메뉴 건너뛰기




Volumn 287, Issue 42, 2012, Pages 35104-35117

Neogenin interacts with matriptase-2 to facilitate hemojuvelin cleavage

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEINS; CELL SURFACES; DEGREE OF SPECIFICITY; DOWN-REGULATION; HEPATOCYTES; HEPCIDIN; IRON HOMEOSTASIS; MEMBRANE PROTEINS; MEMBRANE-BOUND; MULTIPLE FUNCTION; TERNARY COMPLEX; TRANS-MEMBRANE PROTEINS;

EID: 84867411483     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.363937     Document Type: Article
Times cited : (56)

References (53)
  • 1
    • 79551583056 scopus 로고    scopus 로고
    • Hepcidin and disorders of iron metabolism
    • Ganz, T., and Nemeth, E. (2011) Hepcidin and disorders of iron metabolism. Annu. Rev. Med. 62, 347-360
    • (2011) Annu. Rev. Med. , vol.62 , pp. 347-360
    • Ganz, T.1    Nemeth, E.2
  • 2
    • 37549059612 scopus 로고    scopus 로고
    • Regulation of iron acquisition and storage. Consequences for iron-linked disorders
    • De Domenico, I., McVey Ward, D., and Kaplan, J. (2008) Regulation of iron acquisition and storage. Consequences for iron-linked disorders. Nat. Rev. Mol. Cell Biol. 9, 72-81
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 72-81
    • De Domenico, I.1    McVey Ward, D.2    Kaplan, J.3
  • 4
    • 0037111732 scopus 로고    scopus 로고
    • Inappropriate expression of hepcidin is associated with iron refractory anemia: Implications for the anemia of chronic disease
    • DOI 10.1182/blood-2002-04-1260
    • Weinstein, D. A., Roy, C. N., Fleming, M. D., Loda, M. F., Wolfsdorf, J. I., and Andrews, N. C. (2002) Inappropriate expression of hepcidin is associated with iron refractory anemia. Implications for the anemia of chronic disease. Blood 100, 3776-3781 (Pubitemid 35303951)
    • (2002) Blood , vol.100 , Issue.10 , pp. 3776-3781
    • Weinstein, D.A.1    Roy, C.N.2    Fleming, M.D.3    Loda, M.F.4    Wolfsdorf, J.I.5    Andrews, N.C.6
  • 7
    • 26644471267 scopus 로고    scopus 로고
    • Interaction of hemojuvelin with neogenin results in iron accumulation in human embryonic kidney 293 cells
    • DOI 10.1074/jbc.M506207200
    • Zhang, A. S., West, A. P., Jr., Wyman, A. E., Bjorkman, P. J., and Enns, C. A. (2005) Interaction of hemojuvelin with neogenin results in iron accumulation in human embryonic kidney 293 cells. J. Biol. Chem. 280, 33885-33894 (Pubitemid 41443108)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 33885-33894
    • Zhang, A.-S.1    West Jr., A.P.2    Wyman, A.E.3    Bjorkman, P.J.4    Enns, C.A.5
  • 10
    • 23644444316 scopus 로고    scopus 로고
    • Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
    • DOI 10.1172/JCI25683
    • Niederkofler, V., Salie, R., and Arber, S. (2005) Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload. J. Clin. Invest. 115, 2180-2186 (Pubitemid 41134159)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.8 , pp. 2180-2186
    • Niederkofler, V.1    Salie, R.2    Arber, S.3
  • 12
    • 46749158788 scopus 로고    scopus 로고
    • Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin
    • Xia, Y., Babitt, J. L., Sidis, Y., Chung, R. T., and Lin, H. Y. (2008) Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin. Blood 111, 5195-5204
    • (2008) Blood , vol.111 , pp. 5195-5204
    • Xia, Y.1    Babitt, J.L.2    Sidis, Y.3    Chung, R.T.4    Lin, H.Y.5
  • 13
    • 77952747961 scopus 로고    scopus 로고
    • The role of hepatocyte hemojuvelin in the regulation of bone morphogenic protein-6 and hepcidin expression in vivo
    • Zhang, A. S., Gao, J., Koeberl, D. D., and Enns, C. A. (2010) The role of hepatocyte hemojuvelin in the regulation of bone morphogenic protein-6 and hepcidin expression in vivo. J. Biol. Chem. 285, 16416-16423
    • (2010) J. Biol. Chem. , vol.285 , pp. 16416-16423
    • Zhang, A.S.1    Gao, J.2    Koeberl, D.D.3    Enns, C.A.4
  • 14
    • 79959437085 scopus 로고    scopus 로고
    • Skeletal muscle hemojuvelin is dispensable for systemic iron homeostasis
    • Chen, W., Huang, F. W., de Renshaw, T. B., and Andrews, N. C. (2011) Skeletal muscle hemojuvelin is dispensable for systemic iron homeostasis. Blood 117, 6319-6325
    • (2011) Blood , vol.117 , pp. 6319-6325
    • Chen, W.1    Huang, F.W.2    De Renshaw, T.B.3    Andrews, N.C.4
  • 15
    • 80055055193 scopus 로고    scopus 로고
    • Conditional disruption of mouse HFE2 gene. Maintenance of systemic iron homeostasis requires hepatic but not skeletal muscle hemojuvelin
    • Gkouvatsos, K., Wagner, J., Papanikolaou, G., Sebastiani, G., and Pantopoulos, K. (2011) Conditional disruption of mouse HFE2 gene. Maintenance of systemic iron homeostasis requires hepatic but not skeletal muscle hemojuvelin. Hepatology 54, 1800-1807
    • (2011) Hepatology , vol.54 , pp. 1800-1807
    • Gkouvatsos, K.1    Wagner, J.2    Papanikolaou, G.3    Sebastiani, G.4    Pantopoulos, K.5
  • 16
    • 0037020169 scopus 로고    scopus 로고
    • Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins
    • Velasco, G., Cal, S., Quesada, V., Sánchez, L. M., and López-Otín, C. (2002) Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J. Biol. Chem. 277, 37637-37646
    • (2002) J. Biol. Chem. , vol.277 , pp. 37637-37646
    • Velasco, G.1    Cal, S.2    Quesada, V.3    Sánchez, L.M.4    López-Otín, C.5
  • 17
    • 79551629285 scopus 로고    scopus 로고
    • Suppression of hepatic hepcidin expression in response to acute iron deprivation is associated with an increase of matriptase-2 protein
    • Zhang, A. S., Anderson, S. A., Wang, J., Yang, F., DeMaster, K., Ahmed, R., Nizzi, C. P., Eisenstein, R. S., Tsukamoto, H., and Enns, C. A. (2011) Suppression of hepatic hepcidin expression in response to acute iron deprivation is associated with an increase of matriptase-2 protein. Blood 117, 1687-1699
    • (2011) Blood , vol.117 , pp. 1687-1699
    • Zhang, A.S.1    Anderson, S.A.2    Wang, J.3    Yang, F.4    DeMaster, K.5    Ahmed, R.6    Nizzi, C.P.7    Eisenstein, R.S.8    Tsukamoto, H.9    Enns, C.A.10
  • 20
    • 78649839347 scopus 로고    scopus 로고
    • Matriptase-2-and proprotein convertase-cleaved forms of hemojuvelin have different roles in the down-regulation of hepcidin expression
    • Maxson, J. E., Chen, J., Enns, C. A., and Zhang, A. S. (2010) Matriptase-2-and proprotein convertase-cleaved forms of hemojuvelin have different roles in the down-regulation of hepcidin expression. J. Biol. Chem. 285, 39021-39028
    • (2010) J. Biol. Chem. , vol.285 , pp. 39021-39028
    • Maxson, J.E.1    Chen, J.2    Enns, C.A.3    Zhang, A.S.4
  • 21
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., and Camaschella, C. (2008) The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab 8, 502-511
    • (2008) Cell Metab , vol.8 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De Domenico, I.4    Kaplan, J.5    Camaschella, C.6
  • 23
    • 70350482508 scopus 로고    scopus 로고
    • Suppression of the hepcidin-encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase-2/TMPRSS6
    • Truksa, J., Gelbart, T., Peng, H., Beutler, E., Beutler, B., and Lee, P. (2009) Suppression of the hepcidin-encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase-2/TMPRSS6. Br. J. Haematol. 147, 571-581
    • (2009) Br. J. Haematol. , vol.147 , pp. 571-581
    • Truksa, J.1    Gelbart, T.2    Peng, H.3    Beutler, E.4    Beutler, B.5    Lee, P.6
  • 24
    • 77952573858 scopus 로고    scopus 로고
    • Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis
    • Finberg, K. E., Whittlesey, R. L., Fleming, M. D., and Andrews, N. C. (2010) Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis. Blood 115, 3817-3826
    • (2010) Blood , vol.115 , pp. 3817-3826
    • Finberg, K.E.1    Whittlesey, R.L.2    Fleming, M.D.3    Andrews, N.C.4
  • 25
    • 36649027658 scopus 로고    scopus 로고
    • Soluble hemojuvelin is released by proprotein convertase-mediated cleavage at a conserved polybasic RNRR site
    • DOI 10.1016/j.bcmd.2007.06.023, PII S1079979607001428
    • Lin, L., Nemeth, E., Goodnough, J. B., Thapa, D. R., Gabayan, V., and Ganz, T. (2008) Soluble hemojuvelin is released by proprotein convertase-mediated cleavage at a conserved polybasic RNRR site. Blood Cells Mol Dis 40, 122-131 (Pubitemid 350193320)
    • (2008) Blood Cells, Molecules, and Diseases , vol.40 , Issue.1 , pp. 122-131
    • Lin, L.1    Nemeth, E.2    Goodnough, J.B.3    Thapa, D.R.4    Gabayan, V.5    Ganz, T.6
  • 26
    • 38349194098 scopus 로고    scopus 로고
    • Furin-mediated release of soluble hemojuvelin. A new link between hypoxia and iron homeostasis
    • Silvestri, L., Pagani, A., and Camaschella, C. (2008) Furin-mediated release of soluble hemojuvelin. A new link between hypoxia and iron homeostasis. Blood 111, 924-931
    • (2008) Blood , vol.111 , pp. 924-931
    • Silvestri, L.1    Pagani, A.2    Camaschella, C.3
  • 27
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge. From protein traffic to embryogenesis and disease
    • Thomas, G. (2002) Furin at the cutting edge. From protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3, 753-766
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 28
    • 34250308049 scopus 로고    scopus 로고
    • Evidence that inhibition of hemojuvelin shedding in response to iron is mediated through neogenin
    • DOI 10.1074/jbc.M608788200
    • Zhang, A. S., Anderson, S. A., Meyers, K. R., Hernandez, C., Eisenstein, R. S., and Enns, C. A. (2007) Evidence that inhibition of hemojuvelin shedding in response to iron is mediated through neogenin. J. Biol. Chem. 282, 12547-12556 (Pubitemid 47100643)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12547-12556
    • Zhang, A.-S.1    Anderson, S.A.2    Meyers, K.R.3    Hernandez, C.4    Eisenstein, R.S.5    Enns, C.A.6
  • 31
    • 0030981877 scopus 로고    scopus 로고
    • Identification and characterization of neogenin, a DCC-related gene
    • Meyerhardt, J. A., Look, A. T., Bigner, S. H., and Fearon, E. R. (1997) Identification and characterization of neogenin, a DCC-related gene. Oncogene 14, 1129-1136 (Pubitemid 27141914)
    • (1997) Oncogene , vol.14 , Issue.10 , pp. 1129-1136
    • Meyerhardt, J.A.1    Look, A.T.2    Bigner, S.H.3    Fearon, E.R.4
  • 33
    • 41949115757 scopus 로고    scopus 로고
    • Selective binding of RGMc/hemojuvelin, a key protein in systemic iron metabolism, to BMP-2 and neogenin
    • DOI 10.1152/ajpcell.00563.2007
    • Kuns-Hashimoto, R., Kuninger, D., Nili, M., and Rotwein, P. (2008) Selective binding of RGMc/hemojuvelin, a key protein in systemic iron metabolism, to BMP-2 and neogenin. Am. J. Physiol. Cell Physiol 294, C994-C1003 (Pubitemid 351507912)
    • (2008) American Journal of Physiology - Cell Physiology , vol.294 , Issue.4
    • Kuns-Hashimoto, R.1    Kuninger, D.2    Nili, M.3    Rotwein, P.4
  • 34
    • 41849096388 scopus 로고    scopus 로고
    • Neogenin interacts with hemojuvelin through its two membrane-proximal fibronectin type III domains
    • DOI 10.1021/bi800036h
    • Yang, F., West, A. P., Jr., Allendorph, G. P., Choe, S., and Bjorkman, P. J. (2008) Neogenin interacts with hemojuvelin through its two membrane-proximal fibronectin type III domains. Biochemistry 47, 4237-4245 (Pubitemid 351499880)
    • (2008) Biochemistry , vol.47 , Issue.14 , pp. 4237-4245
    • Yang, F.1    West Jr., A.P.2    Allendorph, G.P.3    Choe, S.4    Bjorkman, P.J.5
  • 35
    • 69249118614 scopus 로고    scopus 로고
    • Hemojuvelin-neogenin interaction is required for bone morphogenic protein-4-induced hepcidin expression
    • Zhang, A. S., Yang, F., Wang, J., Tsukamoto, H., and Enns, C. A. (2009) Hemojuvelin-neogenin interaction is required for bone morphogenic protein-4-induced hepcidin expression. J. Biol. Chem. 284, 22580-22589
    • (2009) J. Biol. Chem. , vol.284 , pp. 22580-22589
    • Zhang, A.S.1    Yang, F.2    Wang, J.3    Tsukamoto, H.4    Enns, C.A.5
  • 36
    • 61849129278 scopus 로고    scopus 로고
    • Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells
    • Maxson, J. E., Enns, C. A., and Zhang, A. S. (2009) Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells. Blood 113, 1786-1793
    • (2009) Blood , vol.113 , pp. 1786-1793
    • Maxson, J.E.1    Enns, C.A.2    Zhang, A.S.3
  • 37
    • 0842263988 scopus 로고    scopus 로고
    • Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes
    • DOI 10.1182/blood-2003-07-2378
    • Zhang, A. S., Xiong, S., Tsukamoto, H., and Enns, C. A. (2004) Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes. Blood 103, 1509-1514 (Pubitemid 38168670)
    • (2004) Blood , vol.103 , Issue.4 , pp. 1509-1514
    • Zhang, A.-S.1    Xiong, S.2    Tsukamoto, H.3    Enns, C.A.4
  • 39
    • 80052655782 scopus 로고    scopus 로고
    • The molecular pathogenesis of hereditary hemochromatosis
    • Babitt, J. L., and Lin, H. Y. (2011) The molecular pathogenesis of hereditary hemochromatosis. Semin Liver Dis. 31, 280-292
    • (2011) Semin Liver Dis. , vol.31 , pp. 280-292
    • Babitt, J.L.1    Lin, H.Y.2
  • 40
    • 33748797945 scopus 로고    scopus 로고
    • Complex biosynthesis of the muscle-enriched iron regulator RGMc
    • DOI 10.1242/jcs.03074
    • Kuninger, D., Kuns-Hashimoto, R., Kuzmickas, R., and Rotwein, P. (2006) Complex biosynthesis of the muscle-enriched iron regulator RGMc. J. Cell Sci. 119, 3273-3283 (Pubitemid 44405213)
    • (2006) Journal of Cell Science , vol.119 , Issue.16 , pp. 3273-3283
    • Kuninger, D.1    Kuns-Hashimoto, R.2    Kuzmickas, R.3    Rotwein, P.4
  • 41
    • 79960918043 scopus 로고    scopus 로고
    • TACE cleaves neogenin to desensitize cortical neurons to the repulsive guidance molecule
    • Okamura, Y., Kohmura, E., and Yamashita, T. (2011) TACE cleaves neogenin to desensitize cortical neurons to the repulsive guidance molecule. Neurosci. Res. 71, 63-70
    • (2011) Neurosci. Res. , vol.71 , pp. 63-70
    • Okamura, Y.1    Kohmura, E.2    Yamashita, T.3
  • 44
    • 77954894949 scopus 로고    scopus 로고
    • Neogenin regulation of BMP-induced canonical Smad signaling and endochondral bone formation
    • Zhou, Z., Xie, J., Lee, D., Liu, Y., Jung, J., Zhou, L., Xiong, S., Mei, L., and Xiong, W. C. (2010) Neogenin regulation of BMP-induced canonical Smad signaling and endochondral bone formation. Dev. Cell 19, 90-102
    • (2010) Dev. Cell , vol.19 , pp. 90-102
    • Zhou, Z.1    Xie, J.2    Lee, D.3    Liu, Y.4    Jung, J.5    Zhou, L.6    Xiong, S.7    Mei, L.8    Xiong, W.C.9
  • 45
    • 33646892646 scopus 로고    scopus 로고
    • Dynasore, a Cell-Permeable Inhibitor of Dynamin
    • DOI 10.1016/j.devcel.2006.04.002, PII S1534580706001638
    • Macia, E., Ehrlich, M., Massol, R., Boucrot, E., Brunner, C., and Kirchhausen, T. (2006) Dynasore, a cell-permeable inhibitor of dynamin. Dev. Cell 10, 839-850 (Pubitemid 43779110)
    • (2006) Developmental Cell , vol.10 , Issue.6 , pp. 839-850
    • Macia, E.1    Ehrlich, M.2    Massol, R.3    Boucrot, E.4    Brunner, C.5    Kirchhausen, T.6
  • 46
    • 80051694598 scopus 로고    scopus 로고
    • Essential role of endocytosis of the type II transmembrane serine protease TMPRSS6 in regulating its functionality
    • Béliveau, F., Brulé, C., Désilets, A., Zimmerman, B., Laporte, S. A., Lavoie, C. L., and Leduc, R. (2011) Essential role of endocytosis of the type II transmembrane serine protease TMPRSS6 in regulating its functionality. J. Biol. Chem. 286, 29035-29043
    • (2011) J. Biol. Chem. , vol.286 , pp. 29035-29043
    • Béliveau, F.1    Brulé, C.2    Désilets, A.3    Zimmerman, B.4    Laporte, S.A.5    Lavoie, C.L.6    Leduc, R.7
  • 47
    • 1842715573 scopus 로고    scopus 로고
    • The Netrin receptor Neogenin is required for neural tube formation and somitogenesis in zebrafish
    • DOI 10.1016/j.ydbio.2004.02.001, PII S0012160604000946
    • Mawdsley, D. J., Cooper, H. M., Hogan, B. M., Cody, S. H., Lieschke, G. J., and Heath, J. K. (2004) The Netrin receptor neogenin is required for neural tube formation and somitogenesis in zebrafish. Dev. Biol. 269, 302-315 (Pubitemid 38471841)
    • (2004) Developmental Biology , vol.269 , Issue.1 , pp. 302-315
    • Mawdsley, D.J.1    Cooper, H.M.2    Hogan, B.M.3    Cody, S.H.4    Lieschke, G.J.5    Heath, J.K.6
  • 48
    • 0037345836 scopus 로고    scopus 로고
    • Netrin-1/neogenin interaction stabilizes multipotent progenitor cap cells during mammary gland morphogenesis
    • DOI 10.1016/S1534-5807(03)00054-6, PII S1534580703000546
    • Srinivasan, K., Strickland, P., Valdes, A., Shin, G. C., and Hinck, L. (2003) Netrin-1/neogenin interaction stabilizes multipotent progenitor cap cells during mammary gland morphogenesis. Dev. Cell 4, 371-382 (Pubitemid 36342362)
    • (2003) Developmental Cell , vol.4 , Issue.3 , pp. 371-382
    • Srinivasan, K.1    Strickland, P.2    Valdes, A.3    Shin, G.C.4    Hinck, L.5
  • 50
    • 79953149131 scopus 로고    scopus 로고
    • Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation
    • Hagihara, M., Endo, M., Hata, K., Higuchi, C., Takaoka, K., Yoshikawa, H., and Yamashita, T. (2011) Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation. J. Biol. Chem. 286, 5157-5165
    • (2011) J. Biol. Chem. , vol.286 , pp. 5157-5165
    • Hagihara, M.1    Endo, M.2    Hata, K.3    Higuchi, C.4    Takaoka, K.5    Yoshikawa, H.6    Yamashita, T.7
  • 51
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and γ-secretases in cell biology and disease
    • De Strooper, B., and Annaert, W. (2010) Novel research horizons for presenilins and γ-secretases in cell biology and disease. Annu. Rev. Cell Dev. Biol. 26, 235-260
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 235-260
    • De Strooper, B.1    Annaert, W.2
  • 52
    • 72249094196 scopus 로고    scopus 로고
    • Metabolism, cell surface organization, and disease
    • Dennis, J. W., Nabi, I. R., and Demetriou, M. (2009) Metabolism, cell surface organization, and disease. Cell 139, 1229-1241
    • (2009) Cell , vol.139 , pp. 1229-1241
    • Dennis, J.W.1    Nabi, I.R.2    Demetriou, M.3
  • 53
    • 73949157930 scopus 로고    scopus 로고
    • Neogenin regulates skeletal myofiber size and focal adhesion kinase and extracellular signal-regulated kinase activities in vivo and in vitro
    • Bae, G. U., Yang, Y. J., Jiang, G., Hong, M., Lee, H. J., Tessier-Lavigne, M., Kang, J. S., and Krauss, R. S. (2009) Neogenin regulates skeletal myofiber size and focal adhesion kinase and extracellular signal-regulated kinase activities in vivo and in vitro. Mol. Biol. Cell 20, 4920-4931
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4920-4931
    • Bae, G.U.1    Yang, Y.J.2    Jiang, G.3    Hong, M.4    Lee, H.J.5    Tessier-Lavigne, M.6    Kang, J.S.7    Krauss, R.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.