메뉴 건너뛰기




Volumn 23, Issue 19, 2003, Pages 6973-6981

A phosphomimetic mutation at Ser-138 renders iron regulatory protein 1 sensitive to iron-dependent degradation

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; DEFEROXAMINE; GLUTAMINE; IRON; IRON CHELATING AGENT; IRON REGULATORY PROTEIN 1; LACTACYSTIN; MESSENGER RNA; PROTEASOME INHIBITOR; REGULATOR PROTEIN; SERINE; SULFUR; UNCLASSIFIED DRUG;

EID: 0141781072     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.19.6973-6981.2003     Document Type: Article
Times cited : (43)

References (29)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., R. H. Holm, and E. Münck. 1997. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277:653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 2
    • 0033618254 scopus 로고    scopus 로고
    • Human cytoplasmic aconitase (iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding
    • Brazzolotto, X., J. Gaillard, K. Pantopoulos, M. W. Hentze, and J.-M. Moulis. 1999. Human cytoplasmic aconitase (iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding. J. Biol. Chem. 274:21625-21630.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21625-21630
    • Brazzolotto, X.1    Gaillard, J.2    Pantopoulos, K.3    Hentze, M.W.4    Moulis, J.-M.5
  • 3
    • 0032417611 scopus 로고    scopus 로고
    • Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1
    • Brown, N. M., S. A. Anderson, D. W. Steffen, T. B. Carpenter, M. C. Kennedy, W. E. Walden, and R. S. Eisenstein. 1998. Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1. Proc. Natl. Acad. Sci. USA 95:15235-15240.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15235-15240
    • Brown, N.M.1    Anderson, S.A.2    Steffen, D.W.3    Carpenter, T.B.4    Kennedy, M.C.5    Walden, W.E.6    Eisenstein, R.S.7
  • 4
    • 0036510621 scopus 로고    scopus 로고
    • Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1: Insights into the mechanism of Fe-S cluster cycling
    • Brown, N. M., M. C. Kennedy, W. E. Antholine, R. S. Eisenstein, and W. E. Walden. 2002. Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1: insights into the mechanism of Fe-S cluster cycling. J. Biol. Chem. 277:7246-7254.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7246-7254
    • Brown, N.M.1    Kennedy, M.C.2    Antholine, W.E.3    Eisenstein, R.S.4    Walden, W.E.5
  • 5
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • Cairo, G., and A. Pietrangelo. 2000. Iron regulatory proteins in pathobiology. Biochem. J. 352:241-250.
    • (2000) Biochem. J. , vol.352 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 6
    • 0034696944 scopus 로고    scopus 로고
    • MAPK-dependent expression of p21(WAF) and p27(kip1) in PMA-induced differentiation of HL60 cells
    • Das, D., G. Pintucci, and A. Stern. 2000. MAPK-dependent expression of p21(WAF) and p27(kip1) in PMA-induced differentiation of HL60 cells. FEBS Lett. 472:50-52.
    • (2000) FEBS Lett. , vol.472 , pp. 50-52
    • Das, D.1    Pintucci, G.2    Stern, A.3
  • 7
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier, J. C., H. Hirling, J. Wietzerbin, P. Kaldy, and L. C. Kühn. 1993. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12:3643-3649.
    • (1993) EMBO J. , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kühn, L.C.5
  • 8
    • 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
  • 10
    • 0033525713 scopus 로고    scopus 로고
    • Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress
    • Gehring, N., M. W. Hentze, and K. Pantopoulos. 1999. Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress. J. Biol. Chem. 274:6219-6225.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6219-6225
    • Gehring, N.1    Hentze, M.W.2    Pantopoulos, K.3
  • 11
    • 0011975708 scopus 로고
    • Enhanced degradation of the ferritin repressor protein during induction of ferritin messenger RNA translation
    • Goessling, L. S., S. Daniels-McQueen, M. Bhattacharyya-Pakrasi, J.-J. Lin, and R. E. Thach. 1992. Enhanced degradation of the ferritin repressor protein during induction of ferritin messenger RNA translation. Science 256:670-673.
    • (1992) Science , vol.256 , pp. 670-673
    • Goessling, L.S.1    Daniels-McQueen, S.2    Bhattacharyya-Pakrasi, M.3    Lin, J.-J.4    Thach, R.E.5
  • 12
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89:5547-5551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 13
    • 0027131432 scopus 로고
    • Recombinant iron regulatory factor functions as an iron-responsive element-binding protein, a translational repressor and an aconitase: A functional assay for translational repression and direct demonstration of the iron switch
    • Gray, N. K., S. Quick, B. Goossen, A. Constable, H. Hirling, L. C. Kühn, and M. W. Hentze. 1993. Recombinant iron regulatory factor functions as an iron-responsive element-binding protein, a translational repressor and an aconitase: a functional assay for translational repression and direct demonstration of the iron switch. Eur. J. Biochem. 218:657-667.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 657-667
    • Gray, N.K.1    Quick, S.2    Goossen, B.3    Constable, A.4    Hirling, H.5    Kühn, L.C.6    Hentze, M.W.7
  • 14
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo, B., J. D. Phillips, Y. Yu, and E. A. Leibold. 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
  • 15
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • Haile, D. J., T. A. Rouault, J. B. Harford, M. C. Kennedy, G. A. Blondin, H. Beinert, and R. D. Klausner. 1992. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc. Natl. Acad. Sci. USA 89:11735-11739.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 16
    • 0032812762 scopus 로고    scopus 로고
    • Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species
    • Hanson, E. S., and E. A. Leibold. 1999. Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species. Gene Expr. 7:367-376.
    • (1999) Gene Expr. , vol.7 , pp. 367-376
    • Hanson, E.S.1    Leibold, E.A.2
  • 17
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai, K., R. D. Klausner, and T. A. Rouault. 1995. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J. 14:5350-5357.
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 18
    • 0011141395 scopus 로고    scopus 로고
    • Iron-response element (IRE) structure and combinatorial RNA regulation
    • D. M. Templeton (ed.). Marcel Dekker, Inc., New York, N.Y.
    • Johansson, H. E., and E. C. Theil. 2002. Iron-response element (IRE) structure and combinatorial RNA regulation, p. 237-253. In D. M. Templeton (ed.), Molecular and cellular iron transport. Marcel Dekker, Inc., New York, N.Y.
    • (2002) Molecular and Cellular Iron Transport , pp. 237-253
    • Johansson, H.E.1    Theil, E.C.2
  • 19
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: Implications for macrophage iron homeostasis
    • Kim, S., and P. Ponka. 2002. Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc. Natl. Acad. Sci. USA 99:12214-12219.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 20
    • 0032571002 scopus 로고    scopus 로고
    • Inducible expression of IκBα repressor mutants interferes with NF-κB activity and HIV-1 replication in Jurkat T cells
    • Kwon, H., N. Pelletier, C. DeLuca, P. Genin, S. Cisternas, R. Lin, M. A. Wainberg, and J. Hiscott. 1998. Inducible expression of IκBα repressor mutants interferes with NF-κB activity and HIV-1 replication in Jurkat T cells. J. Biol. Chem. 273:7431-7440.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7431-7440
    • Kwon, H.1    Pelletier, N.2    DeLuca, C.3    Genin, P.4    Cisternas, S.5    Lin, R.6    Wainberg, M.A.7    Hiscott, J.8
  • 21
    • 0036358643 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 (IRP1) by oxidative stress
    • Mueller, S., and K. Pantopoulos. 2002. Activation of iron regulatory protein-1 (IRP1) by oxidative stress. Methods Enzymol. 348:324-337.
    • (2002) Methods Enzymol. , vol.348 , pp. 324-337
    • Mueller, S.1    Pantopoulos, K.2
  • 23
    • 0000901196 scopus 로고    scopus 로고
    • Nitric oxide, oxygen radicals and iron metabolism
    • L. Ignarro (ed.). Academic Press, San Diego, Calif.
    • Pantopoulos, K., and M. W. Hentze. 2000. Nitric oxide, oxygen radicals and iron metabolism, p. 293-313. In L. Ignarro (ed.), Nitric oxide. Academic Press, San Diego, Calif.
    • (2000) Nitric Oxide , pp. 293-313
    • Pantopoulos, K.1    Hentze, M.W.2
  • 24
    • 0022406630 scopus 로고
    • Acquisition of iron from transferrin regulates reticulocyte heme synthesis
    • Ponka, P., and H. M. Schulman. 1985. Acquisition of iron from transferrin regulates reticulocyte heme synthesis. J. Biol. Chem. 260:14717-14721.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14717-14721
    • Ponka, P.1    Schulman, H.M.2
  • 25
    • 0002463490 scopus 로고    scopus 로고
    • Translational control of ferritin synthesis
    • N. Sonenberg, J. W. B. Hershey, and M. B. Mathews (ed.). Cold Spring Harbor Laboratory Press. Cold Spring Harbor, N.Y.
    • Rouault, T., and J. B. Harford. 2000. Translational control of ferritin synthesis, p. 655-670. In N. Sonenberg, J. W. B. Hershey, and M. B. Mathews (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, N.Y.
    • (2000) Translational Control of Gene Expression , pp. 655-670
    • Rouault, T.1    Harford, J.B.2
  • 26
    • 0031002851 scopus 로고    scopus 로고
    • The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites
    • Schalinske, K. L., S. A. Anderson, P. T. Tuazon, O. S. Chen, M. C. Kennedy, and R. S. Eisenstein. 1997. The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites. Biochemistry 36:3950-3958.
    • (1997) Biochemistry , vol.36 , pp. 3950-3958
    • Schalinske, K.L.1    Anderson, S.A.2    Tuazon, P.T.3    Chen, O.S.4    Kennedy, M.C.5    Eisenstein, R.S.6
  • 27
    • 0029914953 scopus 로고    scopus 로고
    • Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells
    • Schalinske, K. L., and R. S. Eisenstein. 1996. Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells. J. Biol. Chem. 271:7168-7176.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7168-7176
    • Schalinske, K.L.1    Eisenstein, R.S.2
  • 28
    • 0026483360 scopus 로고
    • Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation
    • Tang, C. K., J. Chin, J. B. Harford, R. D. Klausner, and T. A. Rouault. 1992. Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation. J. Biol. Chem. 267:24466-24470.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24466-24470
    • Tang, C.K.1    Chin, J.2    Harford, J.B.3    Klausner, R.D.4    Rouault, T.A.5
  • 29
    • 0036275236 scopus 로고    scopus 로고
    • Conditional depression of ferritin synthesis in cells expressing a constitutive IRP1 mutant
    • Wang, J., and K. Pantopoulos. 2002. Conditional depression of ferritin synthesis in cells expressing a constitutive IRP1 mutant. Mol. Cell. Biol. 22:4638-4651.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4638-4651
    • Wang, J.1    Pantopoulos, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.