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Volumn 287, Issue 21, 2012, Pages 17308-17317

Loop diuretic and ion-binding residues revealed by scanning mutagenesis of transmembrane helix 3 (TM3) of Na-K-Cl cotransporter (NKCC1)

Author keywords

[No Author keywords available]

Indexed keywords

EPITHELIAL SALTS; EXTRACELLULAR; FUROSEMIDES; HOMOLOGY MODELS; ION TRANSLOCATION; ION-BINDING; METHANETHIOSULFONATE; ORGANOCATIONS; POLYAMINES; STRUCTURAL HOMOLOGY; SUBSTITUTION EFFECT; TRANSLOCATION PATHWAY; TRANSMEMBRANE HELICES;

EID: 84861210254     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.356014     Document Type: Article
Times cited : (66)

References (39)
  • 1
    • 0036193948 scopus 로고    scopus 로고
    • Human and murine phenotypes associated with defects in cation-chloride cotransport
    • DOI 10.1146/annurev.physiol.64.081501.155847
    • Delpire, E., and Mount, D. B. (2002) Human and murine phenotypes associated with defects in cation-chloride cotransport. Annu. Rev. Physiol. 64, 803-843 (Pubitemid 34259250)
    • (2002) Annual Review of Physiology , vol.64 , pp. 803-843
    • Delpire, E.1    Mount, D.B.2
  • 3
    • 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. (2002) A regulatory locus of phosphorylation in the N terminus of the Na-K-Cl cotransporter, NKCC1. J. Biol. Chem. 277, 37542-37550
    • (2002) J. Biol. Chem. , vol.277 , pp. 37542-37550
    • Darman, R.B.1    Forbush, B.2
  • 6
    • 41449101925 scopus 로고    scopus 로고
    • Intramolecular and intermolecular fluorescence resonance energy transfer in fluorescent protein-tagged Na-K-Cl cotransporter (NKCC1): Sensitivity to regulatory conformational change and cell volume
    • Pedersen, M., Carmosino, M., and Forbush, B. (2008) Intramolecular and intermolecular fluorescence resonance energy transfer in fluorescent protein-tagged Na-K-Cl cotransporter (NKCC1): sensitivity to regulatory conformational change and cell volume. J. Biol. Chem. 283, 2663-2674
    • (2008) J. Biol. Chem. , vol.283 , pp. 2663-2674
    • Pedersen, M.1    Carmosino, M.2    Forbush, B.3
  • 9
    • 84855849454 scopus 로고    scopus 로고
    • Regulatory activation is accompanied by movement in the C terminus of the Na-K-Cl cotransporter (NKCC1)
    • Monette, M. Y., and Forbush, B. (2012) Regulatory activation is accompanied by movement in the C terminus of the Na-K-Cl cotransporter (NKCC1). J. Biol. Chem. 287, 2210-2220
    • (2012) J. Biol. Chem. , vol.287 , pp. 2210-2220
    • Monette, M.Y.1    Forbush, B.2
  • 10
    • 0031742954 scopus 로고    scopus 로고
    • Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in ion transport and bumetanide binding
    • DOI 10.1085/jgp.112.5.549
    • Isenring, P., Jacoby, S. C., Chang, J., and Forbush, B. (1998) Mutagenic mapping of the Na-K-Cl cotransporter for domains involved in ion transport and bumetanide binding. J. Gen. Physiol. 112, 549-558 (Pubitemid 28518954)
    • (1998) Journal of General Physiology , vol.112 , Issue.5 , pp. 549-558
    • Isenring, P.1    Jacoby, S.C.2    Chang, J.3    Forbush III, B.4
  • 11
    • 0037088671 scopus 로고    scopus 로고
    • Spatially distributed alternative splice variants of the renal Na-K-Cl cotransporter exhibit dramatically different affinities for the transported ions
    • DOI 10.1074/jbc.C200021200
    • Giménez, I., Isenring, P., and Forbush, B. (2002) Spatially distributed alternative splice variants of the renal Na-K-Cl cotransporter exhibit dramatically different affinities for the transported ions. J. Biol. Chem. 277, 8767-8770 (Pubitemid 34952940)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8767-8770
    • Gimenez, I.1    Isenring, P.2    Forbush, B.3
  • 16
    • 76749095057 scopus 로고    scopus 로고
    • Mechanism of substrate recognition and transport by an amino acid antiporter
    • Gao, X., Zhou, L., Jiao, X., Lu, F., Yan, C., Zeng, X., Wang, J., and Shi, Y. (2010) Mechanism of substrate recognition and transport by an amino acid antiporter. Nature 463, 828-832
    • (2010) Nature , vol.463 , pp. 828-832
    • Gao, X.1    Zhou, L.2    Jiao, X.3    Lu, F.4    Yan, C.5    Zeng, X.6    Wang, J.7    Shi, Y.8
  • 19
    • 78650397484 scopus 로고    scopus 로고
    • A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe
    • Khafizov, K., Staritzbichler, R., Stamm, M., and Forrest, L. R. (2010) A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe. Biochemistry 49, 10702-10713
    • (2010) Biochemistry , vol.49 , pp. 10702-10713
    • Khafizov, K.1    Staritzbichler, R.2    Stamm, M.3    Forrest, L.R.4
  • 20
    • 57349168590 scopus 로고    scopus 로고
    • Exon loss accounts for differential sorting of Na-K-Cl cotransporters in polarized epithelial cells
    • Carmosino, M., Giménez, I., Caplan, M., and Forbush, B. (2008) Exon loss accounts for differential sorting of Na-K-Cl cotransporters in polarized epithelial cells. Mol. Biol. Cell 19, 4341-4351
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4341-4351
    • Carmosino, M.1    Giménez, I.2    Caplan, M.3    Forbush, B.4
  • 21
    • 0029188965 scopus 로고
    • Distribution and diversity of Na-K-Cl cotransport proteins: A study with monoclonal antibodies
    • Lytle, C., Xu, J. C., Biemesderfer, D., and Forbush, B., 3rd (1995) Distribution and diversity of Na-K-Cl cotransport proteins: a study with monoclonal antibodies. Am. J. Physiol. 269, C1496-1505
    • (1995) Am. J. Physiol. , vol.269
    • Lytle, C.1    Xu, J.C.2    Biemesderfer, D.3    Forbush III, B.4
  • 22
    • 79954488893 scopus 로고    scopus 로고
    • Rare mutations in the human Na-K-Cl cotransporter (NKCC2) associated with lower blood pressure exhibit impaired processing and transport function
    • Monette, M. Y., Rinehart, J., Lifton, R. P., and Forbush, B. (2011) Rare mutations in the human Na-K-Cl cotransporter (NKCC2) associated with lower blood pressure exhibit impaired processing and transport function. Am. J. Physiol. Renal Physiol. 300, F840-847
    • (2011) Am. J. Physiol. Renal Physiol. , vol.300
    • Monette, M.Y.1    Rinehart, J.2    Lifton, R.P.3    Forbush, B.4
  • 23
    • 35148879961 scopus 로고    scopus 로고
    • Ibogaine, a noncompetitive inhibitor of serotonin transport, acts by stabilizing the cytoplasm-facing state of the transporter
    • DOI 10.1074/jbc.M704456200
    • Jacobs, M. T., Zhang, Y. W., Campbell, S. D., and Rudnick, G. (2007) Ibogaine, a noncompetitive inhibitor of serotonin transport, acts by stabilizing the cytoplasm-facing state of the transporter. J. Biol. Chem. 282, 29441-29447 (Pubitemid 350043359)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29441-29447
    • Jacobs, M.T.1    Zhang, Y.-W.2    Campbell, S.D.3    Rudnick, G.4
  • 24
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 25
    • 35648999092 scopus 로고    scopus 로고
    • Fold assessment for comparative protein structure modeling
    • DOI 10.1110/ps.072895107
    • Melo, F., and Sali, A. (2007) Fold assessment for comparative protein structure modeling. Protein Sci. 16, 2412-2426 (Pubitemid 350036748)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2412-2426
    • Melo, F.1    Sali, A.2
  • 26
    • 17044400916 scopus 로고    scopus 로고
    • Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels
    • Silberberg, S. D., Chang, T. H., and Swartz, K. J. (2005) Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels. J. Gen. Physiol. 125, 347-359
    • (2005) J. Gen. Physiol. , vol.125 , pp. 347-359
    • Silberberg, S.D.1    Chang, T.H.2    Swartz, K.J.3
  • 27
    • 34250305147 scopus 로고    scopus 로고
    • The residues determining differences in ion affinities among the alternative splice variants F, A, and B of the mammalian renal Na-K-Cl cotransporter (NKCC2)
    • DOI 10.1074/jbc.M610780200
    • Giménez, I., and Forbush, B. (2007) The residues determining differences in ion affinities among the alternative splice variants F, A, and B of the mammalian renal Na-K-Cl cotransporter (NKCC2). J. Biol. Chem. 282, 6540-6547 (Pubitemid 47100870)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6540-6547
    • Gimenez, I.1    Forbush, B.2
  • 28
    • 0031913416 scopus 로고    scopus 로고
    • A model of Na-K-2Cl cotransport based on ordered ion binding and glide symmetry
    • Lytle, C., McManus, T. J., and Haas, M. (1998) A model of Na-K-2Cl cotransport based on ordered ion binding and glide symmetry. Am. J. Physiol. 274, C299-309
    • (1998) Am. J. Physiol. , vol.274
    • Lytle, C.1    McManus, T.J.2    Haas, M.3
  • 29
    • 0020643069 scopus 로고
    • [3H]Bumetanide binding to membranes isolated from dog kidney outer medulla: Relationship to the Na,K,Cl co-transport system
    • Forbush, B., 3rd, and Palfrey, H. C. (1983) [3H]Bumetanide binding to membranes isolated from dog kidney outer medulla: relationship to the Na,K,Cl co-transport system. J. Biol. Chem. 258, 11787-11792
    • (1983) J. Biol. Chem. , vol.258 , pp. 11787-11792
    • Forbush III, B.1    Palfrey, H.C.2
  • 30
    • 0029025044 scopus 로고
    • - co-transporter: Evidence for an intracellular anion modifier site
    • - co-transporter: evidence for an intracellular anion modifier site. Biochem. J. 309, 637-642
    • (1995) Biochem. J. , vol.309 , pp. 637-642
    • Moore, M.L.1    George, J.N.2    Turner, R.J.3
  • 31
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: A mechanism for ion-coupled solute flux by symmetrical transporters
    • Forrest, L. R., and Rudnick, G. (2009) The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters. Physiology 24, 377-386
    • (2009) Physiology , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 34
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy, H., and Gouaux, E. (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481, 469-474
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 35
    • 0022929861 scopus 로고
    • 3H]Bumetanide binding to duck red cells: Correlation with inhibition of (Na + K + 2Cl) co-transport
    • 3H]Bumetanide binding to duck red cells: correlation with inhibition of (Na + K + 2Cl) co-transport. J. Biol. Chem. 261, 8434-8441
    • (1986) J. Biol. Chem. , vol.261 , pp. 8434-8441
    • Haas, M.1    Forbush III, B.2
  • 36
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • Singh, S. K., Piscitelli, C. L., Yamashita, A., and Gouaux, E. (2008) A competitive inhibitor traps LeuT in an open-to-out conformation. Science 322, 1655-1661
    • (2008) Science , vol.322 , pp. 1655-1661
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 37
    • 0018757033 scopus 로고
    • Mechanism of imipramine inhibition of platelet 5-hydroxytryptamine transport
    • Talvenheimo, J., Nelson, P. J., and Rudnick, G. (1979) Mechanism of imipramine inhibition of platelet 5-hydroxytryptamine transport. J. Biol. Chem. 254, 4631-4635 (Pubitemid 9203493)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.11 , pp. 4631-4635
    • Talvenheimo, J.1    Nelson, P.J.2    Rudnick, G.3
  • 38
    • 78651255888 scopus 로고    scopus 로고
    • +/glucose cotransporter (SGLT1) turnover rate using the ion-trap technique
    • +/glucose cotransporter (SGLT1) turnover rate using the ion-trap technique. Biophys. J. 100, 52-59
    • (2011) Biophys. J. , vol.100 , pp. 52-59
    • Longpré, J.P.1    Lapointe, J.Y.2
  • 39
    • 77951620942 scopus 로고    scopus 로고
    • Transient currents in the glycine cotransporter GlyT1 reveal different steps in transport mechanism
    • Cherubino, F., Bossi, E., Miszner, A., Ghezzi, C., and Peres, A. (2010) Transient currents in the glycine cotransporter GlyT1 reveal different steps in transport mechanism. J. Mol. Neurosci. 41, 243-251
    • (2010) J. Mol. Neurosci. , vol.41 , pp. 243-251
    • Cherubino, F.1    Bossi, E.2    Miszner, A.3    Ghezzi, C.4    Peres, A.5


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