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Volumn 14, Issue 7, 2003, Pages 1949-1951

Role of PDZ domain-containing proteins and ERM proteins in regulation of renal function and dysfunction

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CARRIER PROTEIN; EZRIN; F ACTIN; MOESIN; PARATHYROID HORMONE; PODOCALYXIN; PROTEIN CAL; PROTEIN CAP70; PROTEIN NHERF 1; PROTEIN NHERF 2; PROTEIN PDZK1; PROTEIN ZO1; RADIXIN; SODIUM PROTON EXCHANGE PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 0038205871     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.ASN.0000078768.86317.31     Document Type: Editorial
Times cited : (10)

References (35)
  • 1
    • 0034644740 scopus 로고    scopus 로고
    • Acute regulation of Na+/H+ exchanger NHE3 by parathyroid hormone via NHE3 phosphorylation and dynamin-dependent endocytosis
    • Collazo R, Fan L, Hu MC, Zhao H, Wiederkehr MR, Moe OW: Acute regulation of Na+/H+ exchanger NHE3 by parathyroid hormone via NHE3 phosphorylation and dynamin-dependent endocytosis. J Biol Chem 275: 31601-31608, 2000
    • (2000) J Biol Chem , vol.275 , pp. 31601-31608
    • Collazo, R.1    Fan, L.2    Hu, M.C.3    Zhao, H.4    Wiederkehr, M.R.5    Moe, O.W.6
  • 3
    • 0036084220 scopus 로고    scopus 로고
    • PTH and DA regulate Na-K ATPase through divergent pathways
    • Khundmiri SJ, Lederer E: PTH and DA regulate Na-K ATPase through divergent pathways. Am J Physiol Renal Physiol 282: F512-F522, 2002
    • (2002) Am J Physiol Renal Physiol , vol.282
    • Khundmiri, S.J.1    Lederer, E.2
  • 4
    • 0038311933 scopus 로고    scopus 로고
    • Regulation of Na/Pi transporter in the proximal tubule
    • Murer H, Hernando N, Forster I, Biber J: Regulation of Na/Pi transporter in the proximal tubule. Annu Rev Physiol 65: 531-542, 2003
    • (2003) Annu Rev Physiol , vol.65 , pp. 531-542
    • Murer, H.1    Hernando, N.2    Forster, I.3    Biber, J.4
  • 6
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris BZ, Lim WA: Mechanism and role of PDZ domains in signaling complex assembly. J Cell Sci 114: 3219-3231, 2001
    • (2001) J Cell Sci , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 7
    • 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
  • 8
    • 0035834681 scopus 로고    scopus 로고
    • Essential role for NHERF in cAMP-mediated inhibition of the Na+-HCO3-co-transporter in BSC-1 cells
    • Weinman EJ, Evangelista CM, Steplock D, Liu MZ, Shenolikar S, Bernardo A: Essential role for NHERF in cAMP-mediated inhibition of the Na+-HCO3-co-transporter in BSC-1 cells. J Biol Chem 276: 42339-42346, 2001
    • (2001) J Biol Chem , vol.276 , pp. 42339-42346
    • Weinman, E.J.1    Evangelista, C.M.2    Steplock, D.3    Liu, M.Z.4    Shenolikar, S.5    Bernardo, A.6
  • 9
    • 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, Guggino WB, Li M: 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    Guggino, W.B.4    Li, M.5
  • 10
    • 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 U S A 98: 1300-1305, 2001
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1300-1305
    • Raghuram, V.1    Mak, D.D.2    Foskett, J.K.3
  • 11
    • 0037151039 scopus 로고    scopus 로고
    • Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor
    • Liedtke CM, Yun CH, Kyle N, Wang D: Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor. J Biol Chem 277: 22925-22933, 2002
    • (2002) J Biol Chem , vol.277 , pp. 22925-22933
    • Liedtke, C.M.1    Yun, C.H.2    Kyle, N.3    Wang, D.4
  • 14
    • 0037142080 scopus 로고    scopus 로고
    • Na(+)/H(+) exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signaling
    • Mahon MJ, Donowitz M, Yun CC, Segre GV: Na(+)/H(+) exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signaling. 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
  • 15
    • 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, Bretscher A, von Zastrow M: 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    Bretscher, A.4    Von Zastrow, M.5
  • 16
    • 0033755880 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor association with Na(+)/H(+) exchanger regulatory factor potentiates receptor activity
    • Maudsley S, Zamah AM, Rahman N, Blitzer JT, Luttrell LM, Lefkowitz RJ, Hall RA: Platelet-derived growth factor receptor association with Na(+)/H(+) 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    Blitzer, J.T.4    Luttrell, L.M.5    Lefkowitz, R.J.6    Hall, R.A.7
  • 17
    • 0037166247 scopus 로고    scopus 로고
    • Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors
    • Karthikeyan S, Leung T, Ladias JA: Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors. J Biol Chem 277: 18973-18978, 2002
    • (2002) J Biol Chem , vol.277 , pp. 18973-18978
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3
  • 18
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
    • Hurd TW, Gao L, Roh MH, Macara IG, Margolis B: Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat Cell Biol 5: 137-142, 2003
    • (2003) Nat Cell Biol , vol.5 , pp. 137-142
    • Hurd, T.W.1    Gao, L.2    Roh, M.H.3    Macara, I.G.4    Margolis, B.5
  • 19
    • 0037228253 scopus 로고    scopus 로고
    • Integrated activity of PDZ protein complexes regutares epithelial polarity
    • Bilder D, Schober M, Perrimon N: Integrated activity of PDZ protein complexes regutares epithelial polarity. Nat Cell Biol 5: 53-58, 2003
    • (2003) Nat Cell Biol , vol.5 , pp. 53-58
    • Bilder, D.1    Schober, M.2    Perrimon, N.3
  • 20
    • 0034954343 scopus 로고    scopus 로고
    • Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton
    • Takeda T, McQuistan T, Orlando RA, Farquhar MGL: Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton. J Clin Invest 108: 289-301, 2001
    • (2001) J Clin Invest , vol.108 , pp. 289-301
    • Takeda, T.1    McQuistan, T.2    Orlando, R.A.3    Farquhar, M.G.L.4
  • 22
    • 0031726568 scopus 로고    scopus 로고
    • The plasma membrane-actin linking protein, ezrin, is a glomerular epithelial cell marker in glomerulogenesis, in the adult kidney and in glomerular injury
    • Hugo C, Nangaku M, Shankland SJ, Pichler R, Gordon K, Amieva MR, Couser WG, Furthmayr H, Johnson RJ: The plasma membrane-actin linking protein, ezrin, is a glomerular epithelial cell marker in glomerulogenesis, in the adult kidney and in glomerular injury. Kidney Int 54: 1934-1944, 1998
    • (1998) Kidney Int , vol.54 , pp. 1934-1944
    • Hugo, C.1    Nangaku, M.2    Shankland, S.J.3    Pichler, R.4    Gordon, K.5    Amieva, M.R.6    Couser, W.G.7    Furthmayr, H.8    Johnson, R.J.9
  • 23
    • 0035082651 scopus 로고    scopus 로고
    • The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes
    • Patrie KM, Drescher AJ, Goyal M, Wiggins RC, Margolis B: The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes. J Am Soc Nephrol 12: 667-677, 2001
    • (2001) J Am Soc Nephrol , vol.12 , pp. 667-677
    • Patrie, K.M.1    Drescher, A.J.2    Goyal, M.3    Wiggins, R.C.4    Margolis, B.5
  • 24
    • 0037119361 scopus 로고    scopus 로고
    • Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1
    • Patrie KM, Drescher AJ, Welihinda A, Mundel P, Margolis B: Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1. J Biol Chem 277: 30183-30190, 2002
    • (2002) J Biol Chem , vol.277 , pp. 30183-30190
    • Patrie, K.M.1    Drescher, A.J.2    Welihinda, A.3    Mundel, P.4    Margolis, B.5
  • 26
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher A, Edwards K, Fehon RG: ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 3: 586-599, 2002
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 27
    • 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 NHE 3
    • 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
  • 28
    • 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
  • 29
    • 0037432134 scopus 로고    scopus 로고
    • NHERF-1 uniquely transduces the cAMP signals that inhibit sodium-hydrogen exchange in mouse renal apical membranes
    • Weinman EJ, Steplock D, Shenolikar S: NHERF-1 uniquely transduces the cAMP signals that inhibit sodium-hydrogen exchange in mouse renal apical membranes. FEBS Lett 536: 141-144, 2003
    • (2003) FEBS Lett , vol.536 , pp. 141-144
    • Weinman, E.J.1    Steplock, D.2    Shenolikar, S.3
  • 30
    • 0034889768 scopus 로고    scopus 로고
    • Ezrin binding domain-deficient NHERF attenuates cAMP-mediated inhibition of Na(+)/H(+) exchange in OK cells
    • Weinman EJ, Steplock D, Wade JB, Shenolikar S: Ezrin binding domain-deficient NHERF attenuates cAMP-mediated inhibition of Na(+)/H(+) exchange in OK cells. Am J Physiol Renal Physiol 281: F374-F380, 2001
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Weinman, E.J.1    Steplock, D.2    Wade, J.B.3    Shenolikar, S.4
  • 33
    • 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, Wade JB, Weinman EJ: 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 U S A 99: 11470-11475, 2002
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11470-11475
    • Shenolikar, S.1    Voltz, J.W.2    Minkoff, C.M.3    Wade, J.B.4    Weinman, E.J.5
  • 34
    • 0037315288 scopus 로고    scopus 로고
    • Targeted disruption of the PDZK1 gene by homologous recombination
    • Kocher O, Pal R, Roberts M, Cirovic C, Gilchrist A: 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    Cirovic, C.4    Gilchrist, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.