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Mode of action of parathyroid hormone and cyclic adenosine 3′-5′ monophosphate on renal tubular phosphate reabsorption in the dog
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1 Agus ZS, Puschett JB, Senesky D, Goldberg M. Mode of action of parathyroid hormone and cyclic adenosine 3′-5′ monophosphate on renal tubular phosphate reabsorption in the dog. J Clin Invest 1971; 50:617-626.
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Agus, Z.S.1
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0017194399
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Influence of bicarbonate on parathyroid hormone induced changes in fluid reabsorption by the proximal tubule
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+ exchanger
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This paper describes the reconstitution assay that was pivotal for the identification of NHERF as a protein cofactor that mediates PKA-dependent inhibition of NHE3. This assay is likely to remain an important tool for delineating the detailed molecular mechanisms that control NHE3 activity in mammalian tissues
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+ exchanger. J Memb Biol 1988; 101:11-18. This paper describes the reconstitution assay that was pivotal for the identification of NHERF as a protein cofactor that mediates PKA-dependent inhibition of NHE3. This assay is likely to remain an important tool for delineating the detailed molecular mechanisms that control NHE3 activity in mammalian tissues.
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Weinman, E.J.1
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Molecular cloning of the cDNA and promoter sequences for the mouse sodium-hydrogen exchanger regulatory factor (NHE-RF)
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Biochim Biophys Acta
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Weinman, E.J.1
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Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ERM family
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13 Reczek D, Berryman M, Bretscher J. Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ERM family. J Cell Biol 1997; 139:169-179.
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Reczek, D.1
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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
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18
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0032523823
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Structure-function of the Na/H exchanger regulatory factor (NHE-RF)
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Using recombinant NHERF and NERF fragments expressed in bacteria, this study and [16•,20•] firmly established that NHERF alone was required for NHE3 regulation in vitro and accompanying mutagenesis studies provided evidence that NHERF phosphorylation may contribute to function of this protein as an NHE3 regulator
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18 Weinman EJ, Steplock D, Tate K, Hall RA, Spurney RF, Shenolikar S. Structure-function of the Na/H exchanger regulatory factor (NHE-RF). J Clin Invest 1998; 101:2199-2206. Using recombinant NHERF and NERF fragments expressed in bacteria, this study and [16•,20•] firmly established that NHERF alone was required for NHE3 regulation in vitro and accompanying mutagenesis studies provided evidence that NHERF phosphorylation may contribute to function of this protein as an NHE3 regulator.
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Weinman, E.J.1
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Shenolikar, S.6
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0032491428
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The role of NHERF and E3KARP in the cAMP-mediated Inhibition of NHE3
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20 Lamprecht G, Weinman EJ, Yun C-HC. The role of NHERF and E3KARP in the cAMP-mediated Inhibition of NHE3. J Biol Chem 1998; 273:29972-29978. See [25•].
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Lamprecht, G.1
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0031033178
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Ezrin is a cyclic AMP-dependent protein kinase anchoring protein
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21 Dransfield DT, Bradford AJ, Smith J, Martin M, Roy C, Mangeat PH, Goldring JR. Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. EMBO J 1997; 2:35-43.
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Type II cAMP-dependent protein kinase is associated with the rabbit kidney brush border membranes
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24
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0030835610
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A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade
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24 Tsunoda S, Sierralta J, Bodner R, Suzuki E, Becker A, Socolich M, Zucker C. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade. Nature 1997; 388:243-249.
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26
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0030905044
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The human testis determining factor SRY binds a nuclear factor containing PDZ protein interaction domains
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26 Poulat F, Barbara PS, Desclozeaux M, Soullier S, Moniot B, Bonneaud N, et al. The human testis determining factor SRY binds a nuclear factor containing PDZ protein interaction domains. J Biol Chem 1997; 272:7167-7172.
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Poulat, F.1
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Bonneaud, N.6
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27
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0032498963
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+ exchange
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2-adrenergic receptor with NHERF allowed for GPCR-mediated signaling without coupling to G-proteins. In addition, these studies raised the possibility of a bimodal regulation of NHE3 by G-protein coupled receptors, sometimes activating and at other times inhibiting antiporter activity in response to agonist
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2-adrenergic receptor with NHERF allowed for GPCR-mediated signaling without coupling to G-proteins. In addition, these studies raised the possibility of a bimodal regulation of NHE3 by G-protein coupled receptors, sometimes activating and at other times inhibiting antiporter activity in response to agonist.
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Hall, R.A.1
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28
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0020329613
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Alpha and beta adrenergic agonists stimulate water absorption in the rat proximal tubule
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28 Weinman EJ, Sansom SC, Knight TF, Senekjian HO. Alpha and beta adrenergic agonists stimulate water absorption in the rat proximal tubule. J Memb Biol 1982; 69:107-111.
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29
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0031890998
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+ exchange, is a common interactor for merlin and ERM (MERM) proteins
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This study expands upon the role of NHERF as an ERM binding protein, indicating that NHERF not only binds to ezrin but also moesin, radixin and merlin. These results establish the paradigm of NHERF as an organizer of these actin cytoskeleton interacting proteins. In addition, the interaction with merlin, the NF2 tumor suppressor, offers the tantalizing possibility that NHERF may play a role in growth regulation
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+ exchange, is a common interactor for merlin and ERM (MERM) proteins. J Biol Chem 1998; 273:1273-1276. This study expands upon the role of NHERF as an ERM binding protein, indicating that NHERF not only binds to ezrin but also moesin, radixin and merlin. These results establish the paradigm of NHERF as an organizer of these actin cytoskeleton interacting proteins. In addition, the interaction with merlin, the NF2 tumor suppressor, offers the tantalizing possibility that NHERF may play a role in growth regulation.
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Murthy, A.1
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0032541057
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The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
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30 Reczek D, Bretscher A. The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule. J Biol Chem 1998; 273:18452-18458.
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Reczek, D.1
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31
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0030725928
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Identification of a new gene product (diphor-1) regulated by dietary phosphate
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Using serially deleted fragments, the authors map the NHERF ERM binding domain to the 38 c-terminal residues. NHERF binding is disrupted by the ezrin c-terminal ERM association domain suggesting that NHERF binds only to activated ezrin, indicating physiological regulation for this interaction
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31 Custer M, Spindler B, Verrey F, Murer H, Biber J. Identification of a new gene product (diphor-1) regulated by dietary phosphate. Am J Physiol 1997; 273:F801-F806. Using serially deleted fragments, the authors map the NHERF ERM binding domain to the 38 c-terminal residues. NHERF binding is disrupted by the ezrin c-terminal ERM association domain suggesting that NHERF binds only to activated ezrin, indicating physiological regulation for this interaction.
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Custer, M.1
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32
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A PDZ domain-containing protein with homology to Diphor-1 maps to human chromosome 1q21
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32 White KE, Biber J, Murer H, Econs MJ. A PDZ domain-containing protein with homology to Diphor-1 maps to human chromosome 1q21. Ann Human Genet 1998; 62:287-290.
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Identification and partial characterization of PDZK1: A novel protein containing PDZ interaction domains
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33 Kocher O, Comella N, Tognazzi K, Brown LF. Identification and partial characterization of PDZK1: a novel protein containing PDZ interaction domains. Lab Invest 1998; 78:117-125.
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Kocher, O.1
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34
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0032080043
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Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
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34 Wang S, Raab RW, Schatz PJ, Guggino WB, Li M. Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett 1998; 427:103-108. See [35•]
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Wang, S.1
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Li, M.5
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35
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0032584744
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An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton
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This study and [25•,34•] demonstrated the direct interaction between NHERF and CFTR, suggesting a broader role for NHERF in cellular ion balance. The formation of this complex may serve to associate the CFTR with regulatory proteins or other channels. Finally since several pathologically contributes to a human disease
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35 Short DB, Trotter KW, Reczek D, Kreda SM, Bretscher A, Boucher RC, et al. An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton. J Biol Chem 1998; 273:19797-19801. This study and [25•,34•] demonstrated the direct interaction between NHERF and CFTR, suggesting a broader role for NHERF in cellular ion balance. The formation of this complex may serve to associate the CFTR with regulatory proteins or other channels. Finally since several pathologically contributes to a human disease.
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Short, D.B.1
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