Coming into view: Eukaryotic iron chaperones and intracellular iron delivery

Journal of Biological Chemistry

Volumn 287, Issue 17, 2012, Pages 13518-13523

  Philpott, Caroline C ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEINS; CELLULAR MACHINERY; CRITICAL TASKS; CYTOSOLIC; CYTOSOLIC COMPARTMENTS; EUKARYOTIC CELLS; INTRACELLULAR IRON; IRON-SULFUR CLUSTERS; MAMMALIAN CELLS; METALLATION; METALLO-PROTEINS; MONOTHIOL; NON-HEME IRON ENZYMES; PROTEIN-PROTEIN INTERACTIONS; YEAST CELL;

ENZYMES; MACHINERY; METAL IONS; PORPHYRINS; PROTEINS; SULFUR;

IRON;

BINDING PROTEIN; FERRITIN; FRATAXIN; GLUTAREDOXIN; METALLOCHAPERONE; MONOTHIOL GLUTAREDOXIN; POLY(RC) BINDING PROTEIN 1; POLY(RC) BINDING PROTEIN 2; UNCLASSIFIED DRUG;

BINDING AFFINITY; HUMAN; INTRACELLULAR TRANSPORT; IRON TRANSPORT; METALLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SHORT SURVEY;

ANIMALS; BIOLOGICAL TRANSPORT; CYTOSOL; ENZYMES; GLUTAREDOXINS; HEME; HUMANS; IRON; IRON-BINDING PROTEINS; IRON-SULFUR PROTEINS; METALLOPROTEINS; METALS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; SULFHYDRYL COMPOUNDS;

EID: 84859956110     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R111.326876     Document Type: Short Survey

References (47)

1. Waldron, K. J., Rutherford, J. C., Ford, D., and Robinson, N. J. (2009) Metalloproteins and metal sensing. Nature 460, 823-830
2. Cvetkovic, A., Menon, A. L., Thorgersen, M. P., Scott, J. W., Poole, F. L., 2nd, Jenney, F. E., Jr., Lancaster, W. A., Praissman, J. L., Shanmukh, S., Vaccaro, B. J., Trauger, S. A., Kalisiak, E., Apon, J. V., Siuzdak, G., Yannone, S. M., Tainer, J. A., and Adams, M. W. (2010) Microbial metalloproteomes are largely uncharacterized. Nature 466, 779-782
3. Andreini, C., Bertini, I., Cavallaro, G., Holliday, G. L., and Thornton, J. M. (2008) Metal ions in biological catalysis: from enzyme databases to general principles. J. Biol. Inorg. Chem. 13, 1205-1218
4. Andreini, C., Bertini, I., and Rosato, A. (2009) Metalloproteomes: a bioinformatic approach. Acc. Chem. Res. 42, 1471-1479
5. Outten, C. E., and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292, 2488-2492 (Pubitemid 32605687)
6. Rosenzweig, A. C. (2002) Metallochaperones: bind and deliver. Chem. Biol. 9, 673-677
7. Pandolfo, M. (2009) Friedreich ataxia: the clinical picture. J. Neurol. 256, Suppl. 1, 3-8
8. Stemmler, T. L., Lesuisse, E., Pain, D., and Dancis, A. (2010) Frataxin and mitochondrial Fe-S cluster biogenesis. J. Biol. Chem. 285, 26737-26743
9. Sharma, A. K., Pallesen, L. J., Spang, R. J., and Walden, W. E. (2010) Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation. J. Biol. Chem. 285, 26745-26751
10. Bulteau, A. L., O'Neill, H. A., Kennedy, M. C., Ikeda-Saito, M., Isaya, G., and Szweda, L. I. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305, 242-245 (Pubitemid 38886737)
11. Tsai, C. L., and Barondeau, D. P. (2010) Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex. Biochemistry 49, 9132-9139
12. Tsai, C. L., Bridwell-Rabb, J., and Barondeau, D. P. (2011) Friedreich ataxia variants I154F and W155R diminish frataxin-based activation of the ironsulfur cluster assembly complex. Biochemistry 50, 6478-6487
13. Yoon, H., Golla, R., Lesuisse, E., Pain, J., Donald, J., Lyver, E. R., Pain, D., and Dancis, A. (2012) Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion. Biochem. J. 441, 473-480
14. Pohl, T., Walter, J., Stolpe, S., Soufo, J. H., Grauman, P. L., and Friedrich, T. (2007) Effects of the deletion of the Escherichia coli frataxin homolog CyaY on the respiratory NADH:ubiquinone oxidoreductase. BMC Biochem. 8, 13
15. Shi, H., Bencze, K. Z., Stemmler, T. L., and Philpott, C. C. (2008) A cytosolic iron chaperone that delivers iron to ferritin. Science 320, 1207-1210 (Pubitemid 351929507)
16. Hintze, K. J., and Theil, E. C. (2006) Cellular regulation and molecular interactions of the ferritins. Cell. Mol. Life Sci. 63, 591-600
17. Chaudhury, A., Chander, P., and Howe, P. H. (2010) Heterogeneous nuclear ribonucleoproteins (hnRNPs) in cellular processes: focus on hnRNP E1's multifunctional regulatory roles. RNA 16, 1449-1462
18. Makeyev, A. V., and Liebhaber, S. A. (2002) The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms. RNA 8, 265-278 (Pubitemid 34311177)
19. Ostareck-Lederer, A., and Ostareck, D. H. (2004) Control ofmRNAtranslation and stability in hematopoietic cells: the function of hnRNPs K and E1/E2. Biol. Cell 96, 407-411 (Pubitemid 39157944)
20. Nandal, A., Ruiz, J. C., Subramanian, P., Ghimire-Rijal, S., Sinnamon, R. A., Stemmler, T. L., Bruick, R. K., and Philpott, C. C. (2011) Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2. Cell Metab. 14, 647-657
21. Kaelin, W. G., Jr., and Ratcliffe, P. J. (2008) Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol. Cell 30, 393-402
22. Loenarz, C., and Schofield, C. J. (2008) Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 4, 152-156 (Pubitemid 351264133)
23. Ozer, A., and Bruick, R. K. (2007) Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nat. Chem. Biol. 3, 144-153
24. Bruick, R. K., and McKnight, S. L. (2001) A conserved family of prolyl 4-hydroxylases that modify HIF. Science 294, 1337-1340 (Pubitemid 33063099)
25. Epstein, A. C., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., Tian, Y. M., Masson, N., Hamilton, D. L., Jaakkola, P., Barstead, R., Hodgkin, J., Maxwell, P. H., Pugh, C. W., Schofield, C. J., and Ratcliffe, P. J. (2001) C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54
26. Berra, E., Benizri, E., Ginouvès, A., Volmat, V., Roux, D., and Pouysségur, J. (2003) HIF prolyl hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF1α in normoxia. EMBO J. 22, 4082-4090 (Pubitemid 37021737)
27. Hewitson, K. S., McNeill, L. A., Riordan, M. V., Tian, Y. M., Bullock, A. N., Welford, R. W., Elkins, J. M., Oldham, N. J., Bhattacharya, S., Gleadle, J. M., Ratcliffe, P. J., Pugh, C. W., and Schofield, C. J. (2002) Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J. Biol. Chem. 277, 26351-26355 (Pubitemid 34967127)
28. Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., and Bruick, R. K. (2002) FIH1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16, 1466-1471 (Pubitemid 34686328)
29. Lando, D., Peet, D. J., Whelan, D. A., Gorman, J. J., and Whitelaw, M. L. (2002) Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 295, 858-861 (Pubitemid 34118367)
30. Rouhier, N., Couturier, J., Johnson, M. K., and Jacquot, J. P. (2010) Glutaredoxins: roles in iron homeostasis. Trends Biochem. Sci. 35, 43-52
31. Ojeda, L., Keller, G., Muhlenhoff, U., Rutherford, J. C., Lill, R., and Winge, D. R. (2006) Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. J. Biol. Chem. 281, 17661-17669 (Pubitemid 44035564)
32. Pujol-Carrion, N., Belli, G., Herrero, E., Nogues, A., and de la Torre-Ruiz, M. A. (2006) Glutaredoxins Grx3 and Grx4 regulate nuclear localization of Aft1 and the oxidative stress response in Saccharomyces cerevisiae. J. Cell Sci. 119, 4554-4564
33. Rodríguez-Manzaneque, M. T., Ros, J., Cabiscol, E., Sorribas, A., and Herrero, E. (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 19, 8180-8190 (Pubitemid 30414012)
34. Haunhorst, P., Berndt, C., Eitner, S., Godoy, J. R., and Lillig, C. H. (2010) Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein. Biochem. Biophys. Res. Commun. 394, 372-376
35. Li, H., Mapolelo, D. T., Dingra, N. N., Naik, S. G., Lees, N. S., Hoffman, B. M., Riggs-Gelasco, P. J., Huynh, B. H., Johnson, M. K., and Outten, C. E. (2009) The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation. Biochemistry 48, 9569-9581
36. Kumánovics, A., Chen, O. S., Li, L., Bagley, D., Adkins, E. M., Lin, H., Dingra, N. N., Outten, C. E., Keller, G., Winge, D., Ward, D. M., and Kaplan, J. (2008) Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis. J. Biol. Chem. 283, 10276-10286
37. Philpott, C. C., and Protchenko, O. (2008) Response to iron deprivation in Saccharomyces cerevisiae. Eukaryot. Cell 7, 20-27 (Pubitemid 351959590)
38. Mühlenhoff, U., Molik, S., Godoy, J. R., Uzarska, M. A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., Lillig, C. H., and Lill, R. (2010) Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster. Cell Metab. 12, 373-385
39. Jbel, M., Mercier, A., and Labbé, S. (2011) Grx4 monothiol glutaredoxin is required for iron limitation-dependent inhibition of Fep1. Eukaryot. Cell 10, 629-645
40. Mercier, A., and Labbé, S. (2009) Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1. J. Biol. Chem. 284, 20249-20262
41. Denisenko, O., and Bomsztyk, K. (2002) Yeast hnRNP K-like genes are involved in regulation of the telomeric position effect and telomere length. Mol. Cell. Biol. 22, 286-297 (Pubitemid 33144275)
42. Irie, K., Tadauchi, T., Takizawa, P. A., Vale, R. D., Matsumoto, K., and Herskowitz, I. (2002) The Khd1 protein, which has three KH RNA-binding motifs, is required for proper localization of ASH1 mRNA in yeast. EMBO J. 21, 1158-1167 (Pubitemid 34206189)
43. Mangus, D. A., Amrani, N., and Jacobson, A. (1998) Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mol. Cell. Biol. 18, 7383-7396 (Pubitemid 28533058)
44. Kasai, T., Inoue, M., Koshiba, S., Yabuki, T., Aoki, M., Nunokawa, E., Seki, E., Matsuda, T., Matsuda, N., Tomo, Y., Shirouzu, M., Terada, T., Obayashi, N., Hamana, H., Shinya, N., Tatsuguchi, A., Yasuda, S., Yoshida, M., Hirota, H., Matsuo, Y., Tani, K., Suzuki, H., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kigawa, T., and Yokoyama, S. (2004) Solution structure of a BolA-like protein from Mus musculus. Protein Sci. 13, 545-548 (Pubitemid 38124975)
45. Conlan, A. R., Axelrod, H. L., Cohen, A. E., Abresch, E. C., Zuris, J., Yee, D., Nechushtai, R., Jennings, P. A., and Paddock, M. L. (2009) Crystal structure of Miner1: the redox-active 2Fe-2S protein causative in Wolfram syndrome 2. J. Mol. Biol. 392, 143-153
46. Zuris, J. A., Harir, Y., Conlan, A. R., Shvartsman, M., Michaeli, D., Tamir, S., Paddock, M. L., Onuchic, J. N., Mittler, R., Cabantchik, Z. I., Jennings, P. A., and Nechushtai, R. (2011) Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein. Proc. Natl. Acad. Sci. U.S.A. 108, 13047-13052
47. Amr, S., Heisey, C., Zhang, M., Xia, X. J., Shows, K. H., Ajlouni, K., Pandya, A., Satin, L. S., El-Shanti, H., and Shiang, R. (2007) A homozygous mutation in a novel zinc-finger protein, ERIS, is responsible for Wolfram syndrome 2. Am. J. Hum. Genet. 81, 673-683 (Pubitemid 47596537)