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Volumn 64, Issue 5, 2003, Pages 1733-1745

PDZK1: I. A major scaffolder in brush borders of proximal tubular cells

Author keywords

CFEX; D AKAP2; MAP17; NaPi I; NaPi IIa; PDZ proteins; PDZK1, NHERF 1; Renal transport of phosphate; URAT1; Yeast two hybrid

Indexed keywords

CARRIER PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; ORGANIC CATION TRANSPORTER; PROTEIN PDZK1; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

EID: 10744227996     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1523-1755.2003.00266.x     Document Type: Article
Times cited : (164)

References (77)
  • 3
    • 0033775213 scopus 로고    scopus 로고
    • Proximal tubular phosphate reabsorption: Molecular mechanisms
    • MURER H, HERNANDO N, FORSTER I, BIBER J: Proximal tubular phosphate reabsorption: Molecular mechanisms. Physiol Rev 80: 1373-1409, 2000
    • (2000) Physiol Rev , vol.80 , pp. 1373-1409
    • Murer, H.1    Hernando, N.2    Forster, I.3    Biber, J.4
  • 6
    • 0034995853 scopus 로고    scopus 로고
    • Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK
    • WADE JB, WELLING PA, DONOWITZ M, et al: Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK. Am J Physiol Cell Physiol 280:C192-198, 2001
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Wade, J.B.1    Welling, P.A.2    Donowitz, M.3
  • 8
    • 0035475318 scopus 로고    scopus 로고
    • Expanding the role of NHERF, a PDZ-domain containing protein adapter, to growth regulation
    • VOLTZ JW, WEINMAN EJ, SHENOLIKAR S: Expanding the role of NHERF, a PDZ-domain containing protein adapter, to growth regulation. Oncogene 20:6309-6314, 2001
    • (2001) Oncogene , vol.20 , pp. 6309-6314
    • Voltz, J.W.1    Weinman, E.J.2    Shenolikar, S.3
  • 11
    • 0037143761 scopus 로고    scopus 로고
    • Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting
    • SHENOLIKAR S, VOLTZ JW, MINKOFF CM, et al: Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting. Proc Natl Acad Sci USA 99:11470-11475, 2002
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11470-11475
    • Shenolikar, S.1    Voltz, J.W.2    Minkoff, C.M.3
  • 12
    • 0037315288 scopus 로고    scopus 로고
    • Targeted disruption of the PDZK1 gene by homologous recombination
    • KOCHER O, PAL R, ROBERTS M, et al: Targeted disruption of the PDZK1 gene by homologous recombination. Mol Cell Biol 23:1175-1180, 2003
    • (2003) Mol Cell Biol , vol.23 , pp. 1175-1180
    • Kocher, O.1    Pal, R.2    Roberts, M.3
  • 13
    • 0031883886 scopus 로고    scopus 로고
    • Identification and partial characterization of PDZK1: A novel protein containing PDZ interaction domains
    • KOCHER O, COMELLA N, TOGNAZZI K, BROWN LF: Identification and partial characterization of PDZK1: A novel protein containing PDZ interaction domains. Lab Invest 78:117-125, 1998
    • (1998) Lab Invest , vol.78 , pp. 117-125
    • Kocher, O.1    Comella, N.2    Tognazzi, K.3    Brown, L.F.4
  • 14
    • 0029896232 scopus 로고    scopus 로고
    • Expression of a renal type I sodium/phosphate transporter (NaPi-I) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions
    • BUSCH AE, SCHUSTER A, WALDEGGER S, et al: Expression of a renal type I sodium/phosphate transporter (NaPi-I) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions. Proc Natl Acad Sci USA 93:5347-5351, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5347-5351
    • Busch, A.E.1    Schuster, A.2    Waldegger, S.3
  • 15
    • 0032105462 scopus 로고    scopus 로고
    • i transport are separate functions induced by the expression of NaPi-1 in Xenopus oocytes
    • i transport are separate functions induced by the expression of NaPi-1 in Xenopus oocytes. J Membr Biol 164:71-77, 1998
    • (1998) J Membr Biol , vol.164 , pp. 71-77
    • Broer, S.1    Schuster, A.2    Wagner, C.A.3
  • 16
    • 0032160713 scopus 로고    scopus 로고
    • Hepatic sinusoidal membrane transport of anionic drugs mediated by anion transporter Npt1
    • YABUUCHI H, TAMAI I, MORITA K, et al: Hepatic sinusoidal membrane transport of anionic drugs mediated by anion transporter Npt1. J Pharmacol Exp Ther 286:1391-1396, 1998
    • (1998) J Pharmacol Exp Ther , vol.286 , pp. 1391-1396
    • Yabuuchi, H.1    Tamai, I.2    Morita, K.3
  • 17
    • 0242396687 scopus 로고    scopus 로고
    • Getting more from the two-hybrid system: N-terminal fusions to LexA are efficient and sensitive baits for two-hybrid studies
    • BÉRANGER F, ARESTA S, DE GUNZBURG J, CAMONIS J: Getting more from the two-hybrid system: N-terminal fusions to LexA are efficient and sensitive baits for two-hybrid studies. Nucleic Acids Res 25:2035-2036, 1997
    • (1997) Nucleic Acids Res , vol.25 , pp. 2035-2036
    • Béranger, F.1    Aresta, S.2    De Gunzburg, J.3    Camonis, J.4
  • 18
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • VOJTEK AB, HOLLENBERG SM, COOPER JA: Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214, 1993
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 20
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • GROSSMAN TH, KAWASAKI ES, PUNREDDY SR, OSBURNE MS: Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209:95-103, 1998
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 21
    • 0032509329 scopus 로고    scopus 로고
    • High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D
    • FORRER P, JAUSSI R: High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D. Gene 224:45-52, 1998
    • (1998) Gene , vol.224 , pp. 45-52
    • Forrer, P.1    Jaussi, R.2
  • 23
    • 0034704135 scopus 로고    scopus 로고
    • Molecular and functional characterization of organic cation/carnitine transporter family in mice
    • TAMAI I, OHASHI R, NEZU JI, et al: Molecular and functional characterization of organic cation/carnitine transporter family in mice. J Biol Chem 275:40064-40072, 2000
    • (2000) J Biol Chem , vol.275 , pp. 40064-40072
    • Tamai, I.1    Ohashi, R.2    Nezu, J.I.3
  • 24
    • 0033961249 scopus 로고    scopus 로고
    • Caspase 3 cleavage of the Ste20-related kinase SLK releases and activates an apoptosis-inducing kinase domain and an actin-disassembling region
    • SABOURIN LA, TAMAI K, SEALE P, et al: Caspase 3 cleavage of the Ste20-related kinase SLK releases and activates an apoptosis-inducing kinase domain and an actin-disassembling region. Mol Cell Biol 20:684-696, 2000
    • (2000) Mol Cell Biol , vol.20 , pp. 684-696
    • Sabourin, L.A.1    Tamai, K.2    Seale, P.3
  • 25
    • 0028335037 scopus 로고
    • i cotransport in rat kidney: Localization by RT-PCR and immunohistochemistry
    • i cotransport in rat kidney: localization by RT-PCR and immunohistochemistry. Am J Physiol 266:F767-774, 1994
    • (1994) Am J Physiol , vol.266
    • Custer, M.1    Lötscher, M.2    Biber, J.3
  • 26
    • 0033514423 scopus 로고    scopus 로고
    • Intramolecular chimeras of the p51 subunit between HIV-1 and FIV reverse transcriptases suggest a stabilizing function for the p66 subunit in the heterodimeric enzyme
    • TASARA T, AMACKER M, HÜBSCHER U: Intramolecular chimeras of the p51 subunit between HIV-1 and FIV reverse transcriptases suggest a stabilizing function for the p66 subunit in the heterodimeric enzyme. Biochemistry 38:1633-1642, 1999
    • (1999) Biochemistry , vol.38 , pp. 1633-1642
    • Tasara, T.1    Amacker, M.2    Hübscher, U.3
  • 27
    • 0035979278 scopus 로고    scopus 로고
    • Identification of a chloride-formate exchanger expressed on the brush border membrane of renal proximal tubule cells
    • KNAUF F, YANG CL, THOMSON RB, et al: Identification of a chloride-formate exchanger expressed on the brush border membrane of renal proximal tubule cells. Proc Natl Acad Sci USA 98:9425-9430, 2001
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9425-9430
    • Knauf, F.1    Yang, C.L.2    Thomson, R.B.3
  • 28
    • 0034810502 scopus 로고    scopus 로고
    • Cloning, expression, and ontogeny of mouse organic anion-transporting polypeptide-5, a kidney-specific organic anion transporter
    • CHOUDHURI S, OGURA K, KLAASSEN CD: Cloning, expression, and ontogeny of mouse organic anion-transporting polypeptide-5, a kidney-specific organic anion transporter. Biochem Biophys Res Commun 280:92-98, 2001
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 92-98
    • Choudhuri, S.1    Ogura, K.2    Klaassen, C.D.3
  • 29
    • 0030772953 scopus 로고    scopus 로고
    • Kidney-specific expression of a novel mouse organic cation transporter-like protein
    • MORI K, OGAWA Y, EBIHARA K, et al: Kidney-specific expression of a novel mouse organic cation transporter-like protein. FEBS Lett 417:371-374, 1997
    • (1997) FEBS Lett , vol.417 , pp. 371-374
    • Mori, K.1    Ogawa, Y.2    Ebihara, K.3
  • 30
    • 0037161834 scopus 로고    scopus 로고
    • Molecular identification of a renal urate anion exchanger that regulates blood urate levels
    • ENOMOTO A, KIMURA H, CHAIROUNGDUA A, et al: Molecular identification of a renal urate anion exchanger that regulates blood urate levels. Nature 417:447-452, 2002
    • (2002) Nature , vol.417 , pp. 447-452
    • Enomoto, A.1    Kimura, H.2    Chairoungdua, A.3
  • 32
    • 0030017442 scopus 로고    scopus 로고
    • Identification and partial characterization of a novel membrane-associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth
    • KOCHER O, CHERESH P, LEE SW: Identification and partial characterization of a novel membrane-associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth. Am J Pathol 149:493-500, 1996
    • (1996) Am J Pathol , vol.149 , pp. 493-500
    • Kocher, O.1    Cheresh, P.2    Lee, S.W.3
  • 33
    • 0032738332 scopus 로고    scopus 로고
    • SUMO/sentrin: Protein modifiers regulating important cellular functions
    • KRETZ-REMY C, TANGUAY RM: SUMO/sentrin: Protein modifiers regulating important cellular functions. Biochem Cell Biol 77:299-309, 1999
    • (1999) Biochem Cell Biol , vol.77 , pp. 299-309
    • Kretz-Remy, C.1    Tanguay, R.M.2
  • 34
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • YEH ET, GONG L, KAMITANI T: Ubiquitin-like proteins: New wines in new bottles. Gene 248:1-14, 2000
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 35
    • 0033539894 scopus 로고    scopus 로고
    • Induction of apoptosis by SLK, a Ste20-related kinase
    • SABOURIN LA, RUDNICKI MA: Induction of apoptosis by SLK, a Ste20-related kinase. Oncogene 18:7566-7575, 1999
    • (1999) Oncogene , vol.18 , pp. 7566-7575
    • Sabourin, L.A.1    Rudnicki, M.A.2
  • 36
    • 0030990430 scopus 로고    scopus 로고
    • + exchanger, NHE3, requires an associated regulatory protein
    • + exchanger, NHE3, requires an associated regulatory protein. Proc Natl Acad Sci USA 94:3010-3015, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3010-3015
    • Yun, C.H.1    Oh, S.2    Zizak, M.3
  • 37
    • 0030881687 scopus 로고    scopus 로고
    • D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
    • HUANG LJ, DURICK K, WEINER JA, et al: D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain. Proc Natl Acad Sci USA 94:11184-11189, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11184-11189
    • Huang, L.J.1    Durick, K.2    Weiner, J.A.3
  • 38
    • 0032582378 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • NAGASE T, ISHIKAWA K, SUYAMA M, et al: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res 5:277-286, 1998
    • (1998) DNA Res , vol.5 , pp. 277-286
    • Nagase, T.1    Ishikawa, K.2    Suyama, M.3
  • 39
    • 0142187237 scopus 로고    scopus 로고
    • PDZK1: II. An anchoring site for the PKA-binding protein D-AKAP2 in renal proximal tubular cells
    • GISLER SM, MADJDPOUR C, BACIC D, et al: PDZK1: II. An anchoring site for the PKA-binding protein D-AKAP2 in renal proximal tubular cells. Kidney Int 64:1746-1754, 2003
    • (2003) Kidney Int , vol.64 , pp. 1746-1754
    • Gisler, S.M.1    Madjdpour, C.2    Bacic, D.3
  • 40
    • 0029099062 scopus 로고
    • Expression of NHE-3 in the apical membrane of rat renal proximal tubule and thick ascending limb
    • AMEMIYA M, LOFFING J, LÖTSCHER M, et al: Expression of NHE-3 in the apical membrane of rat renal proximal tubule and thick ascending limb. Kidney Int 48:1206-1215, 1995
    • (1995) Kidney Int , vol.48 , pp. 1206-1215
    • Amemiya, M.1    Loffing, J.2    Lötscher, M.3
  • 41
    • 0028814091 scopus 로고
    • Cloning, genetic mapping, and expression analysis of a mouse renal sodium-dependent phosphate cotransporter
    • CHONG SS, KOZAK CA, LIU L, et al: Cloning, genetic mapping, and expression analysis of a mouse renal sodium-dependent phosphate cotransporter. Am J Physiol 268:F1038-F1045, 1995
    • (1995) Am J Physiol , vol.268
    • Chong, S.S.1    Kozak, C.A.2    Liu, L.3
  • 43
    • 0035943075 scopus 로고    scopus 로고
    • Oligomerization of NHERF-1 and NHERF-2 PDZ domains: Differential regulation by association with receptor carboxyl-termini and by phosphorylation
    • LAU AG, HALL RA: Oligomerization of NHERF-1 and NHERF-2 PDZ domains: differential regulation by association with receptor carboxyl-termini and by phosphorylation. Biochemistry 40:8572-8580, 2001
    • (2001) Biochemistry , vol.40 , pp. 8572-8580
    • Lau, A.G.1    Hall, R.A.2
  • 44
    • 0037077218 scopus 로고    scopus 로고
    • + exchanger isoform 3 in a renal polarized epithelial cell model
    • + exchanger isoform 3 in a renal polarized epithelial cell model. J Biol Chem 277:21480-21488, 2002
    • (2002) J Biol Chem , vol.277 , pp. 21480-21488
    • Bagorda, A.1    Guerra, L.2    Di Sole, F.3
  • 45
    • 0033755880 scopus 로고    scopus 로고
    • + exchanger regulatory factor potentiates receptor activity
    • + exchanger regulatory factor potentiates receptor activity. Mol Cell Biol 20:8352-8363, 2000
    • (2000) Mol Cell Biol , vol.20 , pp. 8352-8363
    • Maudsley, S.1    Zamah, A.M.2    Rahman, N.3
  • 46
    • 0034637561 scopus 로고    scopus 로고
    • Evidence for ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) self-association through PDZ-PDZ interactions
    • FOUASSIER L, YUN CC, FITZ JG, DOCTOR RB: Evidence for ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) self-association through PDZ-PDZ interactions. J Biol Chem 275:25039-25045, 2000
    • (2000) J Biol Chem , vol.275 , pp. 25039-25045
    • Fouassier, L.1    Yun, C.C.2    Fitz, J.G.3    Doctor, R.B.4
  • 47
    • 0035793472 scopus 로고    scopus 로고
    • N-terminal PDZ domain is required for NHERF dimerization
    • SHENOLIKAR S, MINKOFF CM, STEPLOCK DA, et al: N-terminal PDZ domain is required for NHERF dimerization. FEBS Lett 489:233-236, 2001
    • (2001) FEBS Lett , vol.489 , pp. 233-236
    • Shenolikar, S.1    Minkoff, C.M.2    Steplock, D.A.3
  • 48
    • 0034237258 scopus 로고    scopus 로고
    • PDZ domains in synapse assembly and signalling
    • GARNER CC, NASH J, HUGANIR RL: PDZ domains in synapse assembly and signalling. Trends Cell Biol 10:274-280, 2000
    • (2000) Trends Cell Biol , vol.10 , pp. 274-280
    • Garner, C.C.1    Nash, J.2    Huganir, R.L.3
  • 49
    • 0032491428 scopus 로고    scopus 로고
    • The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3
    • LAMPRECHT G, WEINMAN EJ, YUN CH: The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3. J Biol Chem 273:29972-29978, 1998
    • (1998) J Biol Chem , vol.273 , pp. 29972-29978
    • Lamprecht, G.1    Weinman, E.J.2    Yun, C.H.3
  • 50
    • 0032884024 scopus 로고    scopus 로고
    • PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug resistance-associated protein
    • KOCHER O, COMELLA N, GILCHRIST A, et al: PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug resistance-associated protein. Lab Invest 79:1161-1170, 1999
    • (1999) Lab Invest , vol.79 , pp. 1161-1170
    • Kocher, O.1    Comella, N.2    Gilchrist, A.3
  • 51
    • 0037142080 scopus 로고    scopus 로고
    • + exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling
    • + exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling. Nature 417:858-861, 2002
    • (2002) Nature , vol.417 , pp. 858-861
    • Mahon, M.J.1    Donowitz, M.2    Yun, C.C.3    Segre, G.V.4
  • 52
    • 0032935034 scopus 로고    scopus 로고
    • Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations
    • YABUUCHI H, TAMAI I, NEZU J, et al: Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations. J Pharmacol Exp Ther 289:768-773, 1999
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 768-773
    • Yabuuchi, H.1    Tamai, I.2    Nezu, J.3
  • 53
    • 0035853041 scopus 로고    scopus 로고
    • Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein
    • WANG L, SUNAHARA RK, KRUMINS A, et al: Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein. Proc Natl Acad Sci USA 98:3220-3225, 2001
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3220-3225
    • Wang, L.1    Sunahara, R.K.2    Krumins, A.3
  • 54
    • 0035861856 scopus 로고    scopus 로고
    • Classification of PDZ domains
    • BEZPROZVANNY I, MAXIMOV A: Classification of PDZ domains. FEBS Lett 509:457-462, 2001
    • (2001) FEBS Lett , vol.509 , pp. 457-462
    • Bezprozvanny, I.1    Maximov, A.2
  • 55
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • HUNG AY, SHENG M: PDZ domains: Structural modules for protein complex assembly. J Biol Chem 277:5699-5702, 2002
    • (2002) J Biol Chem , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 56
    • 0030772385 scopus 로고    scopus 로고
    • Crystal structure of murine/ human Ubc9 provides insight into the variability of the ubiquitin-conjugating system
    • TONG H, HATEBOER G, PERRAKIS A, et al: Crystal structure of murine/ human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. J Biol Chem 272:21381-21387, 1997
    • (1997) J Biol Chem , vol.272 , pp. 21381-21387
    • Tong, H.1    Hateboer, G.2    Perrakis, A.3
  • 57
    • 0037077265 scopus 로고    scopus 로고
    • Identification of a substrate recognition site on Ubc9
    • LIN D, TATHAM MH, YU B, et al: Identification of a substrate recognition site on Ubc9. J Biol Chem 277:21740-21748, 2002
    • (2002) J Biol Chem , vol.277 , pp. 21740-21748
    • Lin, D.1    Tatham, M.H.2    Yu, B.3
  • 60
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • CAO TT, DEACON HW, RECZEK D, et al: A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature 401:286-290, 1999
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3
  • 61
    • 0036259416 scopus 로고    scopus 로고
    • Physiology and molecular biology of renal carbonic anhydrase
    • SCHWARTZ GJ: Physiology and molecular biology of renal carbonic anhydrase. J Nephrol 15(Suppl 5):S61-S74, 2002
    • (2002) J Nephrol , vol.15 , Issue.5 SUPPL.
    • Schwartz, G.J.1
  • 62
    • 0036259594 scopus 로고    scopus 로고
    • Use of transgenic animals to study renal acid-base transport
    • WANG T, GIEBISCH G, ARONSON PS: Use of transgenic animals to study renal acid-base transport. J Nephrol 15(Suppl 5):S151-S160, 2002
    • (2002) J Nephrol , vol.15 , Issue.5 SUPPL.
    • Wang, T.1    Giebisch, G.2    Aronson, P.S.3
  • 63
    • 0036967547 scopus 로고    scopus 로고
    • Role of the PDZ scaffolding protein in tubule cells in maintenance of polarised function
    • GLYNNE PA, EVANS TJ: Role of the PDZ scaffolding protein in tubule cells in maintenance of polarised function. Exp Nephrol 10:307-312, 2002
    • (2002) Exp Nephrol , vol.10 , pp. 307-312
    • Glynne, P.A.1    Evans, T.J.2
  • 64
    • 0034730330 scopus 로고    scopus 로고
    • Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism to potentiate the chloride channel activity
    • WANG S, YUE H, DERIN RB, et al: Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism to potentiate the chloride channel activity. Cell 103:169-179, 2000
    • (2000) Cell , vol.103 , pp. 169-179
    • Wang, S.1    Yue, H.2    Derin, R.B.3
  • 65
    • 0035970113 scopus 로고    scopus 로고
    • Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction
    • RAGHURAM V, MAK DD, FOSKETT JK: Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction. Proc Natl Acad Sci USA 98:1300-1305, 2001
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1300-1305
    • Raghuram, V.1    Mak, D.D.2    Foskett, J.K.3
  • 66
    • 0034282899 scopus 로고    scopus 로고
    • The PDZ-interacting domain of cystic fibrosis transmembrane conductance regulator is required for functional expression in the apical plasma membrane
    • MOYER BD, DUHAIME M, SHAW C, et al: The PDZ-interacting domain of cystic fibrosis transmembrane conductance regulator is required for functional expression in the apical plasma membrane. J Biol Chem 275:27069-27074, 2000
    • (2000) J Biol Chem , vol.275 , pp. 27069-27074
    • Moyer, B.D.1    Duhaime, M.2    Shaw, C.3
  • 67
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • RECZEK D, BERRYMAN M, BRETSCHER A: Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J Cell Biol 139:169-179, 1997
    • (1997) J Cell Biol , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 68
    • 0033834085 scopus 로고    scopus 로고
    • Signal complex regulation of renal transport proteins: NHERF and regulation of NHE3 by PKA
    • WEINMAN EJ, MINKOFF C, SHENOLIKAR S: Signal complex regulation of renal transport proteins: NHERF and regulation of NHE3 by PKA. Am J Physiol Renal Physiol 279:F393-F399, 2000
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Weinman, E.J.1    Minkoff, C.2    Shenolikar, S.3
  • 69
    • 0034705178 scopus 로고    scopus 로고
    • NHERF associations with sodium-hydrogen exchanger isoform 3 (NHE3) and ezrin are essential for cAMP-mediated phosphorylation and inhibition of NHE3
    • WEINMAN EJ, STEPLOCK D, DONOWITZ M, SHENOLIKAR S: NHERF associations with sodium-hydrogen exchanger isoform 3 (NHE3) and ezrin are essential for cAMP-mediated phosphorylation and inhibition of NHE3. Biochemistry 39:6123-6129, 2000
    • (2000) Biochemistry , vol.39 , pp. 6123-6129
    • Weinman, E.J.1    Steplock, D.2    Donowitz, M.3    Shenolikar, S.4
  • 70
    • 0032736233 scopus 로고    scopus 로고
    • Acute regulation of proximal tubule apical membrane Na/H exchanger NHE-3: Role of phosphorylation, protein trafficking, and regulatory factors
    • MOE OW: Acute regulation of proximal tubule apical membrane Na/H exchanger NHE-3: Role of phosphorylation, protein trafficking, and regulatory factors. J Am Soc Nephrol 10:2412-2425, 1999
    • (1999) J Am Soc Nephrol , vol.10 , pp. 2412-2425
    • Moe, O.W.1
  • 71
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • GIORGINO F, DE ROBERTIS O, LAVIOLA L, et al: The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc Natl Acad Sci USA 97:1125-1130, 2000
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1125-1130
    • Giorgino, F.1    De Robertis, O.2    Laviola, L.3
  • 72
    • 0023730712 scopus 로고
    • Cytoskeleton organization and submembranous interactions in intestinal and renal brush borders
    • COUDRIER E, KERJASCHKI D, LOUVARD D: Cytoskeleton organization and submembranous interactions in intestinal and renal brush borders. Kidney Int 34:309-320, 1988
    • (1988) Kidney Int , vol.34 , pp. 309-320
    • Coudrier, E.1    Kerjaschki, D.2    Louvard, D.3
  • 73
    • 0036570588 scopus 로고    scopus 로고
    • Role of Rho family GTPases in epithelial morphogenesis
    • VAN AELST L, SYMONS M: Role of Rho family GTPases in epithelial morphogenesis. Genes Dev 16:1032-1054, 2002
    • (2002) Genes Dev , vol.16 , pp. 1032-1054
    • Van Aelst, L.1    Symons, M.2
  • 74
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton
    • APODACA G: Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton. Traffic 2:149-159, 2001
    • (2001) Traffic , vol.2 , pp. 149-159
    • Apodaca, G.1
  • 77
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • HILLIER BJ, CHRISTOPHERSON KS, PREHODA KE, et al: Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 284:812-815, 1999
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.