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Volumn 138, Issue 3, 2009, Pages 525-536

Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity

Author keywords

SIGNALING

Indexed keywords

ALANINE; MEMBRANE PROTEIN; POTASSIUM CHLORIDE COTRANSPORTER; POTASSIUM CHLORIDE COTRANSPORTER 2; PROTEIN KINASE WNK1; UNCLASSIFIED DRUG;

EID: 68149100251     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2009.05.031     Document Type: Article
Times cited : (245)

References (43)
  • 1
    • 8644288484 scopus 로고    scopus 로고
    • Regulation of K-Cl cotransport: from function to genes
    • Adragna N.C., Di Fulvio M., and Lauf P.K. Regulation of K-Cl cotransport: from function to genes. J. Membr. Biol. 201 (2004) 109-137
    • (2004) J. Membr. Biol. , vol.201 , pp. 109-137
    • Adragna, N.C.1    Di Fulvio, M.2    Lauf, P.K.3
  • 2
    • 0023888250 scopus 로고
    • Vanadate and fluoride effects on Na+-K+-Cl- cotransport in squid giant axon
    • Altamirano A.A., Breitwieser G.E., and Russell J.M. Vanadate and fluoride effects on Na+-K+-Cl- cotransport in squid giant axon. Am. J. Physiol. 254 (1988) C582-C586
    • (1988) Am. J. Physiol. , vol.254
    • Altamirano, A.A.1    Breitwieser, G.E.2    Russell, J.M.3
  • 3
    • 0036719162 scopus 로고    scopus 로고
    • Excitatory actions of GABA during development: the nature of the nurture
    • Ben-Ari Y. Excitatory actions of GABA during development: the nature of the nurture. Nat. Rev. Neurosci. 3 (2002) 728-739
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 728-739
    • Ben-Ari, Y.1
  • 4
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller B., Mueller L.N., Mueller M., Domon B., and Aebersold R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 4 (2007) 231-237
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 5
    • 0023196676 scopus 로고
    • Cell volume, K transport, and cell density in human erythrocytes
    • Brugnara C., and Tosteson D.C. Cell volume, K transport, and cell density in human erythrocytes. Am. J. Physiol. 252 (1987) C269-C276
    • (1987) Am. J. Physiol. , vol.252
    • Brugnara, C.1    Tosteson, D.C.2
  • 6
    • 0022549289 scopus 로고
    • Regulation of erythrocyte cation and water content in sickle cell anemia
    • Brugnara C., Bunn H.F., and Tosteson D.C. Regulation of erythrocyte cation and water content in sickle cell anemia. Science 232 (1986) 388-390
    • (1986) Science , vol.232 , pp. 388-390
    • Brugnara, C.1    Bunn, H.F.2    Tosteson, D.C.3
  • 7
    • 0027231262 scopus 로고
    • Membrane properties of erythrocytes in subjects undergoing multiple blood donations with or without recombinant erythropoietin
    • Brugnara C., Kruskall M.S., and Johnstone R.M. Membrane properties of erythrocytes in subjects undergoing multiple blood donations with or without recombinant erythropoietin. Br. J. Haematol. 84 (1993) 118-130
    • (1993) Br. J. Haematol. , vol.84 , pp. 118-130
    • Brugnara, C.1    Kruskall, M.S.2    Johnstone, R.M.3
  • 8
    • 0037020145 scopus 로고    scopus 로고
    • A regulatory locus of phosphorylation in the N terminus of the Na-K-Cl cotransporter, NKCC1
    • Darman R.B., and Forbush B. A regulatory locus of phosphorylation in the N terminus of the Na-K-Cl cotransporter, NKCC1. J. Biol. Chem. 277 (2002) 37542-37550
    • (2002) J. Biol. Chem. , vol.277 , pp. 37542-37550
    • Darman, R.B.1    Forbush, B.2
  • 10
    • 0042847432 scopus 로고    scopus 로고
    • PASK (proline-alanine-rich STE20-related kinase), a regulatory kinase of the Na-K-Cl cotransporter (NKCC1)
    • Dowd B.F., and Forbush B. PASK (proline-alanine-rich STE20-related kinase), a regulatory kinase of the Na-K-Cl cotransporter (NKCC1). J. Biol. Chem. 278 (2003) 27347-27353
    • (2003) J. Biol. Chem. , vol.278 , pp. 27347-27353
    • Dowd, B.F.1    Forbush, B.2
  • 11
    • 0019222931 scopus 로고
    • Chloride-activated passive potassium transport in human erythrocytes
    • Dunham P.B., Stewart G.W., and Ellory J.C. Chloride-activated passive potassium transport in human erythrocytes. Proc. Natl. Acad. Sci. USA 77 (1980) 1711-1715
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1711-1715
    • Dunham, P.B.1    Stewart, G.W.2    Ellory, J.C.3
  • 12
    • 0025276708 scopus 로고
    • Sickle cell hemoglobin polymerization
    • Eaton W.A., and Hofrichter J. Sickle cell hemoglobin polymerization. Adv. Protein Chem. 40 (1990) 63-279
    • (1990) Adv. Protein Chem. , vol.40 , pp. 63-279
    • Eaton, W.A.1    Hofrichter, J.2
  • 13
    • 28744450567 scopus 로고    scopus 로고
    • Modulation of GABAergic transmission by activity via postsynaptic Ca2+-dependent regulation of KCC2 function
    • Fiumelli H., Cancedda L., and Poo M.M. Modulation of GABAergic transmission by activity via postsynaptic Ca2+-dependent regulation of KCC2 function. Neuron 48 (2005) 773-786
    • (2005) Neuron , vol.48 , pp. 773-786
    • Fiumelli, H.1    Cancedda, L.2    Poo, M.M.3
  • 14
    • 15544384004 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters
    • Gamba G. Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters. Physiol. Rev. 85 (2005) 423-493
    • (2005) Physiol. Rev. , vol.85 , pp. 423-493
    • Gamba, G.1
  • 15
    • 34250785553 scopus 로고    scopus 로고
    • A single binding motif is required for SPAK activation of the Na-K-2Cl cotransporter
    • Gagnon K.B., England R., and Delpire E. A single binding motif is required for SPAK activation of the Na-K-2Cl cotransporter. Cell. Physiol. Biochem. 20 (2007) 131-142
    • (2007) Cell. Physiol. Biochem. , vol.20 , pp. 131-142
    • Gagnon, K.B.1    England, R.2    Delpire, E.3
  • 16
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites
    • Gnad F., Ren S., Cox J., Olsen J.V., Macek B., Oroshi M., and Mann M. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 8 (2007) R250
    • (2007) Genome Biol. , vol.8
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4    Macek, B.5    Oroshi, M.6    Mann, M.7
  • 17
    • 0033854727 scopus 로고    scopus 로고
    • The Na-K-Cl cotransporter of secretory epithelia
    • Haas M., and Forbush III B. The Na-K-Cl cotransporter of secretory epithelia. Annu. Rev. Physiol. 62 (2000) 515-534
    • (2000) Annu. Rev. Physiol. , vol.62 , pp. 515-534
    • Haas, M.1    Forbush III, B.2
  • 18
    • 0034990498 scopus 로고    scopus 로고
    • Disruption of KCC2 reveals an essential role of K-Cl cotransport already in early synaptic inhibition
    • Hübner C.A., Stein V., Hermans-Borgmeyer I., Meyer T., Ballanyi K., and Jentsch T.J. Disruption of KCC2 reveals an essential role of K-Cl cotransport already in early synaptic inhibition. Neuron 30 (2001) 515-524
    • (2001) Neuron , vol.30 , pp. 515-524
    • Hübner, C.A.1    Stein, V.2    Hermans-Borgmeyer, I.3    Meyer, T.4    Ballanyi, K.5    Jentsch, T.J.6
  • 19
    • 0026080491 scopus 로고
    • Okadaic acid inhibition of KCl cotransport. Evidence that protein dephosphorylation is necessary for activation of transport by either cell swelling or N-ethylmaleimide
    • Jennings M.L., and Schulz R.K. Okadaic acid inhibition of KCl cotransport. Evidence that protein dephosphorylation is necessary for activation of transport by either cell swelling or N-ethylmaleimide. J. Gen. Physiol. 97 (1991) 799-817
    • (1991) J. Gen. Physiol. , vol.97 , pp. 799-817
    • Jennings, M.L.1    Schulz, R.K.2
  • 20
    • 33846936180 scopus 로고    scopus 로고
    • Urea stimulation of KCl cotransport induces abnormal volume reduction in sickle reticulocytes
    • Joiner C.H., Rettig R.K., Jiang M., Risinger M., and Franco R.S. Urea stimulation of KCl cotransport induces abnormal volume reduction in sickle reticulocytes. Blood 109 (2007) 1728-1735
    • (2007) Blood , vol.109 , pp. 1728-1735
    • Joiner, C.H.1    Rettig, R.K.2    Jiang, M.3    Risinger, M.4    Franco, R.S.5
  • 23
    • 35649026880 scopus 로고    scopus 로고
    • Direct protein kinase C-dependent phosphorylation regulates the cell surface stability and activity of the potassium chloride cotransporter KCC2
    • Lee H.H., Walker J.A., Williams J.R., Goodier R.J., Payne J.A., and Moss S.J. Direct protein kinase C-dependent phosphorylation regulates the cell surface stability and activity of the potassium chloride cotransporter KCC2. J. Biol. Chem. 282 (2007) 29777-29784
    • (2007) J. Biol. Chem. , vol.282 , pp. 29777-29784
    • Lee, H.H.1    Walker, J.A.2    Williams, J.R.3    Goodier, R.J.4    Payne, J.A.5    Moss, S.J.6
  • 24
    • 12844273669 scopus 로고    scopus 로고
    • Ion transport pathology in the mechanism of sickle cell dehydration
    • Lew V.L., and Bookchin R.M. Ion transport pathology in the mechanism of sickle cell dehydration. Physiol. Rev. 85 (2005) 179-200
    • (2005) Physiol. Rev. , vol.85 , pp. 179-200
    • Lew, V.L.1    Bookchin, R.M.2
  • 26
    • 0026465685 scopus 로고
    • The Na-K-Cl cotransport protein of shark rectal gland. II. Regulation by direct phosphorylation
    • Lytle C., and Forbush III B. The Na-K-Cl cotransport protein of shark rectal gland. II. Regulation by direct phosphorylation. J. Biol. Chem. 267 (1992) 25438-25443
    • (1992) J. Biol. Chem. , vol.267 , pp. 25438-25443
    • Lytle, C.1    Forbush III, B.2
  • 27
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., and Mann M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1 (2002) 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 28
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 29
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin J.C., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 30
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse M.W., Uitto P.M., Hilhorst M.J., Ooms B., and Heck A.J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76 (2004) 3935-3943
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 31
    • 0030723081 scopus 로고    scopus 로고
    • Expression of the Na-K-2Cl cotransporter is developmentally regulated in postnatal rat brains: a possible mechanism underlying GABA's excitatory role in immature brain
    • Plotkin M.D., Snyder E.Y., Hebert S.C., and Delpire E. Expression of the Na-K-2Cl cotransporter is developmentally regulated in postnatal rat brains: a possible mechanism underlying GABA's excitatory role in immature brain. J. Neurobiol. 33 (1997) 781-795
    • (1997) J. Neurobiol. , vol.33 , pp. 781-795
    • Plotkin, M.D.1    Snyder, E.Y.2    Hebert, S.C.3    Delpire, E.4
  • 36
    • 33644938234 scopus 로고    scopus 로고
    • Ste20-type kinases: evolutionarily conserved regulators of ion transport and cell volume
    • Strange K., Denton J., and Nehrke K. Ste20-type kinases: evolutionarily conserved regulators of ion transport and cell volume. Physiology (Bethesda) 21 (2006) 61-68
    • (2006) Physiology (Bethesda) , vol.21 , pp. 61-68
    • Strange, K.1    Denton, J.2    Nehrke, K.3
  • 37
    • 0024601095 scopus 로고
    • Activity-dependent disinhibition. II. Effects of extracellular potassium, furosemide, and membrane potential on ECl- in hippocampal CA3 neurons
    • Thompson S.M., and Gähwiler B.H. Activity-dependent disinhibition. II. Effects of extracellular potassium, furosemide, and membrane potential on ECl- in hippocampal CA3 neurons. J. Neurophysiol. 61 (1989) 512-523
    • (1989) J. Neurophysiol. , vol.61 , pp. 512-523
    • Thompson, S.M.1    Gähwiler, B.H.2
  • 38
    • 33745530924 scopus 로고    scopus 로고
    • Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1
    • Vitari A.C., Thastrup J., Rafiqi F.H., Deak M., Morrice N.A., Karlsson H.K., and Alessi D.R. Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1. Biochem. J. 397 (2006) 223-231
    • (2006) Biochem. J. , vol.397 , pp. 223-231
    • Vitari, A.C.1    Thastrup, J.2    Rafiqi, F.H.3    Deak, M.4    Morrice, N.A.5    Karlsson, H.K.6    Alessi, D.R.7
  • 39
    • 0030976458 scopus 로고    scopus 로고
    • GABA in the mammalian suprachiasmatic nucleus and its role in diurnal rhythmicity
    • Wagner S., Castel M., Gainer H., and Yarom Y. GABA in the mammalian suprachiasmatic nucleus and its role in diurnal rhythmicity. Nature 387 (1997) 598-603
    • (1997) Nature , vol.387 , pp. 598-603
    • Wagner, S.1    Castel, M.2    Gainer, H.3    Yarom, Y.4
  • 41
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
    • Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., and White F.M. Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc. Natl. Acad. Sci. USA 104 (2007) 5860-5865
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 42
    • 0034595634 scopus 로고    scopus 로고
    • WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II
    • Xu B., English J.M., Wilsbacher J.L., Stippec S., Goldsmith E.J., and Cobb M.H. WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II. J. Biol. Chem. 275 (2000) 16795-16801
    • (2000) J. Biol. Chem. , vol.275 , pp. 16795-16801
    • Xu, B.1    English, J.M.2    Wilsbacher, J.L.3    Stippec, S.4    Goldsmith, E.J.5    Cobb, M.H.6
  • 43
    • 3242683426 scopus 로고    scopus 로고
    • Cl- uptake promoting depolarizing GABA actions in immature rat neocortical neurones is mediated by NKCC1
    • Yamada J., Okabe A., Toyoda H., Kilb W., Luhmann H.J., and Fukuda A. Cl- uptake promoting depolarizing GABA actions in immature rat neocortical neurones is mediated by NKCC1. J. Physiol. 557 (2004) 829-841
    • (2004) J. Physiol. , vol.557 , pp. 829-841
    • Yamada, J.1    Okabe, A.2    Toyoda, H.3    Kilb, W.4    Luhmann, H.J.5    Fukuda, A.6


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