메뉴 건너뛰기




Volumn 16, Issue 21, 1997, Pages 6325-6336

Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination

Author keywords

ENaC; Half life; Lysosome; Proteasome; Ubiquitination

Indexed keywords

ARGININE; BREFELDIN A; LYSINE; PROTEASOME; PROTEIN SUBUNIT; PROTEINASE INHIBITOR; SODIUM CHANNEL; UBIQUITIN;

EID: 0030731428     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.21.6325     Document Type: Article
Times cited : (620)

References (60)
  • 1
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson, S., Davis, D.L., Dahlbaeck, H., Joernvall, H. and Russell, D.W. (1989) Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem., 264, 8222-8229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlbaeck, H.3    Joernvall, H.4    Russell, D.W.5
  • 3
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
    • Brodsky, J.L. and McCracken, A.A. (1997) ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol., 7, 151-156.
    • (1997) Trends Cell Biol , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 4
    • 0027483065 scopus 로고
    • Epithelial sodium channel related to proteins involved in neurodegeneration
    • Canessa, C.M., Horisberger, J.-D. and Rossier, B.C. (1993) Epithelial sodium channel related to proteins involved in neurodegeneration. Nature, 361, 467-470.
    • (1993) Nature , vol.361 , pp. 467-470
    • Canessa, C.M.1    Horisberger, J.-D.2    Rossier, B.C.3
  • 6
    • 0028252575 scopus 로고
    • Membrane topology of the epithelial sodium channel in intact cells
    • Canessa, C.M., Mérillat, A.-M. and Rossier, B.C. (1994b) Membrane topology of the epithelial sodium channel in intact cells. Am. J. Physiol., 267, C1682-C1690.
    • (1994) Am. J. Physiol. , vol.267
    • Canessa, C.M.1    Mérillat, A.-M.2    Rossier, B.C.3
  • 8
    • 13344295074 scopus 로고    scopus 로고
    • Mutations in the subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis. pseudohypoaldosteronism type 1
    • Chang, S.S. et al. (1996) Mutations in the subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis. pseudohypoaldosteronism type 1. Nature Genet., 12, 248-253.
    • (1996) Nature Genet , vol.12 , pp. 248-253
    • Chang, S.S.1
  • 9
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. (1994) The ubiquitin-proteasome proteolytic pathway. Cell, 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 10
    • 0028841492 scopus 로고
    • Make it or break it: The role of ubiquitin-dependent proteolysis in cellular regulation
    • Deshaies, R.J. (1995) Make it or break it: The role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol., 5, 428-434.
    • (1995) Trends Cell Biol , vol.5 , pp. 428-434
    • Deshaies, R.J.1
  • 11
    • 0028588619 scopus 로고
    • Cell-specific expression of epithelial sodium channel α, β and γ subunits in aldosterone-responsive epithelia from the rat: Localization by in situ hybridization and immunocytochemistry
    • Duc, D., Farman, N., Canessa, C.M., Bonvalet, J.-P. and Rossier, B.C. (1994) Cell-specific expression of epithelial sodium channel α, β and γ subunits in aldosterone-responsive epithelia from the rat: localization by in situ hybridization and immunocytochemistry. J. Cell Biol., 127, 1907-1921.
    • (1994) J. Cell Biol. , vol.127 , pp. 1907-1921
    • Duc, D.1    Farman, N.2    Canessa, C.M.3    Bonvalet, J.-P.4    Rossier, B.C.5
  • 12
    • 0030041980 scopus 로고    scopus 로고
    • The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole
    • Egner, R. and Kuchler, K. (1996) The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole. FEBS Lett., 378, 177-181.
    • (1996) FEBS Lett , vol.378 , pp. 177-181
    • Egner, R.1    Kuchler, K.2
  • 13
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Chois, S., Corey, E.J. and Schreiber, S.L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science. 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Chois, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 15
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J.M., Moreau, V., André, B., Vollan, C. and Haguenauer-Tsapis, R. (1996) Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem., 271, 10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    André, B.3    Vollan, C.4    Haguenauer-Tsapis, R.5
  • 16
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalently linked to ubiquitin
    • Galcheva-Garbova, Z., Theroux, S.J. and Davis, R.J. (1995) The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene. 11, 2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Garbova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 17
    • 0030945484 scopus 로고    scopus 로고
    • Epithelial sodium channels: Function, structure, and regulation
    • Garty, H. and Palmer, L.G. (1997) Epithelial sodium channels: function, structure, and regulation. Physiol. Rev., 77, 359-396.
    • (1997) Physiol. Rev. , vol.77 , pp. 359-396
    • Garty, H.1    Palmer, L.G.2
  • 18
    • 0029905492 scopus 로고    scopus 로고
    • Oligomerization and maturation of Na, K-ATPase: Functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit
    • Geering, K., Beggah, A., Good, P., Girardet, S., Roy, S., Schaer, D. and Jaunin, P. (1996) Oligomerization and maturation of Na, K-ATPase: Functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit. J Cell Biol., 133, 1193-1204.
    • (1996) J Cell Biol , vol.133 , pp. 1193-1204
    • Geering, K.1    Beggah, A.2    Good, P.3    Girardet, S.4    Roy, S.5    Schaer, D.6    Jaunin, P.7
  • 19
    • 0029092801 scopus 로고
    • Hypertension caused by a truncated epithelial sodium channel gamma subunit: Genetic heterogeneity of Liddle syndrome
    • Hansson, J.H. et al (1995a) Hypertension caused by a truncated epithelial sodium channel gamma subunit: Genetic heterogeneity of Liddle syndrome. Nature Genet., 11, 76-82.
    • (1995) Nature Genet , vol.11 , pp. 76-82
    • Hansson, J.H.1
  • 20
    • 0029586683 scopus 로고
    • A de novo missense mutation of the β subunit of the epithelial sodium channel causes hypertension and Liddle syndrome, identifying a proline-rich segment critical for regulation of channel activity
    • Hansson, J.H., Schild, L., Lu, Y., Wilson, T.A., Gautschi, I., Shimkets, R.A., Nelson-Williams, C., Rossier, B.C. and Lifton, R.P. (1995b) A de novo missense mutation of the β subunit of the epithelial sodium channel causes hypertension and Liddle syndrome, identifying a proline-rich segment critical for regulation of channel activity. Proc. Natl Acad. Sci. USA. 25, 11495-11499.
    • (1995) Proc. Natl Acad. Sci. USA , vol.25 , pp. 11495-11499
    • Hansson, J.H.1    Schild, L.2    Lu, Y.3    Wilson, T.A.4    Gautschi, I.5    Shimkets, R.A.6    Nelson-Williams, C.7    Rossier, B.C.8    Lifton, R.P.9
  • 21
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein, C., Springael, J.Y., Volland, C., Haguenauer-Tsapis, R. and André, B. (1995) NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol., 18, 77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 22
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. and Riezman, H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell. 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 23
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme. Trends
    • Hilt, W. and Wolf, D.H. (1996) Proteasomes: destruction as a programme. Trends Biochem. Sci., 21, 96-102.
    • (1996) Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 24
    • 0026563337 scopus 로고
    • Highly inducible synthesis of heterologous proteins in epithelial cells carrying a glucocorticoid-responsive vector
    • Hirt, R.P., Poulain-Godefroy, O., Billotle, J., Kraehenbuhel, J.-P. and Fasel, N. (1992) Highly inducible synthesis of heterologous proteins in epithelial cells carrying a glucocorticoid-responsive vector. Gene. 111, 199-206.
    • (1992) Gene , vol.111 , pp. 199-206
    • Hirt, R.P.1    Poulain-Godefroy, O.2    Billotle, J.3    Kraehenbuhel, J.-P.4    Fasel, N.5
  • 25
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser, M. (1996) Protein degradation or regulation: Ub the judge. Cell. 84, 813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 27
    • 0028858161 scopus 로고
    • Multiple proteolytic systems including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L. and Riordan, J.R. (1995) Multiple proteolytic systems including the proteasome, contribute to CFTR processing. Cell. 83, 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 28
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S. and Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell. 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 29
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kölling, R. and Hollenberg, C.P. (1994) The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J., 13, 3261-3271.
    • (1994) EMBO J , vol.13 , pp. 3261-3271
    • Kölling, R.1    Hollenberg, C.P.2
  • 30
    • 0001182641 scopus 로고
    • A familial renal disorder simulating primary aldosteronism but with negligible aldosterone secretion
    • Liddle, G.W., Bledsoe, T. and Coppage, W.S., Jr (1963) A familial renal disorder simulating primary aldosteronism but with negligible aldosterone secretion. Trans. Assoc. Am. Physicians. 76, 199-213.
    • (1963) Trans. Assoc. Am. Physicians. , vol.76 , pp. 199-213
    • Liddle, G.W.1    Bledsoe, T.2    Coppage Jr., W.S.3
  • 34
    • 0029005859 scopus 로고
    • Cloning and expression of the β- And γ-subunits of the human epithelial sodium channel
    • McDonald, F.J., Price, M.P., Snyder, P.M. and Welsh, M.J. (1995) Cloning and expression of the β- and γ-subunits of the human epithelial sodium channel. Am. J. Physiol., 268, C1157-C1163.
    • (1995) Am. J. Physiol. , vol.268
    • McDonald, F.J.1    Price, M.P.2    Snyder, P.M.3    Welsh, M.J.4
  • 35
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product: A possible mechanism of receptor down modulation in M07e cells
    • Miyazawa, K., Toyama, K., Gotoh, A., Hendrie, P.C., Mantel, C. and Broxmeyer, H.E. (1994) Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells. Blood, 83, 137-145.
    • (1994) Blood , vol.83 , pp. 137-145
    • Miyazawa, K.1    Toyama, K.2    Gotoh, A.3    Hendrie, P.C.4    Mantel, C.5    Broxmeyer, H.E.6
  • 36
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori, S., Heldin, C.-H. and Claesson-Welsh, L. (1992) Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor. J. Biol. Chem., 267, 6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.-H.2    Claesson-Welsh, L.3
  • 37
    • 0024323295 scopus 로고
    • A general method of site-specific mutagenesis using a modification of the Thermus aquatiqus polymerase chain reaction
    • Nelson, R.M. and Long, G.L. (1989) A general method of site-specific mutagenesis using a modification of the Thermus aquatiqus polymerase chain reaction. Anal. Biochem., 180, 147-151.
    • (1989) Anal. Biochem. , vol.180 , pp. 147-151
    • Nelson, R.M.1    Long, G.L.2
  • 38
    • 0029059260 scopus 로고
    • + transport by lung epithelium in the clearance of airspace fluid
    • + transport by lung epithelium in the clearance of airspace fluid. New Horizons. 3, 240-247.
    • (1995) New Horizons , vol.3 , pp. 240-247
    • O'Brodovich, H.1
  • 39
    • 0027980321 scopus 로고
    • Ubiquitin and the proteasome are required for processing the NF-κB1 precursor and the activation of NF-κB
    • Palombella, V., Rando, O., Goldberg, A.L. and Maniatis, T. (1994) Ubiquitin and the proteasome are required for processing the NF-κB1 precursor and the activation of NF-κB. Cell. 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.1    Rando, O.2    Goldberg, A.L.3    Maniatis, T.4
  • 40
    • 0027458572 scopus 로고
    • Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors
    • Paolini, R. and Kinet, J.-P. (1993) Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors. EMBO J., 12, 779-786.
    • (1993) EMBO J , vol.12 , pp. 779-786
    • Paolini, R.1    Kinet, J.-P.2
  • 43
    • 0001316575 scopus 로고
    • Mechanisms of aldosterone action on sodium and potassium transport
    • Seldin, D.W. and Giebisch, G. (eds). Raven Press, New York, USA
    • Rossier, B.C. and Palmer, L.G. (1992) Mechanisms of aldosterone action on sodium and potassium transport. In Seldin, D.W. and Giebisch, G. (eds). The Kidney: Physiology and Pathophysiology. Raven Press, New York, USA. pp. 1373-1409.
    • (1992) The Kidney: Physiology and Pathophysiology , pp. 1373-1409
    • Rossier, B.C.1    Palmer, L.G.2
  • 45
    • 0027476871 scopus 로고
    • Electrolyte and fluid transport across the mature alveolar epithelium
    • Saumon, G. and Basset, G. (1993) Electrolyte and fluid transport across the mature alveolar epithelium. J. Appl. Physiol., 74, 1-15.
    • (1993) J. Appl. Physiol. , vol.74 , pp. 1-15
    • Saumon, G.1    Basset, G.2
  • 46
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitm-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J.M., Vierstra, R. and Howley, P.M. (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitm-protein ligase in the ubiquitination of p53. Cell, 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.3    Howley, P.M.4
  • 47
    • 0029046975 scopus 로고
    • A mutation in the epithelial sodium channel causing Liddle's disease increases channel activity in the Xenopus laevis oocyte expression system
    • Schild, L., Canessa, C.M., Shimkets, R.A., Warnock, D.G., Lifton, R.P. and Rossier, B.C. (1995) A mutation in the epithelial sodium channel causing Liddle's disease increases channel activity in the Xenopus laevis oocyte expression system. Proc. Natl Acad. Sci. USA. 92, 5699-5703.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5699-5703
    • Schild, L.1    Canessa, C.M.2    Shimkets, R.A.3    Warnock, D.G.4    Lifton, R.P.5    Rossier, B.C.6
  • 49
    • 0031017054 scopus 로고    scopus 로고
    • Identification of amino acid residues in the alpha, beta and gamma subunits of the epithelial sodium channel (ENaC) involved in amiloride block and ion permeation
    • Schild, L., Schneeberger, E., Gautschi, I. and Firsov, D. (1997) Identification of amino acid residues in the alpha, beta and gamma subunits of the epithelial sodium channel (ENaC) involved in amiloride block and ion permeation. J. Gen. Physiol., 109, 15-26.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 15-26
    • Schild, L.1    Schneeberger, E.2    Gautschi, I.3    Firsov, D.4
  • 50
    • 0027946089 scopus 로고
    • Liddles's syndrome: Heritable human hypertension caused by mutations in the β subunit of the epithelial sodium channel
    • Shimkets, R.A. et al. (1994) Liddles's syndrome: heritable human hypertension caused by mutations in the β subunit of the epithelial sodium channel. Cell, 79, 407-414.
    • (1994) Cell , vol.79 , pp. 407-414
    • Shimkets, R.A.1
  • 51
    • 0028102539 scopus 로고
    • Membrane topology of the amiloride-sensitive epithelial sodium channel
    • Snyder, P.M., McDonald, F.J., Stokes, J.B. and Welsh, M.J. (1994) Membrane topology of the amiloride-sensitive epithelial sodium channel. J. Biol. Chem., 269, 24379-24383.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24379-24383
    • Snyder, P.M.1    McDonald, F.J.2    Stokes, J.B.3    Welsh, M.J.4
  • 54
    • 0030068042 scopus 로고    scopus 로고
    • A novel splice-site mutation in the gamma subunit of the epithelial sodium channel gene in three pseudohypoaldosteronism type 1 families
    • Strautnieks, S.S., Thompson, R.J., Gardiner, R.M. and Chung, E. (1996) A novel splice-site mutation in the gamma subunit of the epithelial sodium channel gene in three pseudohypoaldosteronism type 1 families. Nature Genet., 13, 248-250.
    • (1996) Nature Genet , vol.13 , pp. 248-250
    • Strautnieks, S.S.1    Thompson, R.J.2    Gardiner, R.M.3    Chung, E.4
  • 55
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G.J., Van Kerkhof, P., Govers, R., Ciechanover, A. and Schwartz., A.L. (1996) The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J., 15, 3806-3812.
    • (1996) EMBO J , vol.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 57
    • 0029918734 scopus 로고    scopus 로고
    • Liddle disease caused by a missense mutation of beta subunit of the epithelial sodium channel gene
    • Tamura, H., Schild, L., Enomoto, N., Matsui, N., Marumo, F., Rossier, B.C. and Sasaki, S (1996) Liddle disease caused by a missense mutation of beta subunit of the epithelial sodium channel gene. J. Clin. Invest., 97, 1780-1784.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1780-1784
    • Tamura, H.1    Schild, L.2    Enomoto, N.3    Matsui, N.4    Marumo, F.5    Rossier, B.C.6    Sasaki, S.7
  • 58
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the 5 domain
    • Treier, M., Staszewski, L.M. and Bohmann, D. (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the 5 domain. Cell. 78, 787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 60
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S. and Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.