메뉴 건너뛰기




Volumn 288, Issue 1, 2013, Pages 552-560

F-box and leucine-rich repeat protein 5 (FBXL5) is required for maintenance of cellular and systemic iron homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; GENES; MAINTENANCE; MAMMALS; PHYSIOLOGY; PROTEINS;

EID: 84872081370     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.426171     Document Type: Article
Times cited : (35)

References (41)
  • 1
    • 78751628651 scopus 로고    scopus 로고
    • Inherited disorders of iron metabolism
    • Camaschella, C., and Poggiali, E. (2011) Inherited disorders of iron metabolism. Curr. Opin. Pediatr. 23, 14-20
    • (2011) Curr. Opin. Pediatr. , vol.23 , pp. 14-20
    • Camaschella, C.1    Poggiali, E.2
  • 3
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault, T. A. (2006) The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2, 406-414
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 4
    • 77954249308 scopus 로고    scopus 로고
    • Two to tango. Regulation of mammalian iron metabolism
    • Hentze, M. W., Muckenthaler, M. U., Galy, B., and Camaschella, C. (2010) Two to tango. Regulation of mammalian iron metabolism. Cell 142, 24-38
    • (2010) Cell , vol.142 , pp. 24-38
    • Hentze, M.W.1    Muckenthaler, M.U.2    Galy, B.3    Camaschella, C.4
  • 5
    • 0032878232 scopus 로고    scopus 로고
    • Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation
    • DOI 10.1016/S1357-2725(99)00080-1, PII S1357272599000801
    • Thomson, A. M., Rogers, J. T., and Leedman, P. J. (1999) Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation. Int. J. Biochem. Cell Biol. 31, 1139-1152 (Pubitemid 29454550)
    • (1999) International Journal of Biochemistry and Cell Biology , vol.31 , Issue.10 , pp. 1139-1152
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 7
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo, B., Phillips, J. D., Yu, Y., and Leibold, E. A. (1995) Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem. 270, 21645-21651
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 8
    • 70350576223 scopus 로고    scopus 로고
    • An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
    • Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H. W., Kinch, L. N., Li, Q., Grishin, N. V., and Bruick, R. K. (2009) An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. Science. 326, 722-726
    • (2009) Science , vol.326 , pp. 722-726
    • Salahudeen, A.A.1    Thompson, J.W.2    Ruiz, J.C.3    Ma, H.W.4    Kinch, L.N.5    Li, Q.6    Grishin, N.V.7    Bruick, R.K.8
  • 10
    • 84859613446 scopus 로고    scopus 로고
    • The structural basis of iron sensing by the human F-box protein FBXL5
    • Shu, C., Sung, M. W., Stewart, M. D., Igumenova, T. I., Tan, X., and Li, P. (2012) The structural basis of iron sensing by the human F-box protein FBXL5. Chembiochem. 13, 788-791
    • (2012) Chembiochem. , vol.13 , pp. 788-791
    • Shu, C.1    Sung, M.W.2    Stewart, M.D.3    Igumenova, T.I.4    Tan, X.5    Li, P.6
  • 12
    • 84863614610 scopus 로고    scopus 로고
    • Hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5) communicates cellular iron and oxygen availability by distinct mechanisms
    • Chollangi, S., Thompson, J. W., Ruiz, J. C., Gardner, K. H., and Bruick, R. K. (2012) Hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5) communicates cellular iron and oxygen availability by distinct mechanisms. J. Biol. Chem. 287, 23710-23717
    • (2012) J. Biol. Chem. , vol.287 , pp. 23710-23717
    • Chollangi, S.1    Thompson, J.W.2    Ruiz, J.C.3    Gardner, K.H.4    Bruick, R.K.5
  • 13
    • 84864312739 scopus 로고    scopus 로고
    • Protein degradation and iron homeostasis
    • Thompson, J. W., and Bruick, R. K. (2012) Protein degradation and iron homeostasis. Biochim. Biophys. Acta. 1823, 1484-1490
    • (2012) Biochim. Biophys. Acta. , vol.1823 , pp. 1484-1490
    • Thompson, J.W.1    Bruick, R.K.2
  • 14
    • 70350357467 scopus 로고    scopus 로고
    • Maintaining mammalian iron and oxygen homeostasis. Sensors, regulation, and cross-talk
    • Salahudeen, A. A., and Bruick, R. K. (2009) Maintaining mammalian iron and oxygen homeostasis. Sensors, regulation, and cross-talk. Ann. N.Y. Acad. Sci. 1177, 30-38
    • (2009) Ann. N.Y. Acad. Sci. , vol.1177 , pp. 30-38
    • Salahudeen, A.A.1    Bruick, R.K.2
  • 15
    • 80052698326 scopus 로고    scopus 로고
    • The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo
    • Moroishi, T., Nishiyama, M., Takeda, Y., Iwai, K., and Nakayama, K. I. (2011) The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo. Cell Metab. 14, 339-351
    • (2011) Cell Metab. , vol.14 , pp. 339-351
    • Moroishi, T.1    Nishiyama, M.2    Takeda, Y.3    Iwai, K.4    Nakayama, K.I.5
  • 16
    • 30944449709 scopus 로고    scopus 로고
    • Generation of conditional alleles of the murine iron regulatory protein (IRP)-1 and -2 genes
    • DOI 10.1002/gene.20169
    • Galy, B., Ferring, D., and Hentze, M. W. (2005) Generation of conditional alleles of the murine iron regulatory protein (IRP)-1 and -2 genes. Genesis 43, 181-188 (Pubitemid 43117834)
    • (2005) Genesis , vol.43 , Issue.4 , pp. 181-188
    • Galy, B.1    Feering, D.2    Hentze, M.W.3
  • 17
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
    • DOI 10.1182/blood-2005-04-1365
    • Galy, B., Ferring, D., Minana, B., Bell, O., Janser, H. G., Muckenthaler, M., Schümann, K., and Hentze, M. W. (2005) Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2). Blood 106, 2580-2589 (Pubitemid 41510837)
    • (2005) Blood , vol.106 , Issue.7 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5    Muckenthaler, M.6    Schumann, K.7    Hentze, M.W.8
  • 18
    • 0037174814 scopus 로고    scopus 로고
    • Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter: Identification of a Ctr1-independent copper transport system
    • DOI 10.1074/jbc.M208002200
    • Lee, J., Petris, M. J., and Thiele, D. J. (2002) Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system. J. Biol. Chem. 277, 40253-40259 (Pubitemid 35215596)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40253-40259
    • Lee, J.1    Petris, M.J.2    Thiele, D.J.3
  • 20
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels
    • Guo, B., Brown, F. M., Phillips, J. D., Yu, Y., and Leibold, E. A. (1995) Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels. J. Biol. Chem. 270, 16529-16535
    • (1995) J. Biol. Chem. , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 21
    • 3042577347 scopus 로고    scopus 로고
    • Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo
    • DOI 10.1261/rna.7220704
    • Galy, B., Ferring, D., Benesova, M., Benes, V., and Hentze, M. W. (2004) Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo. RNA 10, 1019-1025 (Pubitemid 38822138)
    • (2004) RNA , vol.10 , Issue.7 , pp. 1019-1025
    • Galy, B.1    Ferring, D.2    Benesova, M.3    Benes, V.4    Hentze, M.W.5
  • 24
    • 0036215728 scopus 로고    scopus 로고
    • Iron deficiency decreases mitochondrial aconitase abundance and citrate concentration without affecting tricarboxylic acid cycle capacity in rat liver
    • Ross, K. L., and Eisenstein, R. S. (2002) Iron deficiency decreases mitochondrial aconitase abundance and citrate concentration without affecting tricarboxylic acid cycle capacity in rat liver. J. Nutr. 132, 643-651 (Pubitemid 34275061)
    • (2002) Journal of Nutrition , vol.132 , Issue.4 , pp. 643-651
    • Ross, K.L.1    Eisenstein, R.S.2
  • 25
    • 37449009448 scopus 로고    scopus 로고
    • Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
    • Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H. J., and Hentze, M. W. (2008) Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell Metab. 7, 79-85
    • (2008) Cell Metab. , vol.7 , pp. 79-85
    • Galy, B.1    Ferring-Appel, D.2    Kaden, S.3    Gröne, H.J.4    Hentze, M.W.5
  • 27
    • 84861355868 scopus 로고    scopus 로고
    • Hepcidin and iron homeostasis
    • Ganz, T., and Nemeth, E. (2012) Hepcidin and iron homeostasis. Biochim. Biophys. Acta. 1823, 1434-1443
    • (2012) Biochim. Biophys. Acta. , vol.1823 , pp. 1434-1443
    • Ganz, T.1    Nemeth, E.2
  • 28
    • 80052689794 scopus 로고    scopus 로고
    • Hepcidin and ferroportin. The new players in iron metabolism
    • De Domenico, I., Ward, D. M., and Kaplan, J. (2011) Hepcidin and ferroportin. The new players in iron metabolism. Semin. Liver Dis. 31, 272-279
    • (2011) Semin. Liver Dis. , vol.31 , pp. 272-279
    • De Domenico, I.1    Ward, D.M.2    Kaplan, J.3
  • 30
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system. An update
    • Pantopoulos, K. (2004) Iron metabolism and the IRE/IRP regulatory system. An update. Ann. N.Y. Acad. Sci. 1012, 1-13
    • (2004) Ann. N.Y. Acad. Sci. , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 31
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein, R. S. (2000) Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu. Rev. Nutr. 20, 627-662
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 33
    • 0029281832 scopus 로고
    • Differential regulation of two related RNA-binding proteins, iron regulatory protein (IRP), and IRPB
    • Pantopoulos, K., Gray, N. K., and Hentze, M. W. (1995) Differential regulation of two related RNA-binding proteins, iron regulatory protein (IRP), and IRPB. RNA 1, 155-163
    • (1995) RNA , vol.1 , pp. 155-163
    • Pantopoulos, K.1    Gray, N.K.2    Hentze, M.W.3
  • 35
    • 0031047314 scopus 로고    scopus 로고
    • Dietary iron intake modulates the activity of iron regulatory proteins and the abundance of ferritin and mitochondrial aconitase in rat liver
    • Chen, O. S., Schalinske, K. L., and Eisenstein, R. S. (1997) Dietary iron intake modulates the activity of iron regulatory proteins and the abundance of ferritin and mitochondrial aconitase in rat liver. J. Nutr. 127, 238-248 (Pubitemid 27079952)
    • (1997) Journal of Nutrition , vol.127 , Issue.2 , pp. 238-248
    • Chen, O.S.1    Schalinske, K.L.2    Eisenstein, R.S.3
  • 36
    • 0035933846 scopus 로고    scopus 로고
    • IRP1 activation by extracellular oxidative stress in the perfused rat liver
    • Mueller, S., Pantopoulos, K., Hübner, C. A., Stremmel, W., and Hentze, M. W. (2001) IRP1 activation by extracellular oxidative stress in the perfused rat liver. J. Biol. Chem. 276, 23192-23196
    • (2001) J. Biol. Chem. , vol.276 , pp. 23192-23196
    • Mueller, S.1    Pantopoulos, K.2    Hübner, C.A.3    Stremmel, W.4    Hentze, M.W.5
  • 37
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith, S. R., Ghosh, M. C., Ollivierre-Wilson, H., Hang Tong, W., and Rouault, T. A. (2006) Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol. Dis. 36, 283-287
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Hang Tong, W.4    Rouault, T.A.5
  • 39
    • 0142183440 scopus 로고    scopus 로고
    • Effects of iron regulatory protein regulation on iron homeostasis during hypoxia
    • DOI 10.1182/blood-2003-02-0433
    • Schneider, B. D., and Leibold, E. A. (2003) Effects of iron regulatory protein regulation on iron homeostasis during hypoxia. Blood 102, 3404-3411 (Pubitemid 37314783)
    • (2003) Blood , vol.102 , Issue.9 , pp. 3404-3411
    • Schneider, B.D.1    Leibold, E.A.2
  • 40
    • 0026684574 scopus 로고
    • Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein
    • Leibold, E. A., and Guo, B. (1992) Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein. Annu. Rev. Nutr. 12, 345-368
    • (1992) Annu. Rev. Nutr. , vol.12 , pp. 345-368
    • Leibold, E.A.1    Guo, B.2
  • 41
    • 0032830130 scopus 로고    scopus 로고
    • The transferrin receptor: Role in health and disease
    • DOI 10.1016/S1357-2725(99)00070-9, PII S1357272599000709
    • Ponka, P., and Lok, C. N. (1999) The transferrin receptor: role in health and disease. Int. J. Biochem. Cell Biol. 31, 1111-1137 (Pubitemid 29454549)
    • (1999) International Journal of Biochemistry and Cell Biology , vol.31 , Issue.10 , pp. 1111-1137
    • Ponka, P.1    Lok, C.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.