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Volumn 1802, Issue 12, 2010, Pages 1166-1177

Regulation of the epithelial sodium channel (ENaC) by membrane trafficking

Author keywords

Clathrin mediated endocytosis; Deubiquitination; ENaC trafficking; Rab proteins; Vesicle recycling

Indexed keywords

CLATHRIN; EPITHELIAL SODIUM CHANNEL; MEMBRANE PROTEIN; RAB PROTEIN;

EID: 78049274132     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2010.03.010     Document Type: Review
Times cited : (106)

References (228)
  • 2
    • 29144500339 scopus 로고    scopus 로고
    • Ubiquitylation of ion channels
    • Abriel H., Staub O. Ubiquitylation of ion channels. Physiology 2005, 20:398.
    • (2005) Physiology , vol.20 , pp. 398
    • Abriel, H.1    Staub, O.2
  • 3
    • 25444438993 scopus 로고    scopus 로고
    • Endogenous protease activation of ENaC: effect of serine protease inhibition on ENaC single channel properties
    • Adebamiro A., Cheng Y., Johnson J.P., Bridges R.J. Endogenous protease activation of ENaC: effect of serine protease inhibition on ENaC single channel properties. J. Gen. Physiol. 2005, 126:339.
    • (2005) J. Gen. Physiol. , vol.126 , pp. 339
    • Adebamiro, A.1    Cheng, Y.2    Johnson, J.P.3    Bridges, R.J.4
  • 5
    • 0037303045 scopus 로고    scopus 로고
    • Role of SGK in hormonal regulation of epithelial sodium channel in A6 cells
    • Alvarez d.l.R., Canessa C.M. Role of SGK in hormonal regulation of epithelial sodium channel in A6 cells. Am. J. Physiol. Cell Physiol. 2003, 284:C404-C414.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Alvarez, D.1    Canessa, C.M.2
  • 6
    • 0036091599 scopus 로고    scopus 로고
    • Effects of aldosterone on biosynthesis, traffic, and functional expression of epithelial sodium channels in A6 cells
    • Alvarez d.l.R., Li H., Canessa C.M. Effects of aldosterone on biosynthesis, traffic, and functional expression of epithelial sodium channels in A6 cells. J. Gen. Physiol. 2002, 119:427.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 427
    • Alvarez, D.1    Li, H.2    Canessa, C.M.3
  • 7
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik A.Y., Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 2004, 1695:189.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 9
    • 14844302797 scopus 로고    scopus 로고
    • A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1
    • Balla A., Tuymetova G., Tsiomenko A., Varnai P., Balla T. A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1. Mol. Biol. Cell 2005, 16:1282.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1282
    • Balla, A.1    Tuymetova, G.2    Tsiomenko, A.3    Varnai, P.4    Balla, T.5
  • 11
  • 14
    • 54049130846 scopus 로고    scopus 로고
    • Mechanisms of ENaC regulation and clinical implications
    • Bhalla V., Hallows K.R. Mechanisms of ENaC regulation and clinical implications. J. Am. Soc. Nephrol. 2008, 19:1845.
    • (2008) J. Am. Soc. Nephrol. , vol.19 , pp. 1845
    • Bhalla, V.1    Hallows, K.R.2
  • 16
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia M., Nielsen S., Engel A., Agre P. Cellular and molecular biology of the aquaporin water channels. Ann. Rev. Biochem. 1999, 68:425.
    • (1999) Ann. Rev. Biochem. , vol.68 , pp. 425
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 17
    • 34548487285 scopus 로고    scopus 로고
    • The formation of the cAMP/protein kinase A-dependent annexin 2-S100A10 complex with cystic fibrosis conductance regulator protein (CFTR) regulates CFTR channel function
    • Borthwick L.A., McGaw J., Conner G., Taylor C.J., Gerke V., Mehta A., Robson L., Muimo R. The formation of the cAMP/protein kinase A-dependent annexin 2-S100A10 complex with cystic fibrosis conductance regulator protein (CFTR) regulates CFTR channel function. Mol. Biol. Cell 2007, 18:3388.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3388
    • Borthwick, L.A.1    McGaw, J.2    Conner, G.3    Taylor, C.J.4    Gerke, V.5    Mehta, A.6    Robson, L.7    Muimo, R.8
  • 18
    • 0037404210 scopus 로고    scopus 로고
    • The ins and outs of aquaporin-2 trafficking
    • Brown D. The ins and outs of aquaporin-2 trafficking. Am. J. Physiol. Renal. Physiol. 2003, 284:F893-F901.
    • (2003) Am. J. Physiol. Renal. Physiol. , vol.284
    • Brown, D.1
  • 19
    • 59849095753 scopus 로고    scopus 로고
    • Sensing, signaling and sorting events in kidney epithelial cell physiology
    • Brown D., Breton S., Ausiello D.A., Marshansky V. Sensing, signaling and sorting events in kidney epithelial cell physiology. Traffic 2009, 10:275.
    • (2009) Traffic , vol.10 , pp. 275
    • Brown, D.1    Breton, S.2    Ausiello, D.A.3    Marshansky, V.4
  • 24
    • 12344311438 scopus 로고    scopus 로고
    • Acute ENaC stimulation by cAMP in a kidney cell line is mediated by exocytic insertion from a recycling channel pool
    • Butterworth M.B., Edinger R.S., Johnson J.P., Frizzell R.A. Acute ENaC stimulation by cAMP in a kidney cell line is mediated by exocytic insertion from a recycling channel pool. J. Gen. Physiol. 2005, 125:81.
    • (2005) J. Gen. Physiol. , vol.125 , pp. 81
    • Butterworth, M.B.1    Edinger, R.S.2    Johnson, J.P.3    Frizzell, R.A.4
  • 25
    • 38049177658 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH-L3 regulates the apical membrane recycling of the epithelial sodium channel
    • Butterworth M.B., Edinger R.S., Ovaa H., Burg D., Johnson J.P., Frizzell R.A. The deubiquitinating enzyme UCH-L3 regulates the apical membrane recycling of the epithelial sodium channel. J. Biol. Chem. 2007, 282:37885.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37885
    • Butterworth, M.B.1    Edinger, R.S.2    Ovaa, H.3    Burg, D.4    Johnson, J.P.5    Frizzell, R.A.6
  • 29
    • 0037013961 scopus 로고    scopus 로고
    • A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane
    • Caplan S., Naslavsky N., Hartnell L.M., Lodge R., Polishchuk R.S., Donaldson J.G., Bonifacino J.S. A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane. EMBO J. 2002, 21:2557.
    • (2002) EMBO J. , vol.21 , pp. 2557
    • Caplan, S.1    Naslavsky, N.2    Hartnell, L.M.3    Lodge, R.4    Polishchuk, R.S.5    Donaldson, J.G.6    Bonifacino, J.S.7
  • 30
    • 54449088865 scopus 로고    scopus 로고
    • Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation
    • Carattino M.D., Hughey R.P., Kleyman T.R. Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation. J. Biol. Chem. 2008, 283:25290.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25290
    • Carattino, M.D.1    Hughey, R.P.2    Kleyman, T.R.3
  • 34
    • 14544288669 scopus 로고    scopus 로고
    • The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin
    • Chen H., De C.P. The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:2766.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2766
    • Chen, H.1    De, C.P.2
  • 36
    • 0031930649 scopus 로고    scopus 로고
    • Protease modulation of the activity of the epithelial sodium channel expressed in Xenopus oocytes
    • Chraibi A., Vallet V., Firsov D., Hess S.K., Horisberger J.D. Protease modulation of the activity of the epithelial sodium channel expressed in Xenopus oocytes. J. Gen. Physiol. 1998, 111:127.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 127
    • Chraibi, A.1    Vallet, V.2    Firsov, D.3    Hess, S.K.4    Horisberger, J.D.5
  • 37
  • 39
    • 58849108762 scopus 로고    scopus 로고
    • Acute inhibition of ENaC function by syntaxin 1A
    • Condliffe S.B., Zhang H., Frizzell R.A. Acute inhibition of ENaC function by syntaxin 1A. FASEB J. 2003, 17:A914.
    • (2003) FASEB J. , vol.17
    • Condliffe, S.B.1    Zhang, H.2    Frizzell, R.A.3
  • 41
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: complex roles at the cell surface
    • Czech M.P. PIP2 and PIP3: complex roles at the cell surface. Cell 2000, 100:603.
    • (2000) Cell , vol.100 , pp. 603
    • Czech, M.P.1
  • 48
    • 70350428098 scopus 로고    scopus 로고
    • The role of galectins in protein trafficking
    • Delacour D., Koch A., Jacob R. The role of galectins in protein trafficking. Traffic 2009, 10:1405.
    • (2009) Traffic , vol.10 , pp. 1405
    • Delacour, D.1    Koch, A.2    Jacob, R.3
  • 50
    • 36348979793 scopus 로고    scopus 로고
    • Sodium channels and cystic fibrosis
    • Donaldson S.H., Boucher R.C. Sodium channels and cystic fibrosis. Chest 2007, 132:1631.
    • (2007) Chest , vol.132 , pp. 1631
    • Donaldson, S.H.1    Boucher, R.C.2
  • 53
    • 33644688683 scopus 로고    scopus 로고
    • Annexin II light chain p11 promotes functional expression of acid-sensing ion channel ASIC1a
    • Donier E., Rugiero F., Okuse K., Wood J.N. Annexin II light chain p11 promotes functional expression of acid-sensing ion channel ASIC1a. J. Biol. Chem. 2005, 280:38666.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38666
    • Donier, E.1    Rugiero, F.2    Okuse, K.3    Wood, J.N.4
  • 54
    • 0042744682 scopus 로고    scopus 로고
    • What is the role of SNARE proteins in membrane fusion?
    • Duman J.G., Forte J.G. What is the role of SNARE proteins in membrane fusion?. Am. J. Physiol. Cell Physiol. 2003, 285:C237-C249.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Duman, J.G.1    Forte, J.G.2
  • 55
    • 33750437407 scopus 로고    scopus 로고
    • Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes
    • Eathiraj S., Mishra A., Prekeris R., Lambright D.G. Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes. J. Mol. Biol. 2006, 364:121.
    • (2006) J. Mol. Biol. , vol.364 , pp. 121
    • Eathiraj, S.1    Mishra, A.2    Prekeris, R.3    Lambright, D.G.4
  • 56
    • 0041659182 scopus 로고    scopus 로고
    • Actin remodeling to facilitate membrane fusion
    • Eitzen G. Actin remodeling to facilitate membrane fusion. Biochim. Biophys. Acta 2003, 1641:175.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 175
    • Eitzen, G.1
  • 57
    • 33748439266 scopus 로고    scopus 로고
    • Regulation of maturation and processing of ENaC subunits in the rat kidney
    • Ergonul Z., Frindt G., Palmer L.G. Regulation of maturation and processing of ENaC subunits in the rat kidney. Am. J. Physiol. Renal. Physiol. 2006, 291:F683-F693.
    • (2006) Am. J. Physiol. Renal. Physiol. , vol.291
    • Ergonul, Z.1    Frindt, G.2    Palmer, L.G.3
  • 59
    • 0041659220 scopus 로고    scopus 로고
    • Structural insights into the SNARE mechanism
    • Fasshauer D. Structural insights into the SNARE mechanism. Biochim. Biophys. Acta 2003, 1641:87.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 87
    • Fasshauer, D.1
  • 61
    • 0038388266 scopus 로고    scopus 로고
    • The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes
    • Flores S.Y., Debonneville C., Staub O. The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes. Pflugers Arch. 2003, 446:334.
    • (2003) Pflugers Arch. , vol.446 , pp. 334
    • Flores, S.Y.1    Debonneville, C.2    Staub, O.3
  • 62
    • 41549120213 scopus 로고    scopus 로고
    • Regulation of membrane trafficking in polarized epithelial cells
    • Folsch H. Regulation of membrane trafficking in polarized epithelial cells. Curr. Opin. Cell Biol. 2008, 20:208.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 208
    • Folsch, H.1
  • 63
    • 34147167759 scopus 로고    scopus 로고
    • Na channel expression and activity in the medullary collecting duct of rat kidney
    • Frindt G., Ergonul Z., Palmer L.G. Na channel expression and activity in the medullary collecting duct of rat kidney. Am. J. Physiol. Renal. Physiol. 2007, 292:F1190-F1196.
    • (2007) Am. J. Physiol. Renal. Physiol. , vol.292
    • Frindt, G.1    Ergonul, Z.2    Palmer, L.G.3
  • 64
    • 44349121823 scopus 로고    scopus 로고
    • Surface expression of epithelial Na channel protein in rat kidney
    • Frindt G., Ergonul Z., Palmer L.G. Surface expression of epithelial Na channel protein in rat kidney. J. Gen. Physiol. 2008, 131:617.
    • (2008) J. Gen. Physiol. , vol.131 , pp. 617
    • Frindt, G.1    Ergonul, Z.2    Palmer, L.G.3
  • 65
    • 33645255532 scopus 로고    scopus 로고
    • Molecular physiology of renal aquaporins and sodium transporters: exciting approaches to understand regulation of renal water handling
    • Frokiaer J., Nielsen S., Knepper M.A. Molecular physiology of renal aquaporins and sodium transporters: exciting approaches to understand regulation of renal water handling. J. Am. Soc. Neprol. 2005, 16:2827.
    • (2005) J. Am. Soc. Neprol. , vol.16 , pp. 2827
    • Frokiaer, J.1    Nielsen, S.2    Knepper, M.A.3
  • 66
    • 52549126992 scopus 로고    scopus 로고
    • Regulation of secretory vesicle traffic by Rab small GTPases
    • Fukuda M. Regulation of secretory vesicle traffic by Rab small GTPases. Cell. Mol. Life Sci. 2008, 65:2801.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2801
    • Fukuda, M.1
  • 68
    • 0030945484 scopus 로고    scopus 로고
    • Epithelial sodium channels: function, structure, and regulation
    • Garty H., Palmer L.G. Epithelial sodium channels: function, structure, and regulation. Phys. Rev. 1997, 77:359.
    • (1997) Phys. Rev. , vol.77 , pp. 359
    • Garty, H.1    Palmer, L.G.2
  • 69
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V., Moss S.E. Annexins: from structure to function. Physiol. Rev. 2002, 82:331.
    • (2002) Physiol. Rev. , vol.82 , pp. 331
    • Gerke, V.1    Moss, S.E.2
  • 73
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: achieving specificity in membrane traffic
    • Grosshans B.L., Ortiz D., Novick P. Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:11821.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11821
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 79
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: lipid rafts and intracellular trafficking
    • Helms J.B., Zurzolo C. Lipids as targeting signals: lipid rafts and intracellular trafficking. Traffic 2004, 5:247.
    • (2004) Traffic , vol.5 , pp. 247
    • Helms, J.B.1    Zurzolo, C.2
  • 80
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L., Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 2003, 19:141.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141
    • Hicke, L.1    Dunn, R.2
  • 81
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • Hilgemann D.W., Feng S., Nasuhoglu C. The complex and intriguing lives of PIP2 with ion channels and transporters. Sci. STKE 2001, 2001:RE19.
    • (2001) Sci. STKE , vol.2001
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 82
    • 0037072733 scopus 로고    scopus 로고
    • Endogenously expressed epithelial sodium channel is present in lipid rafts in A6 cells
    • Hill W.G., An B., Johnson J.P. Endogenously expressed epithelial sodium channel is present in lipid rafts in A6 cells. J. Biol. Chem. 2002, 277:33541.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33541
    • Hill, W.G.1    An, B.2    Johnson, J.P.3
  • 84
    • 70449900602 scopus 로고    scopus 로고
    • A negative regulatory pathway of GLUT4 trafficking in adipocyte: new function of RIP140 in the cytoplasm via AS160
    • Ho P.C., Lin Y.W., Tsui Y.C., Gupta P., Wei L.N. A negative regulatory pathway of GLUT4 trafficking in adipocyte: new function of RIP140 in the cytoplasm via AS160. Cell Metab. 2009, 10:516.
    • (2009) Cell Metab. , vol.10 , pp. 516
    • Ho, P.C.1    Lin, Y.W.2    Tsui, Y.C.3    Gupta, P.4    Wei, L.N.5
  • 85
    • 34547943623 scopus 로고    scopus 로고
    • Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking
    • Hou J.C., Pessin J.E. Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking. Curr. Opin. Cell Biol. 2007, 19:466.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 466
    • Hou, J.C.1    Pessin, J.E.2
  • 86
    • 33947596679 scopus 로고    scopus 로고
    • The GLUT4 glucose transporter
    • Huang S., Czech M.P. The GLUT4 glucose transporter. Cell Metab. 2007, 5:237.
    • (2007) Cell Metab. , vol.5 , pp. 237
    • Huang, S.1    Czech, M.P.2
  • 88
    • 10344258627 scopus 로고    scopus 로고
    • Distinct pools of epithelial sodium channels are expressed at the plasma membrane
    • Hughey R.P., Bruns J.B., Kinlough C.L., Kleyman T.R. Distinct pools of epithelial sodium channels are expressed at the plasma membrane. J. Biol. Chem. 2004, 279:48491.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48491
    • Hughey, R.P.1    Bruns, J.B.2    Kinlough, C.L.3    Kleyman, T.R.4
  • 90
    • 0038689471 scopus 로고    scopus 로고
    • Epithelial sodium channel, salt intake, and hypertension
    • Hummler E. Epithelial sodium channel, salt intake, and hypertension. Curr. Hypertens. Rep. 2003, 5:11.
    • (2003) Curr. Hypertens. Rep. , vol.5 , pp. 11
    • Hummler, E.1
  • 91
    • 0032896647 scopus 로고    scopus 로고
    • Genetic disorders of membrane transport V. The epithelial sodium channel and its implication in human diseases
    • Hummler E., Horisberger J.-D. Genetic disorders of membrane transport V. The epithelial sodium channel and its implication in human diseases. Am. J. Physiol. 1999, 276:G567-G571.
    • (1999) Am. J. Physiol. , vol.276
    • Hummler, E.1    Horisberger, J.-D.2
  • 92
    • 33644877842 scopus 로고    scopus 로고
    • Lessons from mouse mutants of epithelial sodium channel and its regulatory proteins
    • Hummler E., Vallon V. Lessons from mouse mutants of epithelial sodium channel and its regulatory proteins. J. Am. Soc. Neprol. 2005, 16:3160.
    • (2005) J. Am. Soc. Neprol. , vol.16 , pp. 3160
    • Hummler, E.1    Vallon, V.2
  • 93
    • 0028872864 scopus 로고
    • + channels determines apparent channel conductance, ion selectivity and amiloride sensitivity
    • + channels determines apparent channel conductance, ion selectivity and amiloride sensitivity. Biophys. J. 1995, 69:1789.
    • (1995) Biophys. J. , vol.69 , pp. 1789
    • Ismailov, I.I.1    Berdiev, B.K.2    Benos, D.J.3
  • 94
    • 22344437651 scopus 로고    scopus 로고
    • Nedd4-2 isoforms differentially associate with ENaC and regulate its activity
    • Itani O.A., Stokes J.B., Thomas C.P. Nedd4-2 isoforms differentially associate with ENaC and regulate its activity. Am. J. Physiol. Renal. Physiol. 2005, 289(2):F334.
    • (2005) Am. J. Physiol. Renal. Physiol. , vol.289 , Issue.2
    • Itani, O.A.1    Stokes, J.B.2    Thomas, C.P.3
  • 95
    • 0036139675 scopus 로고    scopus 로고
    • Association of a sodium channel alpha subunit promoter variant with blood pressure
    • Iwai N., Baba S., Mannami T., Ogihara T., Ogata J. Association of a sodium channel alpha subunit promoter variant with blood pressure. J. Am. Soc. Neprol. 2002, 13:80.
    • (2002) J. Am. Soc. Neprol. , vol.13 , pp. 80
    • Iwai, N.1    Baba, S.2    Mannami, T.3    Ogihara, T.4    Ogata, J.5
  • 96
    • 33646364334 scopus 로고    scopus 로고
    • {delta}-Subunit confers novel biophysical features to {alpha}beta{gamma}-human epithelial sodium channel (ENaC) via a physical interaction
    • Ji H.L., Su X.F., Kedar S., Li J., Barbry P., Smith P.R., Matalon S., Benos D.J. {delta}-Subunit confers novel biophysical features to {alpha}beta{gamma}-human epithelial sodium channel (ENaC) via a physical interaction. J. Biol. Chem. 2006, 281:8233.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8233
    • Ji, H.L.1    Su, X.F.2    Kedar, S.3    Li, J.4    Barbry, P.5    Smith, P.R.6    Matalon, S.7    Benos, D.J.8
  • 97
    • 70349780899 scopus 로고    scopus 로고
    • Polarized endocytic transport: the roles of Rab11 and Rab11-FIPs in regulating cell polarity
    • Jing J., Prekeris R. Polarized endocytic transport: the roles of Rab11 and Rab11-FIPs in regulating cell polarity. Histol. Histopathol. 2009, 24:1171.
    • (2009) Histol. Histopathol. , vol.24 , pp. 1171
    • Jing, J.1    Prekeris, R.2
  • 98
    • 64249086005 scopus 로고    scopus 로고
    • Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell motility by modulating the actin cytoskeleton
    • Jing J., Tarbutton E., Wilson G., Prekeris R. Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell motility by modulating the actin cytoskeleton. Eur. J. Cell Biol. 2009, 88:325.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 325
    • Jing, J.1    Tarbutton, E.2    Wilson, G.3    Prekeris, R.4
  • 99
    • 0026612322 scopus 로고
    • Cellular mechanisms of action of mineralocorticoid hormones
    • Johnson J.P. Cellular mechanisms of action of mineralocorticoid hormones. Pharm. Ther. 1992, 53:1.
    • (1992) Pharm. Ther. , vol.53 , pp. 1
    • Johnson, J.P.1
  • 100
    • 66349123530 scopus 로고    scopus 로고
    • Eps15 homology domain 1-associated tubules contain phosphatidylinositol-4-phosphate and phosphatidylinositol-(4,5)-bisphosphate and are required for efficient recycling
    • Jovic M., Kieken F., Naslavsky N., Sorgen P.L., Caplan S. Eps15 homology domain 1-associated tubules contain phosphatidylinositol-4-phosphate and phosphatidylinositol-(4,5)-bisphosphate and are required for efficient recycling. Mol. Biol. Cell 2009, 20:2731.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2731
    • Jovic, M.1    Kieken, F.2    Naslavsky, N.3    Sorgen, P.L.4    Caplan, S.5
  • 103
    • 0034677749 scopus 로고    scopus 로고
    • Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2
    • Kawanishi M., Tamori Y., Okazawa H., Araki S., Shinoda H., Kasuga M. Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2. J. Biol. Chem. 2000, 275:8240.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8240
    • Kawanishi, M.1    Tamori, Y.2    Okazawa, H.3    Araki, S.4    Shinoda, H.5    Kasuga, M.6
  • 105
    • 68949094195 scopus 로고    scopus 로고
    • ENaC at the cutting edge: regulation of epithelial sodium channels by proteases
    • Kleyman T.R., Carattino M.D., Hughey R.P. ENaC at the cutting edge: regulation of epithelial sodium channels by proteases. J. Biol. Chem. 2009, 284:20447.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20447
    • Kleyman, T.R.1    Carattino, M.D.2    Hughey, R.P.3
  • 106
    • 33749523601 scopus 로고    scopus 로고
    • Regulation of ENaCs by proteases: an increasingly complex story
    • Kleyman T.R., Myerburg M.M., Hughey R.P. Regulation of ENaCs by proteases: an increasingly complex story. Kidney Int. 2006, 70:1391.
    • (2006) Kidney Int. , vol.70 , pp. 1391
    • Kleyman, T.R.1    Myerburg, M.M.2    Hughey, R.P.3
  • 109
  • 110
    • 1942442455 scopus 로고    scopus 로고
    • Early nongenomic events in aldosterone action in renal collecting duct cells: PKCalpha activation, mineralocorticoid receptor phosphorylation, and cross-talk with the genomic response
    • Le M.C., Ouvrard-Pascaud A., Capurro C., Cluzeaud F., Fay M., Jaisser F., Farman N., Blot-Chabaud M. Early nongenomic events in aldosterone action in renal collecting duct cells: PKCalpha activation, mineralocorticoid receptor phosphorylation, and cross-talk with the genomic response. J. Am. Soc. Nephrol. 2004, 15:1145.
    • (2004) J. Am. Soc. Nephrol. , vol.15 , pp. 1145
    • Le, M.C.1    Ouvrard-Pascaud, A.2    Capurro, C.3    Cluzeaud, F.4    Fay, M.5    Jaisser, F.6    Farman, N.7    Blot-Chabaud, M.8
  • 113
    • 67649816872 scopus 로고    scopus 로고
    • The activity of the epithelial sodium channels is regulated by caveolin-1 via a Nedd4-2-dependent mechanism
    • Lee I.H., Campbell C.R., Song S.H., Day M.L., Kumar S., Cook D.I., Dinudom A. The activity of the epithelial sodium channels is regulated by caveolin-1 via a Nedd4-2-dependent mechanism. J. Biol. Chem. 2009, 284:12663.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12663
    • Lee, I.H.1    Campbell, C.R.2    Song, S.H.3    Day, M.L.4    Kumar, S.5    Cook, D.I.6    Dinudom, A.7
  • 114
    • 35649027433 scopus 로고    scopus 로고
    • Akt mediates the effect of insulin on epithelial sodium channels by inhibiting Nedd4-2
    • Lee I.H., Dinudom A., Sanchez-Perez A., Kumar S., Cook D.I. Akt mediates the effect of insulin on epithelial sodium channels by inhibiting Nedd4-2. J. Biol. Chem. 2007, 282:29866.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29866
    • Lee, I.H.1    Dinudom, A.2    Sanchez-Perez, A.3    Kumar, S.4    Cook, D.I.5
  • 116
    • 0001182641 scopus 로고
    • A familial renal disorder simulating primary aldosteronism but with negligible aldosterone secretion
    • Liddle G.W., Bledsoe T., Coppage W.S. A familial renal disorder simulating primary aldosteronism but with negligible aldosterone secretion. Trans. Assoc. Am. Phys. 1963, 76:199.
    • (1963) Trans. Assoc. Am. Phys. , vol.76 , pp. 199
    • Liddle, G.W.1    Bledsoe, T.2    Coppage, W.S.3
  • 117
    • 0035936780 scopus 로고    scopus 로고
    • Molecular mechanisms of human hypertension
    • Lifton R.P., Gharavi A.G., Geller D.S. Molecular mechanisms of human hypertension. Cell 2001, 104:545.
    • (2001) Cell , vol.104 , pp. 545
    • Lifton, R.P.1    Gharavi, A.G.2    Geller, D.S.3
  • 118
    • 0001647625 scopus 로고    scopus 로고
    • Exocytosis: the many masters of the exocyst
    • Lipschutz J.H., Mostov K.E. Exocytosis: the many masters of the exocyst. Curr. Biol. 2002, 12:R212-R214.
    • (2002) Curr. Biol. , vol.12
    • Lipschutz, J.H.1    Mostov, K.E.2
  • 119
    • 64149085069 scopus 로고    scopus 로고
    • Regulated sodium transport in the renal connecting tubule (CNT) via the epithelial sodium channel (ENaC)
    • Loffing J., Korbmacher C. Regulated sodium transport in the renal connecting tubule (CNT) via the epithelial sodium channel (ENaC). Pflugers Arch. 2009, 458:111.
    • (2009) Pflugers Arch. , vol.458 , pp. 111
    • Loffing, J.1    Korbmacher, C.2
  • 121
    • 34547830212 scopus 로고    scopus 로고
    • The PY motif of ENaC, mutated in Liddle syndrome, regulates channel internalization, sorting and mobilization from subapical pool
    • Lu C., Pribanic S., Debonneville A., Jiang C., Rotin D. The PY motif of ENaC, mutated in Liddle syndrome, regulates channel internalization, sorting and mobilization from subapical pool. Traffic 2007, 8:1246.
    • (2007) Traffic , vol.8 , pp. 1246
    • Lu, C.1    Pribanic, S.2    Debonneville, A.3    Jiang, C.4    Rotin, D.5
  • 122
    • 34548652014 scopus 로고    scopus 로고
    • Regulation of the epithelial sodium channel by phosphatidylinositides: experiments, implications, and speculations
    • Ma H.P., Chou C.F., Wei S.P., Eaton D.C. Regulation of the epithelial sodium channel by phosphatidylinositides: experiments, implications, and speculations. Pflugers Arch. 2007, 455:169.
    • (2007) Pflugers Arch. , vol.455 , pp. 169
    • Ma, H.P.1    Chou, C.F.2    Wei, S.P.3    Eaton, D.C.4
  • 123
    • 20844435326 scopus 로고    scopus 로고
    • Role of Nedd4-2 and polyubiquitination in epithelial sodium channel degradation in untransfected renal A6 cells expressing endogenous ENaC subunits
    • Malik B., Yue Q., Yue G., Chen X., Price S.R., Mitch W.E., Eaton D.C. Role of Nedd4-2 and polyubiquitination in epithelial sodium channel degradation in untransfected renal A6 cells expressing endogenous ENaC subunits. Am. J. Physiol. Renal. Physiol. 2005, 289(1):F107.
    • (2005) Am. J. Physiol. Renal. Physiol. , vol.289 , Issue.1
    • Malik, B.1    Yue, Q.2    Yue, G.3    Chen, X.4    Price, S.R.5    Mitch, W.E.6    Eaton, D.C.7
  • 125
    • 33845355027 scopus 로고    scopus 로고
    • Interaction of epithelial ion channels with the actin-based cytoskeleton
    • Mazzochi C., Benos D.J., Smith P.R. Interaction of epithelial ion channels with the actin-based cytoskeleton. Am. J. Physiol. Renal. Physiol. 2006, 291:F1113-F1122.
    • (2006) Am. J. Physiol. Renal. Physiol. , vol.291
    • Mazzochi, C.1    Benos, D.J.2    Smith, P.R.3
  • 126
    • 18244382092 scopus 로고    scopus 로고
    • SGK1: a rapid aldosterone-induced regulator of renal sodium reabsorption
    • McCormick J.A., Bhalla V., Pao A.C., Pearce D. SGK1: a rapid aldosterone-induced regulator of renal sodium reabsorption. Physiology (Bethesda) 2005, 20:134.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 134
    • McCormick, J.A.1    Bhalla, V.2    Pao, A.C.3    Pearce, D.4
  • 127
    • 41649119435 scopus 로고    scopus 로고
    • Aldosterone regulates rapid trafficking of ENaC subunits in renal cortical collecting duct cells via protein kinase D a ctivation
    • McEneaney V., Harvey B.J., Thomas W. Aldosterone regulates rapid trafficking of ENaC subunits in renal cortical collecting duct cells via protein kinase D a ctivation. Mol. Endocrinol. 2008, 22(4):881.
    • (2008) Mol. Endocrinol. , vol.22 , Issue.4 , pp. 881
    • McEneaney, V.1    Harvey, B.J.2    Thomas, W.3
  • 128
    • 15544364940 scopus 로고    scopus 로고
    • Links between dietary salt intake, renal salt handling, blood pressure, and cardiovascular diseases
    • Meneton P., Jeunemaitre X., de Wardener H.E., Macgregor G.A. Links between dietary salt intake, renal salt handling, blood pressure, and cardiovascular diseases. Phys. Rev. 2005, 85:679.
    • (2005) Phys. Rev. , vol.85 , pp. 679
    • Meneton, P.1    Jeunemaitre, X.2    de Wardener, H.E.3    Macgregor, G.A.4
  • 129
    • 33646795597 scopus 로고    scopus 로고
    • Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes
    • Millard S.M., Wood S.A. Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes. J. Cell Biol. 2006, 173:463.
    • (2006) J. Cell Biol. , vol.173 , pp. 463
    • Millard, S.M.1    Wood, S.A.2
  • 134
    • 41149162021 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics by Arf-family GTPases
    • Myers K.R., Casanova J.E. Regulation of actin cytoskeleton dynamics by Arf-family GTPases. Trends Cell Biol. 2008, 18:184.
    • (2008) Trends Cell Biol. , vol.18 , pp. 184
    • Myers, K.R.1    Casanova, J.E.2
  • 136
    • 2342489409 scopus 로고    scopus 로고
    • Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane
    • Naslavsky N., Boehm M., Backlund P.S., Caplan S. Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane. Mol. Biol. Cell 2004, 15:2410.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2410
    • Naslavsky, N.1    Boehm, M.2    Backlund, P.S.3    Caplan, S.4
  • 137
    • 30044449424 scopus 로고    scopus 로고
    • Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport
    • Naslavsky N., Rahajeng J., Sharma M., Jovic M., Caplan S. Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport. Mol. Biol. Cell 2006, 17:163.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 163
    • Naslavsky, N.1    Rahajeng, J.2    Sharma, M.3    Jovic, M.4    Caplan, S.5
  • 138
    • 34547095021 scopus 로고    scopus 로고
    • Aldosterone-induced modification of osmoregulated ENaC trafficking
    • Niisato N., Taruno A., Marunaka Y. Aldosterone-induced modification of osmoregulated ENaC trafficking. Biochem. Biophys. Res. Commun. 2007, 361:162.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 162
    • Niisato, N.1    Taruno, A.2    Marunaka, Y.3
  • 140
    • 29244477972 scopus 로고    scopus 로고
    • Trafficking mechanism of water channel aquaporin-2
    • Noda Y., Sasaki S. Trafficking mechanism of water channel aquaporin-2. Biol. Cell 2005, 97:885.
    • (2005) Biol. Cell , vol.97 , pp. 885
    • Noda, Y.1    Sasaki, S.2
  • 141
    • 2942606055 scopus 로고    scopus 로고
    • Differential translational efficiency of ENaC subunits during lung development
    • Otulakowski G., Rafii B., O'Brodovich H. Differential translational efficiency of ENaC subunits during lung development. Am. J. Respir. Cell. Mol. Biol. 2004, 30:862.
    • (2004) Am. J. Respir. Cell. Mol. Biol. , vol.30 , pp. 862
    • Otulakowski, G.1    Rafii, B.2    O'Brodovich, H.3
  • 142
    • 33645277808 scopus 로고    scopus 로고
    • GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells
    • Paladino S., Pocard T., Catino M.A., Zurzolo C. GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells. J. Cell Biol. 2006, 172:1023.
    • (2006) J. Cell Biol. , vol.172 , pp. 1023
    • Paladino, S.1    Pocard, T.2    Catino, M.A.3    Zurzolo, C.4
  • 143
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S., Sarnataro D., Pillich R., Tivodar S., Nitsch L., Zurzolo C. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 2004, 167:699.
    • (2004) J. Cell Biol. , vol.167 , pp. 699
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 144
    • 0026520186 scopus 로고
    • Epithelial Na channels: function and diversity
    • Palmer L.G. Epithelial Na channels: function and diversity. Annu. Rev. Physiol. 1992, 54:51.
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 51
    • Palmer, L.G.1
  • 145
    • 0034169041 scopus 로고    scopus 로고
    • Vesicular transport as a new paradigm in short-term regulation of transepithelial transport
    • Park C.S., Leem C.H., Jang Y.J., Shim Y.H. Vesicular transport as a new paradigm in short-term regulation of transepithelial transport. J. Korean Med. Sci. 2000, 15:123.
    • (2000) J. Korean Med. Sci. , vol.15 , pp. 123
    • Park, C.S.1    Leem, C.H.2    Jang, Y.J.3    Shim, Y.H.4
  • 147
    • 33847402692 scopus 로고    scopus 로고
    • Salt, sodium channels, and SGK1
    • Pearce D., Kleyman T.R. Salt, sodium channels, and SGK1. J. Clin. Invest. 2007, 117:592.
    • (2007) J. Clin. Invest. , vol.117 , pp. 592
    • Pearce, D.1    Kleyman, T.R.2
  • 149
    • 35548947255 scopus 로고    scopus 로고
    • Ion channel regulation by Ras, Rho, and Rab small GTPases
    • Pochynyuk O., Stockand J.D., Staruschenko A. Ion channel regulation by Ras, Rho, and Rab small GTPases. Exp. Biol. Med. 2007, 232:1258.
    • (2007) Exp. Biol. Med. , vol.232 , pp. 1258
    • Pochynyuk, O.1    Stockand, J.D.2    Staruschenko, A.3
  • 152
    • 33644876406 scopus 로고    scopus 로고
    • Central role for ENaC in development of hypertension
    • Pratt J.H. Central role for ENaC in development of hypertension. J. Am. Soc. Nephrol. 2005, 16:3154.
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 3154
    • Pratt, J.H.1
  • 153
    • 1542395155 scopus 로고    scopus 로고
    • Rabs, Rips, FIPs, and endocytic membrane traffic
    • Prekeris R. Rabs, Rips, FIPs, and endocytic membrane traffic. Sci. World J. 2003, 3:870.
    • (2003) Sci. World J. , vol.3 , pp. 870
    • Prekeris, R.1
  • 154
    • 0033031225 scopus 로고    scopus 로고
    • Effect of subunit composition and Liddle's syndrome mutations on biosynthesis of ENaC
    • Prince L.S., Welsh M.J. Effect of subunit composition and Liddle's syndrome mutations on biosynthesis of ENaC. Am. J. Physiol. 1999, 276:C1346-C1351.
    • (1999) Am. J. Physiol. , vol.276
    • Prince, L.S.1    Welsh, M.J.2
  • 155
    • 33646542676 scopus 로고    scopus 로고
    • Adipocytes support cAMP-dependent translocation of aquaporin-2 from intracellular sites distinct from the insulin-responsive GLUT4 storage compartment
    • Procino G., Caces D.B., Valenti G., Pessin J.E. Adipocytes support cAMP-dependent translocation of aquaporin-2 from intracellular sites distinct from the insulin-responsive GLUT4 storage compartment. Am. J. Physiol. Renal. Physiol. 2006, 290:F985-F994.
    • (2006) Am. J. Physiol. Renal. Physiol. , vol.290
    • Procino, G.1    Caces, D.B.2    Valenti, G.3    Pessin, J.E.4
  • 161
    • 3242887228 scopus 로고    scopus 로고
    • Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
    • Rescher U., Ruhe D., Ludwig C., Zobiack N., Gerke V. Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J. Cell Sci. 2004, 117:3473.
    • (2004) J. Cell Sci. , vol.117 , pp. 3473
    • Rescher, U.1    Ruhe, D.2    Ludwig, C.3    Zobiack, N.4    Gerke, V.5
  • 163
    • 3142666167 scopus 로고    scopus 로고
    • Recycling and resensitization of the neurokinin 1 receptor. Influence of agonist concentration and Rab GTPases
    • Roosterman D., Cottrell G.S., Schmidlin F., Steinhoff M., Bunnett N.W. Recycling and resensitization of the neurokinin 1 receptor. Influence of agonist concentration and Rab GTPases. J. Biol. Chem. 2004, 279:30670.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30670
    • Roosterman, D.1    Cottrell, G.S.2    Schmidlin, F.3    Steinhoff, M.4    Bunnett, N.W.5
  • 164
    • 0036197218 scopus 로고    scopus 로고
    • Epithelial sodium channel and the control of sodium balance: interaction between genetic and environmental factors
    • Rossier B.C., Pradervand S., Schild L., Hummler E. Epithelial sodium channel and the control of sodium balance: interaction between genetic and environmental factors. Annu. Rev. Physiol. 2002, 64:877.
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 877
    • Rossier, B.C.1    Pradervand, S.2    Schild, L.3    Hummler, E.4
  • 165
    • 0036019838 scopus 로고    scopus 로고
    • Hormonal regulation of the epithelial sodium channel ENaC: N or Po?
    • Rossier B.C. Hormonal regulation of the epithelial sodium channel ENaC: N or Po?. J. Gen. Physiol. 2002, 120:67.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 67
    • Rossier, B.C.1
  • 166
    • 0037382813 scopus 로고    scopus 로고
    • Negative regulators of sodium transport in the kidney: key factors in understanding salt-sensitive hypertension?
    • Rossier B.C. Negative regulators of sodium transport in the kidney: key factors in understanding salt-sensitive hypertension?. J. Clin. Inv. 2003, 111:947.
    • (2003) J. Clin. Inv. , vol.111 , pp. 947
    • Rossier, B.C.1
  • 167
    • 10344236448 scopus 로고    scopus 로고
    • The epithelial sodium channel: activation by membrane-bound serine proteases
    • Rossier B.C. The epithelial sodium channel: activation by membrane-bound serine proteases. Proc. Am. Thorac. Soc. 2004, 1:4.
    • (2004) Proc. Am. Thorac. Soc. , vol.1 , pp. 4
    • Rossier, B.C.1
  • 168
    • 54249139553 scopus 로고    scopus 로고
    • Role of the UPS in Liddle syndrome
    • Rotin D. Role of the UPS in Liddle syndrome. BMC Biochem. 2008, 9(Suppl 1):S5.
    • (2008) BMC Biochem. , vol.9 , Issue.SUPPL 1
    • Rotin, D.1
  • 170
    • 52449131279 scopus 로고    scopus 로고
    • ENaC and its regulatory proteins as drug targets for blood pressure control
    • Rotin D., Schild L. ENaC and its regulatory proteins as drug targets for blood pressure control. Curr. Drug Targets. 2008, 9:709.
    • (2008) Curr. Drug Targets. , vol.9 , pp. 709
    • Rotin, D.1    Schild, L.2
  • 174
    • 27144473630 scopus 로고    scopus 로고
    • Rab proteins regulate epithelial sodium channel activity in colonic epithelial HT-29 cells
    • Saxena S., Singh M., Engisch K., Fukuda M., Kaur S. Rab proteins regulate epithelial sodium channel activity in colonic epithelial HT-29 cells. Biochem. Biophys. Res. Commun. 2005, 337:1219.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1219
    • Saxena, S.1    Singh, M.2    Engisch, K.3    Fukuda, M.4    Kaur, S.5
  • 175
    • 33646087205 scopus 로고    scopus 로고
    • Rab27a regulates epithelial sodium channel (ENaC) activity through synaptotagmin-like protein (SLP-5) and Munc13-4 effector mechanism
    • Saxena S.K., Horiuchi H., Fukuda M. Rab27a regulates epithelial sodium channel (ENaC) activity through synaptotagmin-like protein (SLP-5) and Munc13-4 effector mechanism. Biochem. Biophys. Res. Commun. 2006, 344:651.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 651
    • Saxena, S.K.1    Horiuchi, H.2    Fukuda, M.3
  • 176
    • 33750720020 scopus 로고    scopus 로고
    • Regulation of epithelial ion channels by Rab GTPases
    • Saxena S.K., Kaur S. Regulation of epithelial ion channels by Rab GTPases. Biochem. Biophys. Res. Commun. 2006, 351:582.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 582
    • Saxena, S.K.1    Kaur, S.2
  • 177
    • 29644432113 scopus 로고    scopus 로고
    • Rab4 GTP/GDP modulates amiloride-sensitive sodium channel (ENaC) function in colonic epithelia
    • Saxena S.K., Singh M., Shibata H., Kaur S., George C. Rab4 GTP/GDP modulates amiloride-sensitive sodium channel (ENaC) function in colonic epithelia. Biochem. Biophys. Res. Commun. 2006, 340:726.
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 726
    • Saxena, S.K.1    Singh, M.2    Shibata, H.3    Kaur, S.4    George, C.5
  • 178
    • 0033498876 scopus 로고    scopus 로고
    • Lung symptoms in pseudohypoaldosteronism type I are associated with deficiency of the α-subunit of the epithelial sodium channel
    • Schaedel C., Marthinsen L., Kristofferson A.-C., Kornfalt R., Nilsson K.O., Orlenius B., Holmberg L. Lung symptoms in pseudohypoaldosteronism type I are associated with deficiency of the α-subunit of the epithelial sodium channel. J. Pediatr. 1999, 135:739.
    • (1999) J. Pediatr. , vol.135 , pp. 739
    • Schaedel, C.1    Marthinsen, L.2    Kristofferson, A.-C.3    Kornfalt, R.4    Nilsson, K.O.5    Orlenius, B.6    Holmberg, L.7
  • 181
    • 33745863535 scopus 로고    scopus 로고
    • Body water homeostasis: clinical disorders of urinary dilution and concentration
    • Schrier R.W. Body water homeostasis: clinical disorders of urinary dilution and concentration. J. Am. Soc. Neprol. 2006, 17:1820.
    • (2006) J. Am. Soc. Neprol. , vol.17 , pp. 1820
    • Schrier, R.W.1
  • 183
    • 0030820814 scopus 로고    scopus 로고
    • The activity of the epithelial sodium channel is regulated by clathrin-mediated endocytosis
    • Shimkets R.A., Lifton R.P., Canessa C.M. The activity of the epithelial sodium channel is regulated by clathrin-mediated endocytosis. J. Biol. Chem. 1997, 272:25537.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25537
    • Shimkets, R.A.1    Lifton, R.P.2    Canessa, C.M.3
  • 187
    • 77950188929 scopus 로고    scopus 로고
    • The role of FIP3-dependent endosome transport during cytokinesis
    • Simon G.C., Prekeris R. The role of FIP3-dependent endosome transport during cytokinesis. Commun. Integr. Biol. 2008, 1:132.
    • (2008) Commun. Integr. Biol. , vol.1 , pp. 132
    • Simon, G.C.1    Prekeris, R.2
  • 188
    • 27844476338 scopus 로고    scopus 로고
    • + channel trafficking
    • + channel trafficking. Endocrinology 2005, 146:5079.
    • (2005) Endocrinology , vol.146 , pp. 5079
    • Snyder, P.M.1
  • 190
    • 6344260586 scopus 로고    scopus 로고
    • Increased blood pressure, aldosterone activity, and regional differences in renal ENaC protein during vasopressin escape
    • Song J., Hu X., Khan O., Tian Y., Verbalis J.G., Ecelbarger C.A. Increased blood pressure, aldosterone activity, and regional differences in renal ENaC protein during vasopressin escape. Am. J. Physiol. Renal. Physiol. 2004, 287:F1076-F1083.
    • (2004) Am. J. Physiol. Renal. Physiol. , vol.287
    • Song, J.1    Hu, X.2    Khan, O.3    Tian, Y.4    Verbalis, J.G.5    Ecelbarger, C.A.6
  • 191
    • 33646541375 scopus 로고    scopus 로고
    • Regulation of blood pressure, the epithelial sodium channel (ENaC), and other key renal sodium transporters by chronic insulin infusion in rats
    • Song J., Hu X., Riazi S., Tiwari S., Wade J.B., Ecelbarger C.A. Regulation of blood pressure, the epithelial sodium channel (ENaC), and other key renal sodium transporters by chronic insulin infusion in rats. Am. J. Physiol. Renal. Physiol. 2006, 290:F1055-F1064.
    • (2006) Am. J. Physiol. Renal. Physiol. , vol.290
    • Song, J.1    Hu, X.2    Riazi, S.3    Tiwari, S.4    Wade, J.B.5    Ecelbarger, C.A.6
  • 192
    • 0035050460 scopus 로고    scopus 로고
    • Diabetes, hypertension, and cardiovascular disease: an update
    • Sowers J.R., Epstein M., Frohlich E.D. Diabetes, hypertension, and cardiovascular disease: an update. Hypertension 2001, 37:1053.
    • (2001) Hypertension , vol.37 , pp. 1053
    • Sowers, J.R.1    Epstein, M.2    Frohlich, E.D.3
  • 193
    • 28244497743 scopus 로고    scopus 로고
    • + channel activity by conserved serine/threonine switches within sorting signals
    • + channel activity by conserved serine/threonine switches within sorting signals. J. Biol. Chem. 2005, 280:39161.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39161
    • Staruschenko, A.1    Pochynyuk, O.2    Stockand, J.D.3
  • 198
    • 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., Chung E. A novel splice-site mutation in the gamma subunit of the epithelial sodium channel gene in three pseudohypoaldosteronism type 1 families. Nat. Genet. 1996, 13:248.
    • (1996) Nat. Genet. , vol.13 , pp. 248
    • Strautnieks, S.S.1    Thompson, R.J.2    Gardiner, R.M.3    Chung, E.4
  • 199
    • 0037659044 scopus 로고    scopus 로고
    • Altered renal handling of sodium in human hypertension: short review of the evidence
    • Strazzullo P., Galletti F., Barba G. Altered renal handling of sodium in human hypertension: short review of the evidence. Hypertension 2003, 41:1000.
    • (2003) Hypertension , vol.41 , pp. 1000
    • Strazzullo, P.1    Galletti, F.2    Barba, G.3
  • 201
    • 0043162015 scopus 로고    scopus 로고
    • Revisiting the role of SNAREs in exocytosis and membrane fusion
    • Szule J.A., Coorssen J.R. Revisiting the role of SNAREs in exocytosis and membrane fusion. Biochim. Biophys. Acta 2003, 1641:121.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 121
    • Szule, J.A.1    Coorssen, J.R.2
  • 202
    • 10944248447 scopus 로고    scopus 로고
    • Molecular mechanisms and drug development in aquaporin water channel diseases: water channel aquaporin-2 of kidney collecting duct cells
    • Takata K., Tajika Y., Matsuzaki T., Aoki T., Suzuki T., Abduxukur A., Hagiwara H. Molecular mechanisms and drug development in aquaporin water channel diseases: water channel aquaporin-2 of kidney collecting duct cells. J. Pharmacol. Sci. 2004, 96:255.
    • (2004) J. Pharmacol. Sci. , vol.96 , pp. 255
    • Takata, K.1    Tajika, Y.2    Matsuzaki, T.3    Aoki, T.4    Suzuki, T.5    Abduxukur, A.6    Hagiwara, H.7
  • 203
    • 32344431710 scopus 로고    scopus 로고
    • Class I FIPs, Rab11-binding proteins that regulate endocytic sorting and recycling
    • Tarbutton E., Peden A.A., Junutula J.R., Prekeris R. Class I FIPs, Rab11-binding proteins that regulate endocytic sorting and recycling. Methods Enzymol. 2005, 403:512.
    • (2005) Methods Enzymol. , vol.403 , pp. 512
    • Tarbutton, E.1    Peden, A.A.2    Junutula, J.R.3    Prekeris, R.4
  • 205
    • 33749503026 scopus 로고    scopus 로고
    • Analysis of detergent-resistant membranes associated with apical and basolateral GPI-anchored proteins in polarized epithelial cells
    • Tivodar S., Paladino S., Pillich R., Prinetti A., Chigorno V., van M.G., Sonnino S., Zurzolo C. Analysis of detergent-resistant membranes associated with apical and basolateral GPI-anchored proteins in polarized epithelial cells. FEBS Lett. 2006, 580:5705.
    • (2006) FEBS Lett. , vol.580 , pp. 5705
    • Tivodar, S.1    Paladino, S.2    Pillich, R.3    Prinetti, A.4    Chigorno, V.5    van, M.G.6    Sonnino, S.7    Zurzolo, C.8
  • 206
    • 38549147387 scopus 로고    scopus 로고
    • Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells
    • Trifaro J.M., Gasman S., Gutierrez L.M. Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells. Acta Physiol. (Oxf.) 2008, 192:165.
    • (2008) Acta Physiol. (Oxf.) , vol.192 , pp. 165
    • Trifaro, J.M.1    Gasman, S.2    Gutierrez, L.M.3
  • 208
    • 0030879756 scopus 로고    scopus 로고
    • An epithelial serine protease activates the amiloride-sensitive sodium channel
    • Vallet V., Chraibi A., Gaeggeler H.P., Horisberger J.D., Rossier B.C. An epithelial serine protease activates the amiloride-sensitive sodium channel. Nature 1997, 389:607.
    • (1997) Nature , vol.389 , pp. 607
    • Vallet, V.1    Chraibi, A.2    Gaeggeler, H.P.3    Horisberger, J.D.4    Rossier, B.C.5
  • 209
    • 12144279572 scopus 로고    scopus 로고
    • New insights into the role of serum- and glucocorticoid-inducible kinase SGK1 in the regulation of renal function and blood pressure
    • Vallon V., Lang F. New insights into the role of serum- and glucocorticoid-inducible kinase SGK1 in the regulation of renal function and blood pressure. Curr. Opin. Nephrol. Hypertens. 2005, 14:59.
    • (2005) Curr. Opin. Nephrol. Hypertens. , vol.14 , pp. 59
    • Vallon, V.1    Lang, F.2
  • 211
    • 33845487091 scopus 로고    scopus 로고
    • FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells
    • Vieira O.V., Gaus K., Verkade P., Fullekrug J., Vaz W.L., Simons K. FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:18556.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18556
    • Vieira, O.V.1    Gaus, K.2    Verkade, P.3    Fullekrug, J.4    Vaz, W.L.5    Simons, K.6
  • 212
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Vieira O.V., Verkade P., Manninen A., Simons K. FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J. Cell Biol. 2005, 170:521.
    • (2005) J. Cell Biol. , vol.170 , pp. 521
    • Vieira, O.V.1    Verkade, P.2    Manninen, A.3    Simons, K.4
  • 213
    • 0036023427 scopus 로고    scopus 로고
    • Synergistic activation of ENaC by three membrane-bound channel-activating serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid-regulated kinase (Sgk1) in Xenopus Oocytes
    • Vuagniaux G., Vallet V., Jaeger N.F., Hummler E., Rossier B.C. Synergistic activation of ENaC by three membrane-bound channel-activating serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid-regulated kinase (Sgk1) in Xenopus Oocytes. J. Gen. Physiol. 2002, 120:191.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 191
    • Vuagniaux, G.1    Vallet, V.2    Jaeger, N.F.3    Hummler, E.4    Rossier, B.C.5
  • 216
    • 70450128390 scopus 로고    scopus 로고
    • Apical trafficking in epithelial cells: signals, clusters and motors
    • Weisz O.A., Rodriguez-Boulan E. Apical trafficking in epithelial cells: signals, clusters and motors. J. Cell Sci. 2009, 122:4253.
    • (2009) J. Cell Sci. , vol.122 , pp. 4253
    • Weisz, O.A.1    Rodriguez-Boulan, E.2
  • 218
    • 0034965426 scopus 로고    scopus 로고
    • Round-trip ticket: recycling to the plasma membrane requires RME-1
    • Wendland B. Round-trip ticket: recycling to the plasma membrane requires RME-1. Nat. Cell Biol. 2001, 3:E133-E135.
    • (2001) Nat. Cell Biol. , vol.3
    • Wendland, B.1
  • 219
  • 220
    • 27844564821 scopus 로고    scopus 로고
    • Modulation of basal and peptide hormone-stimulated Na transport by membrane cholesterol content in the A6 epithelial cell line
    • West A., Blazer-Yost B. Modulation of basal and peptide hormone-stimulated Na transport by membrane cholesterol content in the A6 epithelial cell line. Cell. Physiol. Biochem. 2005, 16:263.
    • (2005) Cell. Physiol. Biochem. , vol.16 , pp. 263
    • West, A.1    Blazer-Yost, B.2
  • 221
    • 34347221863 scopus 로고    scopus 로고
    • Epithelial sodium channel (ENaC) is multi-ubiquitinated at the cell surface
    • Wiemuth D., Ke Y., Rohlfs M., McDonald F.J. Epithelial sodium channel (ENaC) is multi-ubiquitinated at the cell surface. Biochem. J. 2007, 405:147.
    • (2007) Biochem. J. , vol.405 , pp. 147
    • Wiemuth, D.1    Ke, Y.2    Rohlfs, M.3    McDonald, F.J.4
  • 222
    • 33744548797 scopus 로고    scopus 로고
    • Stimulation of the epithelial sodium channel (ENaC) by cAMP involves putative ERK phosphorylation sites in the C-termini of the channel's beta- and gamma-subunit
    • Yang L.M., Rinke R., Korbmacher C. Stimulation of the epithelial sodium channel (ENaC) by cAMP involves putative ERK phosphorylation sites in the C-termini of the channel's beta- and gamma-subunit. J. Biol. Chem. 2006, 281(15):9859.
    • (2006) J. Biol. Chem. , vol.281 , Issue.15 , pp. 9859
    • Yang, L.M.1    Rinke, R.2    Korbmacher, C.3
  • 223
    • 57349191615 scopus 로고    scopus 로고
    • Single-channel analysis of functional epithelial sodium channel (ENaC) stability at the apical membrane of A6 distal kidney cells
    • Yu L., Helms M.N., Yue Q., Eaton D.C. Single-channel analysis of functional epithelial sodium channel (ENaC) stability at the apical membrane of A6 distal kidney cells. Am. J. Physiol. Renal. Physiol. 2008, 295:F1519-F1527.
    • (2008) Am. J. Physiol. Renal. Physiol. , vol.295
    • Yu, L.1    Helms, M.N.2    Yue, Q.3    Eaton, D.C.4
  • 224
    • 66349083804 scopus 로고    scopus 로고
    • Cargo-mediated regulation of a rapid Rab4-dependent recycling pathway
    • Yudowski G.A., Puthenveedu M.A., Henry A.G., von Z.M. Cargo-mediated regulation of a rapid Rab4-dependent recycling pathway. Mol. Biol. Cell 2009, 20:2774.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2774
    • Yudowski, G.A.1    Puthenveedu, M.A.2    Henry, A.G.3    von, Z.M.4
  • 225
    • 0037023759 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate (PIP2) stimulates epithelial sodium channel activity in A6 cells
    • Yue G., Malik B., Yue G., Eaton D.C. Phosphatidylinositol 4,5-bisphosphate (PIP2) stimulates epithelial sodium channel activity in A6 cells. J. Biol. Chem. 2002, 277:11965.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11965
    • Yue, G.1    Malik, B.2    Yue, G.3    Eaton, D.C.4
  • 227
    • 34547107368 scopus 로고    scopus 로고
    • Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC
    • Zhou R., Patel S.V., Snyder P.M. Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC. J. Biol. Chem. 2007, 282(28):20207.
    • (2007) J. Biol. Chem. , vol.282 , Issue.28 , pp. 20207
    • Zhou, R.1    Patel, S.V.2    Snyder, P.M.3
  • 228
    • 14244254080 scopus 로고    scopus 로고
    • Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation
    • Zhou R., Snyder P.M. Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation. J. Biol. Chem. 2005, 280:4518.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4518
    • Zhou, R.1    Snyder, P.M.2


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