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Volumn 288, Issue 18, 2013, Pages 12901-12909

Mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation stabilizes ISCU protein: Implications for iron metabolism

Author keywords

[No Author keywords available]

Indexed keywords

COFACTORS; COMPLEX 1; IRON METABOLISM; IRON-SULFUR CLUSTERS; MAMMALIAN TARGET; METABOLIC PROCESS; PROTEIN LEVEL; SCAFFOLD PROTEIN;

EID: 84877146678     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.424499     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
    • Ye, H., and Rouault, T. A. (2010) Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease. Biochemistry 49, 4945-4956
    • (2010) Biochemistry , vol.49 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 2
    • 0034331239 scopus 로고    scopus 로고
    • Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
    • Tong, W. H., and Rouault, T. (2000) Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 19, 5692-5700
    • (2000) EMBO J. , vol.19 , pp. 5692-5700
    • Tong, W.H.1    Rouault, T.2
  • 3
    • 44349149346 scopus 로고    scopus 로고
    • Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect
    • DOI 10.1093/hmg/ddn057
    • Olsson, A., Lind, L., Thornell, L. E., and Holmberg, M. (2008) Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11 and caused by an intron mutation in the ISCU gene resulting in a splicing defect. Hum. Mol. Genet. 17, 1666-1672 (Pubitemid 351737170)
    • (2008) Human Molecular Genetics , vol.17 , Issue.11 , pp. 1666-1672
    • Olsson, A.1    Lind, L.2    Thornell, L.-E.3    Holmberg, M.4
  • 4
    • 79953832566 scopus 로고    scopus 로고
    • Tissue-specific splicing of ISCU results in a skeletal muscle phenotype in myopathy with lactic acidosis, while complete loss of ISCU results in early embryonic death in mice
    • Nordin, A., Larsson, E., Thornell, L. E., and Holmberg, M. (2011) Tissue-specific splicing of ISCU results in a skeletal muscle phenotype in myopathy with lactic acidosis, while complete loss of ISCU results in early embryonic death in mice. Hum. Genet. 129, 371-378
    • (2011) Hum. Genet. , vol.129 , pp. 371-378
    • Nordin, A.1    Larsson, E.2    Thornell, L.E.3    Holmberg, M.4
  • 5
    • 70349478990 scopus 로고    scopus 로고
    • MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2
    • Chan, S. Y., Zhang, Y. Y., Hemann, C., Mahoney, C. E., Zweier, J. L., and Loscalzo, J. (2009) MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2. Cell Metab. 10, 273-284
    • (2009) Cell Metab. , vol.10 , pp. 273-284
    • Chan, S.Y.1    Zhang, Y.Y.2    Hemann, C.3    Mahoney, C.E.4    Zweier, J.L.5    Loscalzo, J.6
  • 6
    • 77955170881 scopus 로고    scopus 로고
    • Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression
    • Chen, Z., Li, Y., Zhang, H., Huang, P., and Luthra, R. (2010) Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression. Oncogene 29, 4362-4368
    • (2010) Oncogene , vol.29 , pp. 4362-4368
    • Chen, Z.1    Li, Y.2    Zhang, H.3    Huang, P.4    Luthra, R.5
  • 7
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong, W. H., and Rouault, T. A. (2006) Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 3, 199-210
    • (2006) Cell Metab. , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 8
    • 78650510609 scopus 로고    scopus 로고
    • mTOR: From growth signal integration to cancer, diabetes and ageing
    • Zoncu, R., Efeyan, A., and Sabatini, D. M. (2011) mTOR: from growth signal integration to cancer, diabetes and ageing. Nat. Rev. Mol. Cell Biol. 12, 21-35
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 10
    • 0016176231 scopus 로고
    • Endogenous C-type virus of a mouse cell line and its defectiveness
    • Yoshikura, H., and Hirokawa, Y. (1974) Endogenous C-type virus of a mouse cell line and its defectiveness. J. Virol. 13, 1319-1325
    • (1974) J. Virol. , vol.13 , pp. 1319-1325
    • Yoshikura, H.1    Hirokawa, Y.2
  • 11
    • 27744588780 scopus 로고    scopus 로고
    • Tuberous sclerosis: A GAP at the crossroads of multiple signaling pathways
    • DOI 10.1093/hmg/ddi260
    • Kwiatkowski, D. J., and Manning, B. D. (2005) Tuberous sclerosis: a GAP at the crossroads of multiple signaling pathways. Hum. Mol. Genet. 14, R251-258 (Pubitemid 41631882)
    • (2005) Human Molecular Genetics , vol.14 , Issue.SUPPL. 2
    • Kwiatkowski, D.J.1    Manning, B.D.2
  • 12
    • 0018869666 scopus 로고
    • Induction of fatty acid synthetase synthesis in differentiating 3T3-L1 preadipocytes
    • Student, A. K., Hsu, R. Y., and Lane, M. D. (1980) Induction of fatty acid synthetase synthesis in differentiating 3T3-L1 preadipocytes. J. Biol. Chem. 255, 4745-4750 (Pubitemid 10060752)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.10 , pp. 4745-4750
    • Kaiden, S.A.1    Hsu, R.Y.2    Lane, M.D.3
  • 15
    • 66349106471 scopus 로고    scopus 로고
    • Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach
    • Gauci, S., Helbig, A. O., Slijper, M., Krijgsveld, J., Heck, A. J., and Mohammed, S. (2009) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. 81, 4493-4501
    • (2009) Anal. Chem. , vol.81 , pp. 4493-4501
    • Gauci, S.1    Helbig, A.O.2    Slijper, M.3    Krijgsveld, J.4    Heck, A.J.5    Mohammed, S.6
  • 16
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • Mayya, V., Lundgren, D. H., Hwang, S. I., Rezaul, K., Wu, L., Eng, J. K., Rodionov, V., and Han, D. K. (2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal 2, ra46
    • (2009) Sci. Signal , vol.2
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 17
    • 33644886769 scopus 로고    scopus 로고
    • Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation
    • Tzatsos, A., and Kandror, K. V. (2006) Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation. Mol. Cell Biol. 26, 63-76
    • (2006) Mol. Cell Biol. , vol.26 , pp. 63-76
    • Tzatsos, A.1    Kandror, K.V.2
  • 18
    • 77952036652 scopus 로고    scopus 로고
    • Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control of RNA polymerase III-dependent transcription in cancer cells
    • Shor, B., Wu, J., Shakey, Q., Toral-Barza, L., Shi, C., Follettie, M., and Yu, K. (2010) Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control of RNA polymerase III-dependent transcription in cancer cells. J. Biol. Chem. 285, 15380-15392
    • (2010) J. Biol. Chem. , vol.285 , pp. 15380-15392
    • Shor, B.1    Wu, J.2    Shakey, Q.3    Toral-Barza, L.4    Shi, C.5    Follettie, M.6    Yu, K.7
  • 19
    • 47049127002 scopus 로고    scopus 로고
    • Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation
    • Wang, L., Harris, T. E., and Lawrence, J. C., Jr. (2008) Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation. J. Biol. Chem. 283, 15619-15627
    • (2008) J. Biol. Chem. , vol.283 , pp. 15619-15627
    • Wang, L.1    Harris, T.E.2    Lawrence Jr., J.C.3
  • 21
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B., Latham, V., and Sullivan, M. (2012) PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-270
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 24
    • 0030781431 scopus 로고    scopus 로고
    • Active unfolding of precursor proteins during mitochondrial protein import
    • Matouschek, A., Azem, A., Ratliff, K., Glick, B. S., Schmid, K., and Schatz, G. (1997) Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 16, 6727-6736 (Pubitemid 27503485)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6727-6736
    • Matouschek, A.1    Azem, A.2    Ratliff, K.3    Glick, B.S.4    Schmid, K.5    Schatz, G.6
  • 26
    • 0033968596 scopus 로고    scopus 로고
    • Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR
    • DOI 10.1016/S0960-9822(99)00268-7
    • Yokogami, K., Wakisaka, S., Avruch, J., and Reeves, S. A. (2000) Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR. Curr. Biol. 10, 47-50 (Pubitemid 30057415)
    • (2000) Current Biology , vol.10 , Issue.1 , pp. 47-50
    • Yokogami, K.1    Wakisaka, S.2    Avruch, J.3    Reeves, S.A.4
  • 27
    • 77952562382 scopus 로고    scopus 로고
    • Glucose addiction of TSC null cells is caused by failed mTORC1-dependent balancing of metabolic demand with supply
    • Choo, A. Y., Kim, S. G., Vander Heiden, M. G., Mahoney, S. J., Vu, H., Yoon, S. O., Cantley, L. C., and Blenis, J. (2010) Glucose addiction of TSC null cells is caused by failed mTORC1-dependent balancing of metabolic demand with supply. Mol. Cell 38, 487-499
    • (2010) Mol. Cell , vol.38 , pp. 487-499
    • Choo, A.Y.1    Kim, S.G.2    Vander Heiden, M.G.3    Mahoney, S.J.4    Vu, H.5    Yoon, S.O.6    Cantley, L.C.7    Blenis, J.8
  • 28
    • 84862882932 scopus 로고    scopus 로고
    • Design of iron chelators with therapeutic application
    • Zhou, T., Ma, Y., Kong, X., and Hider, R. C. (2012) Design of iron chelators with therapeutic application. Dalton Trans. 41, 6371-6389
    • (2012) Dalton Trans. , vol.41 , pp. 6371-6389
    • Zhou, T.1    Ma, Y.2    Kong, X.3    Hider, R.C.4
  • 29
    • 78751616780 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR) inhibitors: Potential uses and a review of haematological adverse effects
    • Sofroniadou, S., and Goldsmith, D. (2011) Mammalian target of rapamycin (mTOR) inhibitors: potential uses and a review of haematological adverse effects. Drug Saf. 34, 97-115
    • (2011) Drug Saf. , vol.34 , pp. 97-115
    • Sofroniadou, S.1    Goldsmith, D.2
  • 30
    • 77957874796 scopus 로고    scopus 로고
    • Erythropoiesis and iron sulfur cluster biogenesis
    • Ye, H., and Rouault, T. A. (2010) Erythropoiesis and iron sulfur cluster biogenesis. Adv. Hematol. 2010, 329394
    • (2010) Adv. Hematol. , vol.2010 , pp. 329394
    • Ye, H.1    Rouault, T.A.2


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