메뉴 건너뛰기




Volumn 1 AUG, Issue , 2010, Pages

Identification of zebrafish Fxyd11a protein that is highly expressed in ion-transporting epithelium of the gill and skin and its possible role in ion homeostasis

Author keywords

Calcium; Danio renio; FXYD domain ion transport regulator; Mitochondria rich cell; Na + K + ATPase; Osmoregulation; Salinity; Teleost

Indexed keywords


EID: 79955540150     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2010.00129     Document Type: Article
Times cited : (33)

References (66)
  • 3
    • 70349694752 scopus 로고    scopus 로고
    • The involvement of SLC26 anion transporters in chloride uptake in zebrafish (Danio rerio) larvae
    • Bayaa, M., Vulesevic, B., Esbaugh, A., Braun, M., Ekker, M. E., Grosell, M., and Perry, S. F. (2009). The involvement of SLC26 anion transporters in chloride uptake in zebrafish (Danio rerio) larvae. J. Exp. Biol. 212, 3283-3295.
    • (2009) J. Exp. Biol , vol.212 , pp. 3283-3295
    • Bayaa, M.1    Vulesevic, B.2    Esbaugh, A.3    Braun, M.4    Ekker, M.E.5    Grosell, M.6    Perry, S.F.7
  • 4
    • 0035421235 scopus 로고    scopus 로고
    • CHIF, a member of the FXYD protein family, is a regulator of Na,K-ATPase distinct from the gamma-subunit
    • Béguin, P., Crambert, G., Guennoun, S., Garty, H., Horisberger, J. D., and Geering, K. (2001). CHIF, a member of the FXYD protein family, is a regulator of Na,K-ATPase distinct from the gamma-subunit. EMBO J. 20, 3993-4002.
    • (2001) EMBO J , vol.20 , pp. 3993-4002
    • Béguin, P.1    Crambert, G.2    Guennoun, S.3    Garty, H.4    Horisberger, J.D.5    Geering, K.6
  • 6
    • 0039438642 scopus 로고    scopus 로고
    • The gamma subunit is a specific component of the Na,K-ATPase and modulates its transport function
    • Béguin, P., Wang, X., Firsov, D., Puoti, A., Claeys, D., Horisberger, J. D., and Geering, K. (1997). The gamma subunit is a specific component of the Na,K-ATPase and modulates its transport function. EMBO J. 16, 4250-4260.
    • (1997) EMBO J , vol.16 , pp. 4250-4260
    • Béguin, P.1    Wang, X.2    Firsov, D.3    Puoti, A.4    Claeys, D.5    Horisberger, J.D.6    Geering, K.7
  • 7
    • 33846028572 scopus 로고    scopus 로고
    • Structural and functional properties of two human FXYD3 (Mat-8) isoforms
    • Bibert, S., Roy, S., Schaer, D., Felley-Bosco, E., and Geering, K. (2006). Structural and functional properties of two human FXYD3 (Mat-8) isoforms. J. Biol. Chem. 281, 39142-39151.
    • (2006) J. Biol. Chem , vol.281 , pp. 39142-39151
    • Bibert, S.1    Roy, S.2    Schaer, D.3    Felley-Bosco, E.4    Geering, K.5
  • 8
    • 34447253806 scopus 로고    scopus 로고
    • Gill membrane remodeling with soft-water acclimation in zebrafish (Danio rerio)
    • Craig, P. M., Wood, C. M., and McClelland, G. B. (2007). Gill membrane remodeling with soft-water acclimation in zebrafish (Danio rerio). Physiol. Genomics 30, 53-60.
    • (2007) Physiol. Genomics , vol.30 , pp. 53-60
    • Craig, P.M.1    Wood, C.M.2    McClelland, G.B.3
  • 9
    • 0037143722 scopus 로고    scopus 로고
    • Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties
    • Crambert, G., Fuzesi, M., Garty, H., Karlish, S., and Geering, K. (2002). Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties. Proc. Natl. Acad. Sci. U.S.A. 99, 11476-11481.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11476-11481
    • Crambert, G.1    Fuzesi, M.2    Garty, H.3    Karlish, S.4    Geering, K.5
  • 10
    • 18244401341 scopus 로고    scopus 로고
    • FXYD3 (Mat-8), a new regulator of Na,K-ATPase
    • Crambert, G., Li, C., Claeys, D., and Geering, K. (2005). FXYD3 (Mat-8), a new regulator of Na,K-ATPase. Mol. Biol. Cell 16, 2363-2371.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2363-2371
    • Crambert, G.1    Li, C.2    Claeys, D.3    Geering, K.4
  • 11
    • 34147191990 scopus 로고    scopus 로고
    • FXYD6 is a novel regulator of Na,K- ATPase expressed in the inner ear
    • Delprat, B., Schaer, D., Roy, S., Wang, J., Puel, J. L., and Geering, K. (2007). FXYD6 is a novel regulator of Na,K- ATPase expressed in the inner ear. J. Biol. Chem. 282, 7450-7456.
    • (2007) J. Biol. Chem , vol.282 , pp. 7450-7456
    • Delprat, B.1    Schaer, D.2    Roy, S.3    Wang, J.4    Puel, J.L.5    Geering, K.6
  • 14
    • 12944265303 scopus 로고    scopus 로고
    • The multifunctional fish gill: dominant site of gas exchange, osmoregulation, acid-base regulation, and excretion of nitrogenous waste
    • Evans, D. H., Piermarini, P. M., and Choe, K. P. (2005). The multifunctional fish gill: dominant site of gas exchange, osmoregulation, acid-base regulation, and excretion of nitrogenous waste. Physiol. Rev. 85, 97-177.
    • (2005) Physiol. Rev , vol.85 , pp. 97-177
    • Evans, D.H.1    Piermarini, P.M.2    Choe, K.P.3
  • 15
    • 0035133295 scopus 로고    scopus 로고
    • Sodium-potassium-adenosinetriphosphatase-dependent sodium transport in the kidney: hormonal control
    • Feraille, E., and Doucet, A. (2001). Sodium-potassium-adenosinetriphosphatase-dependent sodium transport in the kidney: hormonal control. Physiol. Rev. 81, 345-418.
    • (2001) Physiol. Rev , vol.81 , pp. 345-418
    • Feraille, E.1    Doucet, A.2
  • 17
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of beta subunits in oligomeric P-type ATPases
    • Geering, K. (2001). The functional role of beta subunits in oligomeric P-type ATPases. J. Bioenerg. Biomembr. 33, 425-438.
    • (2001) J. Bioenerg. Biomembr , vol.33 , pp. 425-438
    • Geering, K.1
  • 18
    • 33644870868 scopus 로고    scopus 로고
    • FXYD proteins: new regulators of Na-K-ATPase
    • Geering, K. (2006). FXYD proteins: new regulators of Na-K-ATPase. Am. J. Physiol. Renal. Physiol. 290, F241-F250.
    • (2006) Am. J. Physiol. Renal. Physiol , vol.290
    • Geering, K.1
  • 22
  • 25
    • 34447105988 scopus 로고    scopus 로고
    • Expression of endocrine genes in zebrafish larvae in response to environmental salinity
    • Hoshijima, K., and Hirose, S. (2007). Expression of endocrine genes in zebrafish larvae in response to environmental salinity. J. Endocrinol. 193, 481-491.
    • (2007) J. Endocrinol , vol.193 , pp. 481-491
    • Hoshijima, K.1    Hirose, S.2
  • 26
    • 34347259725 scopus 로고    scopus 로고
    • A positive regulatory loop between foxi3a and foxi3b is essential for specification and differentiation of zebrafish epidermal ionocytes
    • doi: 10.1371/journal. pone.0000302.
    • Hsiao, C. D., You, M. S., Guh, Y. J., Ma, M., Jiang, Y. J., and Hwang, P. P. (2007). A positive regulatory loop between foxi3a and foxi3b is essential for specification and differentiation of zebrafish epidermal ionocytes. PLoS ONE 2, e302. doi: 10.1371/journal. pone.0000302.
    • (2007) PLoS ONE , vol.2
    • Hsiao, C.D.1    You, M.S.2    Guh, Y.J.3    Ma, M.4    Jiang, Y.J.5    Hwang, P.P.6
  • 27
    • 66449134820 scopus 로고    scopus 로고
    • Ion uptake and acid secretion in zebrafish (Danio rerio)
    • Hwang, P. P. (2009). Ion uptake and acid secretion in zebrafish (Danio rerio). J. Exp. Biol. 212, 1745-1752.
    • (2009) J. Exp. Biol , vol.212 , pp. 1745-1752
    • Hwang, P.P.1
  • 28
    • 34347247326 scopus 로고    scopus 로고
    • Foxi3 transcription factors and Notch signaling control the formation of skin ionocytes from epidermal precursors of the zebrafish embryo
    • Jänicke, M., Carney, T. J., and Hammerschmidt, M. (2007). Foxi3 transcription factors and Notch signaling control the formation of skin ionocytes from epidermal precursors of the zebrafish embryo. Dev. Biol. 307, 258-271.
    • (2007) Dev. Biol , vol.307 , pp. 258-271
    • Jänicke, M.1    Carney, T.J.2    Hammerschmidt, M.3
  • 31
    • 2342628035 scopus 로고    scopus 로고
    • The mechanism of sodium chloride uptake in hyper-regulating aquatic animals
    • Kirschner, L. B. (2004). The mechanism of sodium chloride uptake in hyper-regulating aquatic animals. J. Exp. Biol. 207, 1439-1452.
    • (2004) J. Exp. Biol , vol.207 , pp. 1439-1452
    • Kirschner, L.B.1
  • 32
    • 33646415381 scopus 로고    scopus 로고
    • Cytoplasmic targeting signals mediate delivery of phospholemman to the plasma membrane
    • Lansbery, K. L., Burcea, L. C., Mendenhall, M. L., and Mercer, R. W. (2006). Cytoplasmic targeting signals mediate delivery of phospholemman to the plasma membrane. Am. J. Physiol. Cell Physiol. 290, C1275-R1286.
    • (2006) Am. J. Physiol. Cell Physiol , vol.290
    • Lansbery, K.L.1    Burcea, L.C.2    Mendenhall, M.L.3    Mercer, R.W.4
  • 34
    • 37249067492 scopus 로고    scopus 로고
    • Expression and water calcium dependence of calcium transporter isoforms in zebrafish gill mitochondrion-rich cells
    • doi: 10.1186/1471-2164-8-354
    • Liao, B. K., Deng, A. N., Chen, S. C., Chou, M. Y., and Hwang, P. P. (2007). Expression and water calcium dependence of calcium transporter isoforms in zebrafish gill mitochondrion-rich cells. BMC Genomics 8, 354. doi: 10.1186/1471-2164-8-354.
    • (2007) BMC Genomics , vol.8 , pp. 354
    • Liao, B.K.1    Deng, A.N.2    Chen, S.C.3    Chou, M.Y.4    Hwang, P.P.5
  • 37
    • 0141844566 scopus 로고    scopus 로고
    • Regulation of Na,K-ATPase by PLMS, the phospholemman-like protein from shark: molecular cloning, sequence, expression, cellular distribution, and functional effects of PLMS
    • Mahmmoud, Y. A., Cramb, G., Maunsbach, A. B., Cutler, C. P., Meischke, L., and Cornelius, F. (2003). Regulation of Na,K-ATPase by PLMS, the phospholemman-like protein from shark: molecular cloning, sequence, expression, cellular distribution, and functional effects of PLMS. J. Biol. Chem. 278, 37427-37438.
    • (2003) J. Biol. Chem , vol.278 , pp. 37427-37438
    • Mahmmoud, Y.A.1    Cramb, G.2    Maunsbach, A.B.3    Cutler, C.P.4    Meischke, L.5    Cornelius, F.6
  • 38
    • 0034680861 scopus 로고    scopus 로고
    • Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na,K-ATPase by protein kinase c via a novel member of the FXYDY family
    • Mahmmoud, Y. A., Vorum, H., and Cornelius, F. (2000). Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na,K-ATPase by protein kinase c via a novel member of the FXYDY family. J. Biol. Chem. 275, 35969-35977.
    • (2000) J. Biol. Chem , vol.275 , pp. 35969-35977
    • Mahmmoud, Y.A.1    Vorum, H.2    Cornelius, F.3
  • 39
    • 0036667258 scopus 로고    scopus 로고
    • 2+ transport by fish gills: retrospective review and prospective synthesis
    • 2+ transport by fish gills: retrospective review and prospective synthesis. J. Exp. Zool. 293, 264-283.
    • (2002) J. Exp. Zool , vol.293 , pp. 264-283
    • Marshall, W.S.1
  • 40
    • 0025372071 scopus 로고
    • +-ATPase in intact cells by use of a fluorescent derivative of ouabain: salinity and teleost chloride cells
    • +-ATPase in intact cells by use of a fluorescent derivative of ouabain: salinity and teleost chloride cells. Cell Tissue Res. 260, 529-533.
    • (1990) Cell Tissue Res , vol.260 , pp. 529-533
    • McCormick, S.D.1
  • 43
    • 0036453682 scopus 로고    scopus 로고
    • RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica
    • Miyamoto, K., Nakamura, N., Kashiwagi, M., Honda, S., Kato, A., Hasegawa, S., Takei, Y., and Hirose, S. (2002). RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica. Eur. J. Biochem. 269, 6152-6161.
    • (2002) Eur. J. Biochem , vol.269 , pp. 6152-6161
    • Miyamoto, K.1    Nakamura, N.2    Kashiwagi, M.3    Honda, S.4    Kato, A.5    Hasegawa, S.6    Takei, Y.7    Hirose, S.8
  • 44
    • 35148870132 scopus 로고    scopus 로고
    • Localization of ammonia transporter Rhcg1 in mitochondrion-rich cells of yolk sac, gill, and kidney of zebrafish and its ionic strength-dependent expression
    • Nakada, T., Hoshijima, K., Esaki, M., Nagayoshi, S., Kawakami, K., and Hirose, S. (2007). Localization of ammonia transporter Rhcg1 in mitochondrion-rich cells of yolk sac, gill, and kidney of zebrafish and its ionic strength-dependent expression. Am. J. Physiol. Regul. Integr. Comp. Physiol. 293, R1743-R1753.
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.293
    • Nakada, T.1    Hoshijima, K.2    Esaki, M.3    Nagayoshi, S.4    Kawakami, K.5    Hirose, S.6
  • 45
    • 16344381891 scopus 로고    scopus 로고
    • MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking
    • Nakamura, N., Fukuda, H., Kato, A., and Hirose, S. (2005). MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol. Biol. Cell 16, 1696-1710.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1696-1710
    • Nakamura, N.1    Fukuda, H.2    Kato, A.3    Hirose, S.4
  • 46
    • 48249124967 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane
    • Nakamura, N., and Hirose, S. (2008). Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane. Mol. Biol. Cell 19, 1903-1911.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1903-1911
    • Nakamura, N.1    Hirose, S.2
  • 49
    • 0346264748 scopus 로고    scopus 로고
    • Channels, pumps, and exchangers in the gill and kidney of freshwater fishes: their role in ionic and acid-base regulation
    • Perry, S. F., Shahsavarani, A., Georgalis, T., Bayaa, M., Furimsky, M., and Thomas, S. L. (2003). Channels, pumps, and exchangers in the gill and kidney of freshwater fishes: their role in ionic and acid-base regulation. J. Exp. Zool. A Comp. Exp. Biol. 300, 53-62.
    • (2003) J. Exp. Zool. A Comp. Exp. Biol , vol.300 , pp. 53-62
    • Perry, S.F.1    Shahsavarani, A.2    Georgalis, T.3    Bayaa, M.4    Furimsky, M.5    Thomas, S.L.6
  • 50
    • 70349630424 scopus 로고    scopus 로고
    • Evidence that SLC26 anion transporters mediate branchial chloride uptake in adult zebrafish (Danio rerio)
    • Perry, S. F., Vulesevic, B., Grosell, M., and Bayaa, M. (2009). Evidence that SLC26 anion transporters mediate branchial chloride uptake in adult zebrafish (Danio rerio). Am. J. Physiol. Regul. Integr. Comp. Physiol. 297, R988-R997.
    • (2009) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.297
    • Perry, S.F.1    Vulesevic, B.2    Grosell, M.3    Bayaa, M.4
  • 51
    • 0035827529 scopus 로고    scopus 로고
    • Functional role and immunocytochemical localization of the γa and γb forms of the Na,K-ATPase γ subunit
    • Pu, H. X., Cluzeaud, F., Goldshleger, R., Karlish, S. J., Farman, N., and Blostein, R. (2001). Functional role and immunocytochemical localization of the γa and γb forms of the Na,K-ATPase γ subunit. J. Biol. Chem. 276, 20370-20378.
    • (2001) J. Biol. Chem , vol.276 , pp. 20370-20378
    • Pu, H.X.1    Cluzeaud, F.2    Goldshleger, R.3    Karlish, S.J.4    Farman, N.5    Blostein, R.6
  • 52
    • 0037036441 scopus 로고    scopus 로고
    • Distinct regulatory effects of the Na,K-ATPase γ subunit
    • Pu, H. X., Scanzano, R., and Blostein, R. (2002). Distinct regulatory effects of the Na,K-ATPase γ subunit. J. Biol. Chem. 277, 20270-20276.
    • (2002) J. Biol. Chem , vol.277 , pp. 20270-20276
    • Pu, H.X.1    Scanzano, R.2    Blostein, R.3
  • 53
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 Å resolution
    • Shinoda, T., Ogawa, H., Cornelius, F., and Toyoshima, C. (2009). Crystal structure of the sodium-potassium pump at 2.4 Å resolution. Nature 459, 446-450.
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 54
    • 48049110299 scopus 로고    scopus 로고
    • Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay
    • Söderberg, O., Leuchowius, K. J., Gullberg, M., Jarvius, M., Weibrecht, I., Larsson, L. G., and Landegren, U. (2008). Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay. Methods 45, 227-232.
    • (2008) Methods , vol.45 , pp. 227-232
    • Söderberg, O.1    Leuchowius, K.J.2    Gullberg, M.3    Jarvius, M.4    Weibrecht, I.5    Larsson, L.G.6    Landegren, U.7
  • 55
    • 0034662757 scopus 로고    scopus 로고
    • The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression
    • Sweadner, K. J., and Rael, E. (2000). The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression. Genomics 68, 41-56.
    • (2000) Genomics , vol.68 , pp. 41-56
    • Sweadner, K.J.1    Rael, E.2
  • 57
    • 41749125690 scopus 로고    scopus 로고
    • Identification of FXYD protein genes in a teleost: tissue-specific expression and response to salinity change
    • Tipsmark, C. K. (2008). Identification of FXYD protein genes in a teleost: tissue-specific expression and response to salinity change. Am. J. Physiol. Regul. Integr. Comp. Physiol. 294, R1367-R1378.
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.294
    • Tipsmark, C.K.1
  • 58
    • 33748949692 scopus 로고    scopus 로고
    • Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the LIM-interaction domain
    • Tran, Y. H., Xu, Z., Kato, A., Mistry, A. C., Goya, Y., Taira, M., Brandt, S. J., and Hirose, S. (2006). Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the LIM-interaction domain. J. Biochem. 140, 105-119.
    • (2006) J. Biochem , vol.140 , pp. 105-119
    • Tran, Y.H.1    Xu, Z.2    Kato, A.3    Mistry, A.C.4    Goya, Y.5    Taira, M.6    Brandt, S.J.7    Hirose, S.8
  • 61
    • 66149177043 scopus 로고    scopus 로고
    • Role of SLC12A10.2, a Na-Cl cotransporterlike protein, in a Cl uptake mechanism in zebrafish (Danio rerio)
    • Wang, Y. F., Tseng, Y. C., Yan, J. J., Hiroi, J., and Hwang, P. P. (2009). Role of SLC12A10.2, a Na-Cl cotransporterlike protein, in a Cl uptake mechanism in zebrafish (Danio rerio). Am. J. Physiol. Regul. Integr. Comp. Physiol. 296, R1650-R1660.
    • (2009) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.296
    • Wang, Y.F.1    Tseng, Y.C.2    Yan, J.J.3    Hiroi, J.4    Hwang, P.P.5
  • 63
    • 0032555572 scopus 로고    scopus 로고
    • A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway
    • Xu, Y., Wong, S. H., Tang, B. L., Subramaniam, V. N., Zhang, T., and Hong, W. (1998). A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway. J. Biol. Chem. 273, 21783-21789.
    • (1998) J. Biol. Chem , vol.273 , pp. 21783-21789
    • Xu, Y.1    Wong, S.H.2    Tang, B.L.3    Subramaniam, V.N.4    Zhang, T.5    Hong, W.6
  • 65
    • 0032559599 scopus 로고    scopus 로고
    • A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells
    • Yoon, Y., Pitts, K. R., Dahan, S., and McNiven, M. A. (1998). A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. J. Cell Biol. 140, 779-793.
    • (1998) J. Cell Biol , vol.140 , pp. 779-793
    • Yoon, Y.1    Pitts, K.R.2    Dahan, S.3    McNiven, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.