메뉴 건너뛰기




Volumn 7, Issue 1, 2010, Pages 65-70

Role of ubiquitination in Na,K-ATPase regulation during lung injury

Author keywords

Lysosome; Proteasome; Protein degradation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); UBIQUITIN;

EID: 77953257372     PISSN: 15463222     EISSN: 19435665     Source Type: Journal    
DOI: 10.1513/pats.200907-082JS     Document Type: Review
Times cited : (30)

References (80)
  • 1
    • 0015609534 scopus 로고
    • Morphological basis of alveolar-capillary gas exchange
    • Weibel ER. Morphological basis of alveolar-capillary gas exchange. Physiol Rev 1973;53:419-495.
    • (1973) Physiol Rev , vol.53 , pp. 419-495
    • Weibel, E.R.1
  • 2
    • 0001991128 scopus 로고
    • Lung morphometry and models in respiratory physiology
    • New York: Dekker
    • Weibel ER. Lung morphometry and models in respiratory physiology. In: Respiratory physiology: an analytical approach. New York: Dekker; 1989. pp. 1-56.
    • (1989) Respiratory Physiology: An Analytical Approach , pp. 1-56
    • Weibel, E.R.1
  • 4
    • 0034993527 scopus 로고    scopus 로고
    • Alveolar fluid clearance is impaired in the majority of patients with acute lung injury and the acute respiratory distress syndrome
    • Ware LB, Matthay MA. Alveolar fluid clearance is impaired in the majority of patients with acute lung injury and the acute respiratory distress syndrome. Am J Respir Crit Care Med 2001;163:1376-1383. (Pubitemid 32506602)
    • (2001) American Journal of Respiratory and Critical Care Medicine , vol.163 , Issue.6 , pp. 1376-1383
    • Ware, L.B.1    Matthay, M.A.2
  • 5
    • 34447128929 scopus 로고    scopus 로고
    • Alveolar epithelium and Na,K-ATPase in acute lung injury
    • DOI 10.1007/s00134-007-0661-8
    • Vadasz I, Raviv S, Sznajder JI. Alveolar epithelium and Na,K-ATPase in acute lung injury. Intensive Care Med 2007;33:1243-1251. (Pubitemid 47036896)
    • (2007) Intensive Care Medicine , vol.33 , Issue.7 , pp. 1243-1251
    • Vadasz, I.1    Raviv, S.2    Sznajder, J.I.3
  • 6
    • 0034992884 scopus 로고    scopus 로고
    • Alveolar edema must be cleared for the acute respiratory distress syndrome patient to survive
    • Sznajder JI. Alveolar edema must be cleared for the acute respiratory distress syndrome patient to survive. Am J Respir Crit Care Med 2001;163:1293-1294. (Pubitemid 32506584)
    • (2001) American Journal of Respiratory and Critical Care Medicine , vol.163 , Issue.6 , pp. 1293-1294
    • Sznajder, J.I.1
  • 11
    • 0033066855 scopus 로고    scopus 로고
    • Sodium channels in alveolar epithelial cells: Molecular characterization, biophysical properties, and physiological significance
    • DOI 10.1146/annurev.physiol.61.1.627
    • Matalon S, O'Brodovich H. Sodium channels in alveolar epithelial cells: molecular characterization, biophysical properties, and physiological significance. Annu Rev Physiol 1999;61:627-661. (Pubitemid 29143186)
    • (1999) Annual Review of Physiology , vol.61 , pp. 627-661
    • Matalon, S.1    O'Brodovich, H.2
  • 12
    • 0036307827 scopus 로고    scopus 로고
    • Epithelial sodium channel/degenerin family of ion channels: A variety of functions for a shared structure
    • Kellenberger S, Schild L. Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure. Physiol Rev 2002;82:735-767. (Pubitemid 34743337)
    • (2002) Physiological Reviews , vol.82 , Issue.3 , pp. 735-767
    • Kellenberger, S.1    Schild, L.2
  • 13
    • 0036300549 scopus 로고    scopus 로고
    • Lung epithelial fluid transport and the resolution of pulmonary edema
    • Matthay MA, Folkesson HG, Clerici C. Lung epithelial fluid transport and the resolution of pulmonary edema. Physiol Rev 2002;82:569-600. (Pubitemid 34743332)
    • (2002) Physiological Reviews , vol.82 , Issue.3 , pp. 569-600
    • Matthay, M.A.1    Folkesson, H.G.2    Clerici, C.3
  • 14
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • DOI 10.1146/annurev.biochem.71.102201.141218
    • Kaplan JH. Biochemistry of Na,K-ATPase. Annu Rev Biochem 2002;71:511-535. (Pubitemid 34800229)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 15
    • 0032129846 scopus 로고    scopus 로고
    • Nobel lecture. The identification of the sodium pump
    • Skou JC. Nobel lecture. The identification of the sodium pump. Biosci Rep 1998;18:155-169.
    • (1998) Biosci Rep , vol.18 , pp. 155-169
    • Skou, J.C.1
  • 16
    • 0025305262 scopus 로고
    • The sodium pump needs its beta subunit
    • McDonough AA, Geering K, Farley RA. The sodium pump needs its beta subunit. FASEB J 1990;4:1598-1605.
    • (1990) FASEB J , vol.4 , pp. 1598-1605
    • McDonough, A.A.1    Geering, K.2    Farley, R.A.3
  • 17
    • 21344443929 scopus 로고    scopus 로고
    • The Na/K-ATPase and its isozymes: What we have learned using the baculovirus expression system
    • Blanco G. The Na/K-ATPase and its isozymes: what we have learned using the baculovirus expression system. Front Biosci 2005;10:2397-2411. (Pubitemid 40905307)
    • (2005) Frontiers in Bioscience , vol.10 , Issue.SUPPL. 1 , pp. 2397-2411
    • Blanco, G.1
  • 19
    • 58149352846 scopus 로고    scopus 로고
    • Functional roles of Na,K-ATPase subunits
    • Geering K. Functional roles of Na,K-ATPase subunits. Curr Opin Nephrol Hypertens 2008;17:526-532.
    • (2008) Curr Opin Nephrol Hypertens , vol.17 , pp. 526-532
    • Geering, K.1
  • 23
    • 0035839428 scopus 로고    scopus 로고
    • Ion pumps in polarized cells: Sorting and regulation of the Na+, K+- and H+, K+-ATPases
    • Dunbar LA, Caplan MJ. Ion pumps in polarized cells: sorting and regulation of the Na+, K+- and H+, K+-ATPases. J Biol Chem 2001;276:29617-29620.
    • (2001) J Biol Chem , vol.276 , pp. 29617-29620
    • Dunbar, L.A.1    Caplan, M.J.2
  • 24
    • 0038070931 scopus 로고    scopus 로고
    • + pump regulation and skeletal muscle contractility
    • Clausen T. Na+-K+ pump regulation and skeletal muscle contractility. Physiol Rev 2003;83:1269-1324. (Pubitemid 37222273)
    • (2003) Physiological Reviews , vol.83 , Issue.4 , pp. 1269-1324
    • Clausen, T.1
  • 25
    • 27644446481 scopus 로고    scopus 로고
    • The dopamine paradox in lung and kidney epithelia: Sharing the same target but operating different signaling networks
    • DOI 10.1165/rcmb.2005-0297TR
    • Bertorello AM, Sznajder JI. The dopamine paradox in lung and kidney epithelia: sharing the same target but operating different signaling networks. Am J Respir Cell Mol Biol 2005;33:432-437. (Pubitemid 41572685)
    • (2005) American Journal of Respiratory Cell and Molecular Biology , vol.33 , Issue.5 , pp. 432-437
    • Bertorello, A.M.1    Sznajder, J.I.2
  • 30
    • 0034329439 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of an Na+/K+-ATPase beta1 subunit gene improves alveolar fluid clearance and survival in hyperoxic rats
    • Factor P, Dumasius V, Saldias F, Brown LA, Sznajder JI. Adenovirus-mediated transfer of an Na+/K+-ATPase beta1 subunit gene improves alveolar fluid clearance and survival in hyperoxic rats. Hum Gene Ther 2000;11:2231-2242.
    • (2000) Hum Gene Ther , vol.11 , pp. 2231-2242
    • Factor, P.1    Dumasius, V.2    Saldias, F.3    Brown, L.A.4    Sznajder, J.I.5
  • 33
    • 0037192340 scopus 로고    scopus 로고
    • Na,K-ATPase overexpression improves alveolar fluid clearance in a rat model of elevated left atrial pressure
    • DOI 10.1161/hc0402.102848
    • Azzam ZS, Dumasius V, Saldias FJ, Adir Y, Sznajder JI, Factor P. Na,K-ATPase overexpression improves alveolar fluid clearance in a rat model of elevated left atrial pressure. Circulation 2002;105:497-501. (Pubitemid 34141708)
    • (2002) Circulation , vol.105 , Issue.4 , pp. 497-501
    • Azzam, Z.S.1    Dumasius, V.2    Saldias, F.J.3    Adir, Y.4    Sznajder, J.I.5    Factor, P.6
  • 36
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • DOI 10.1016/0006-291X(78)91249-4
    • Ciechanover A, Hod Y, Hershko A. A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun 1978;81:1100-1105. (Pubitemid 8331462)
    • (1978) Biochemical and Biophysical Research Communications , vol.81 , Issue.4 , pp. 1100-1105
    • Ciehanover, A.1    Hod, Y.2    Hershko, A.3
  • 37
    • 0019225640 scopus 로고
    • Characterization of the heatstable polypeptide of the ATP-dependent proteolytic system from reticulocytes
    • Ciechanover A, Elias S, Heller H, Ferber S, Hershko A. Characterization of the heat-stable polypeptide of the atp-dependent proteolytic system from reticulocytes. J Biol Chem 1980;255:7525-7528. (Pubitemid 11239454)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.16 , pp. 7525-7528
    • Ciechanover, A.1    Elias, S.2    Heller, H.3
  • 38
    • 37249026703 scopus 로고    scopus 로고
    • Intracellular protein degradation from a vague idea through the lysosome and the ubiquitin-proteasome system and on to human diseases and drug targeting: Nobel lecture, December 8, 2004
    • DOI 10.1196/annals.1402.078, Skeletal Biology and Medicine, Part A: Aspects of Bone Morphogenesis and Remodeling
    • Ciechanover A. Intracellular protein degradation from a vague idea through the lysosome and the ubiquitin-proteasome system and on to human diseases and drug targeting: Nobel lecture, December 8, 2004. Ann NY Acad Sci 2007;1116:1-28. (Pubitemid 350274349)
    • (2007) Annals of the New York Academy of Sciences , vol.1116 , pp. 1-28
    • Ciechanover, A.1
  • 39
    • 33847705665 scopus 로고    scopus 로고
    • Role of ubiquitin- And Ubl-binding proteins in cell signaling
    • DOI 10.1016/j.ceb.2007.02.002, PII S0955067407000166
    • Kirkin V, Dikic I. Role of ubiquitin- and ubl-binding proteins in cell signaling. Curr Opin Cell Biol 2007;19:199-205. (Pubitemid 46386400)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.2 , pp. 199-205
    • Kirkin, V.1    Dikic, I.2
  • 40
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins
    • DOI 10.1146/annurev.cellbio.19.110701.154617
    • Hicke L, Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 2003;19:141-172. (Pubitemid 37487346)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 41
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • DOI 10.1126/science.1127085
    • Mukhopadhyay D, Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007;315:201-205. (Pubitemid 46166358)
    • (2007) Science , vol.315 , Issue.5809 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 42
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen ZJ, Sun LJ. Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 2009;33:275-286.
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 43
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • DOI 10.1016/S0968-0004(03)00113-0
    • Schwartz DC, Hochstrasser M. A superfamily of protein tags: ubiquitin, sumo and related modifiers. Trends Biochem Sci 2003;28:321-328. (Pubitemid 36776295)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 44
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • DOI 10.1038/35056563
    • Weissman AM. Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2001;2:169-178. (Pubitemid 33675741)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 169-178
    • Weissman, A.M.1
  • 47
    • 24044547036 scopus 로고    scopus 로고
    • Regulating the regulators: Control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli
    • DOI 10.1016/j.molcel.2005.08.017, PII S1097276505015595
    • Gao M, Karin M. Regulating the regulators: control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli. Mol Cell 2005;19:581-593. (Pubitemid 41219435)
    • (2005) Molecular Cell , vol.19 , Issue.5 , pp. 581-593
    • Gao, M.1    Karin, M.2
  • 48
    • 19644384744 scopus 로고    scopus 로고
    • E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation
    • d'Azzo A, Bongiovanni A, Nastasi T. E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. Traffic 2005;6:429-441.
    • (2005) Traffic , vol.6 , pp. 429-441
    • D'Azzo, A.1    Bongiovanni, A.2    Nastasi, T.3
  • 49
    • 36749010218 scopus 로고    scopus 로고
    • The Age of Crosstalk: Phosphorylation, Ubiquitination, and Beyond
    • DOI 10.1016/j.molcel.2007.11.019, PII S1097276507007988
    • Hunter T. The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell 2007;28:730-738. (Pubitemid 350217067)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 730-738
    • Hunter, T.1
  • 51
    • 0029036701 scopus 로고
    • A family of proteins structurally and functionally related to the e6-ap ubiquitinprotein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM. A family of proteins structurally and functionally related to the e6-ap ubiquitinprotein ligase. Proc Natl Acad Sci USA 1995;92:5249.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5249
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 52
    • 0034266806 scopus 로고    scopus 로고
    • Ring finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. Ring finger proteins: mediators of ubiquitin ligase activity. Cell 2000;102:549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 53
    • 0037459172 scopus 로고    scopus 로고
    • U-box proteins as a new family of ubiquitin ligases
    • Hatakeyama S, Nakayama KI. U-box proteins as a new family of ubiquitin ligases. Biochem Biophys Res Commun 2003;302:635-645.
    • (2003) Biochem Biophys Res Commun , vol.302 , pp. 635-645
    • Hatakeyama, S.1    Nakayama, K.I.2
  • 54
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Annu Rev Genet 1996;30:405-439.
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 56
    • 1342272916 scopus 로고    scopus 로고
    • How the cyclin became a cyclin: Regulated proteolysis in the cell cycle
    • DOI 10.1016/S0092-8674(00)80753-9
    • Koepp DM, Harper JW, Elledge SJ. How the cyclin became a cyclin: regulated proteolysis in the cell cycle. Cell 1999;97:431-434. (Pubitemid 29231166)
    • (1999) Cell , vol.97 , Issue.4 , pp. 431-434
    • Koepp, D.M.1    Harper, J.W.2    Elledge, S.J.3
  • 57
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathway
    • DOI 10.1146/annurev.cellbio.14.1.19
    • Bonifacino JS, Weissman AM. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol 1998;14:19-57. (Pubitemid 29001448)
    • (1998) Annual Review of Cell and Developmental Biology , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 58
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J, Sadis S, Haas AL, Finley D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 1995;15:1265-1273.
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 59
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by traf6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ. Activation of the IkappaB kinase complex by traf6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000;103:351-361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 60
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein modifications: Beyond the usual suspects' review series
    • Ikeda F, Dikic I. Atypical ubiquitin chains: new molecular signals. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 2008;9:536-542.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 61
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 2003;72:395-447. (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 62
    • 0037329054 scopus 로고    scopus 로고
    • The role of ubiquitylation in signaling by growth factors: Implications to cancer
    • DOI 10.1016/S1044-579X(02)00097-4, PII S1044579X02000974
    • Shtiegman K, Yarden Y. The role of ubiquitylation in signaling by growth factors: implications to cancer. Semin Cancer Biol 2003;13:29-40. (Pubitemid 36269178)
    • (2003) Seminars in Cancer Biology , vol.13 , Issue.1 , pp. 29-40
    • Shtiegman, K.1    Yarden, Y.2
  • 63
    • 0033523010 scopus 로고    scopus 로고
    • Cblmediated negative regulation of platelet-derived growth factor receptor-dependent cell proliferation: A critical role for cbl tyrosine kinase-binding domain
    • Miyake S, Mullane-Robinson KP, Lill NL, Douillard P, Band H. Cblmediated negative regulation of platelet-derived growth factor receptor-dependent cell proliferation: a critical role for cbl tyrosine kinase-binding domain. J Biol Chem 1999;274:16619-16628.
    • (1999) J Biol Chem , vol.274 , pp. 16619-16628
    • Miyake, S.1    Mullane-Robinson, K.P.2    Lill, N.L.3    Douillard, P.4    Band, H.5
  • 64
    • 0037075606 scopus 로고    scopus 로고
    • The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met
    • DOI 10.1038/416187a
    • Petrelli A, Gilestro GF, Lanzardo S, Comoglio PM, Migone N, Giordano S. The endophilin-cin85-cbl complex mediates ligand-dependent downregulation of c-met. Nature 2002;416:187-190. (Pubitemid 34246477)
    • (2002) Nature , vol.416 , Issue.6877 , pp. 187-190
    • Petrelli, A.1    Gilestro, G.F.2    Lanzardo, S.3    Comoglio, P.M.4    Migone, N.5    Giordano, S.6
  • 66
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • DOI 10.1007/s002320001079
    • Rotin D, Staub O, Haguenauer-Tsapis R. Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/rsp5p family of ubiquitin-protein ligases. J Membr Biol 2000;176:1-17. (Pubitemid 30451985)
    • (2000) Journal of Membrane Biology , vol.176 , Issue.1 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 67
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih SC, Sloper-Mould KE, Hicke L. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J 2000;19:187-198. (Pubitemid 30042701)
    • (2000) EMBO Journal , vol.19 , Issue.2 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 68
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • DOI 10.1038/35056583
    • Hicke L. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2001;2:195-201. (Pubitemid 33675744)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 195-201
    • Hicke, L.1
  • 69
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • DOI 10.1042/BJ20061138
    • Hurley JH, Lee S, Prag G. Ubiquitin-binding domains. Biochem J 2006;399:361-372. (Pubitemid 44672627)
    • (2006) Biochemical Journal , vol.399 , Issue.3 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 70
    • 0030933170 scopus 로고    scopus 로고
    • Ubiquitination of Na,K-ATPase alpha1 and alpha2 subunits
    • DOI 10.1016/S0014-5793(97)00182-8, PII S0014579397001828
    • Coppi MV, Guidotti G. Ubiquitination of Na,K-ATPase alpha1 and alpha2 subunits. FEBS Lett 1997;405:281-284. (Pubitemid 27138492)
    • (1997) FEBS Letters , vol.405 , Issue.3 , pp. 281-284
    • Coppi, M.V.1    Guidotti, G.2
  • 71
    • 0038271589 scopus 로고    scopus 로고
    • +-ATPase through proteasomal and endo- /lysosomal proteolytic pathways
    • Thevenod F, Friedmann JM. Cadmium-mediated oxidative stress in kidney proximal tubule cells induces degradation of Na+/K(+)-ATPase through proteasomal and endo-/lysosomal proteolytic pathways. FASEB J 1999;13:1751-1761. (Pubitemid 29473337)
    • (1999) FASEB Journal , vol.13 , Issue.13 , pp. 1751-1761
    • Thevenod, F.1    Friedmann, J.M.2
  • 72
    • 0037380667 scopus 로고    scopus 로고
    • Hypoxia-induced endocytosis, of Na,K-ATPase in alveolar epithelial cells is mediated by mitochondrial reactive oxygen species and PKC-zeta
    • DOI 10.1172/JCI200316826
    • Dada LA, Chandel NS, Ridge KM, Pedemonte C, Bertorello AM, Sznajder JI. Hypoxia-induced endocytosis of Na,K-ATPase in alveolar epithelial cells is mediated by mitochondrial reactive oxygen species and PKC-zeta. J Clin Invest 2003;111:1057-1064. (Pubitemid 36397482)
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.7 , pp. 1057-1064
    • Dada, L.A.1    Chandel, N.S.2    Ridge, K.M.3    Pedemonte, C.4    Bertorello, A.M.5    Sznajder, J.I.6
  • 73
    • 0033593228 scopus 로고    scopus 로고
    • Dopamine-induced endocytosis of Na,K-ATPase is initiated by phosphorylation of ser-18 in the rat alpha subunit and is responsible for the decreased activity in epithelial cells
    • Chibalin AV, Ogimoto G, Pedemonte CH, Pressley TA, Katz AI, Feraille E, Berggren PO, Bertorello AM. Dopamine-induced endocytosis of Na,K-ATPase is initiated by phosphorylation of ser-18 in the rat alpha subunit and is responsible for the decreased activity in epithelial cells. J Biol Chem 1999;274:1920-1927.
    • (1999) J Biol Chem , vol.274 , pp. 1920-1927
    • Chibalin, A.V.1    Ogimoto, G.2    Pedemonte, C.H.3    Pressley, T.A.4    Katz, A.I.5    Feraille, E.6    Berggren, P.O.7    Bertorello, A.M.8
  • 74
    • 67650032833 scopus 로고    scopus 로고
    • Alpha1-amp-activated protein kinase regulates hypoxiainduced Na,K-ATPase endocytosis via direct phosphorylation of protein kinase c zeta
    • Gusarova GA, Dada LA, Kelly AM, Brodie C, Witters LA, Chandel NS, Sznajder JI. Alpha1-amp-activated protein kinase regulates hypoxiainduced Na,K-ATPase endocytosis via direct phosphorylation of protein kinase c zeta. Mol Cell Biol 2009;29:3455-3464.
    • (2009) Mol Cell Biol , vol.29 , pp. 3455-3464
    • Gusarova, G.A.1    Dada, L.A.2    Kelly, A.M.3    Brodie, C.4    Witters, L.A.5    Chandel, N.S.6    Sznajder, J.I.7
  • 76
    • 34447580910 scopus 로고    scopus 로고
    • Phosphorylation and ubiquitination are necessary for Na,K-ATPase endocytosis during hypoxia
    • DOI 10.1016/j.cellsig.2007.04.013, PII S089865680700126X
    • Dada LA, Welch LC, Zhou G, Ben-Saadon R, Ciechanover A, Sznajder JI. Phosphorylation and ubiquitination are necessary for Na,KATPase endocytosis during hypoxia. Cell Signal 2007;19:1893-1898. (Pubitemid 47081380)
    • (2007) Cellular Signalling , vol.19 , Issue.9 , pp. 1893-1898
    • Dada, L.A.1    Welch, L.C.2    Zhou, G.3    Ben-Saadon, R.4    Ciechanover, A.5    Sznajder, J.I.6
  • 77
  • 79
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • DOI 10.1016/S0092-8674(00)80403-1
    • Skowyra D, Craig KL, Tyers M, Elledge SJ, Harper JW. F-box proteins are receptors that recruit phosphorylated substrates to the scf ubiquitin-ligase complex. Cell 1997;91:209-219. (Pubitemid 27456388)
    • (1997) Cell , vol.91 , Issue.2 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.