIRT1 substrate binding affinity, deacetylase activity, and cellular response to DNA damage
    • Kang, H., Jung, J. W., Kim, M. K., and Chung, J. H. (2009) CK2 is the regulator of SIRT1 substrate binding affinity, deacetylase activity, and cellular response to DNA damage. Plos One 4, e6611
    • (2009) Plos One , vol.4
    • Kang, H.1    Jung, J.W.2    Kim, M.K.3    Chung, J.H.4
  • 42
    • 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., and Li, X. (2010) DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1. J. Biol. Chem. 285, 13223-13232
    • (2010) J. Biol. Chem. , vol.285 , pp. 13223-13232
    • Guo, X.1    Williams, J.G.2    Schug, T.T.3    Li, X.4
  • 43
    • 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., and Um, S. J. (2007) Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol. Cell 28, 277-290
    • (2007) Mol. Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 44
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • DOI 10.1038/nature06500, PII NATURE06500
    • Kim, J. E., Chen, J., and Lou, Z. (2008) DBC1 is a negative regulator of SIRT1. Nature 451, 583-586 (Pubitemid 351186264)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 583-586
    • Kim, J.-E.1    Chen, J.2    Lou, Z.3
  • 45
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • DOI 10.1038/nature06515, PII NATURE06515
    • Zhao, W., Kruse, J. P., Tang, Y., Jung, S. Y., Qin, J., and Gu, W. (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451, 587-590 (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
  • 46
    • 70349438679 scopus 로고    scopus 로고
    • 4E-BP extends lifespan upon dietary restriction by enhancing mitochondrial activity in Drosophila
    • Zid, B. M., Rogers, A. N., Katewa, S. D., Vargas, M. A., Kolipinski, M. C., Lu, T. A., Benzer, S., and Kapahi, P. (2009) 4E-BP extends lifespan upon dietary restriction by enhancing mitochondrial activity in Drosophila. Cell 139, 149-160
    • (2009) Cell , vol.139 , pp. 149-160
    • Zid, B.M.1    Rogers, A.N.2    Katewa, S.D.3    Vargas, M.A.4    Kolipinski, M.C.5    Lu, T.A.6    Benzer, S.7    Kapahi, P.8
  • 48
    • 70349783430 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Parkinson disease genes: Insights from Drosophila
    • Park, J., Kim, Y., and Chung, J. (2009) Mitochondrial dysfunction and Parkinson disease genes: insights from Drosophila. Dis. Model. Mech. 2, 336-340
    • (2009) Dis. Model. Mech. , vol.2 , pp. 336-340
    • Park, J.1    Kim, Y.2    Chung, J.3
  • 54
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani, E., Tao, R. N., and Whitworth, A. J. (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107, 5018-5023
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 55
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway
    • Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., and Pallanck, L. (2010) The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. Plos One 5, e10054
    • (2010) Plos One , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.