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Volumn 44, Issue 5, 2012, Pages 815-823

The interaction between megalin and ClC-5 is scaffolded by the Na +-H + exchanger regulatory factor 2 (NHERF2) in proximal tubule cells

Author keywords

ClC 5; Megalin; NHERF2; PDZ binding motif; Protein complex

Indexed keywords

ALBUMIN; CUBILIN; HYBRID PROTEIN; MEGALIN; MEMBRANE PROTEIN; PROTEIN C1C 5; PROTEIN NHERF 2; SCAFFOLD PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84859269830     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2012.02.007     Document Type: Article
Times cited : (26)

References (41)
  • 2
    • 33646708967 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of megalin: Linking urinary protein and gene regulation in proximal tubule?
    • DOI 10.1038/sj.ki.5000298, PII 5000298
    • D. Biemesderfer Regulated intramembrane proteolysis of megalin: linking urinary protein and gene regulation in proximal tubule Kidney Int 69 2006 1717 1721 (Pubitemid 43739196)
    • (2006) Kidney International , vol.69 , Issue.10 , pp. 1717-1721
    • Biemesderfer, D.1
  • 3
    • 0035971106 scopus 로고    scopus 로고
    • Active (9.6S) and inactive (21S) oligomers of NHE3 in microdomains of the renal brush border
    • D. Biemesderfer, B. DeGray, and P.S. Aronson Active (9.6S) and inactive (21S) oligomers of NHE3 in microdomains of the renal brush border J Biol Chem 276 2001 10161 10167
    • (2001) J Biol Chem , vol.276 , pp. 10161-10167
    • Biemesderfer, D.1    Degray, B.2    Aronson, P.S.3
  • 5
    • 4344578072 scopus 로고    scopus 로고
    • The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP
    • DOI 10.1242/jcs.01180
    • B. Cha, A. Kenworthy, R. Murtazina, and M. Donowitz The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP J Cell Sci 117 2004 3353 3365 (Pubitemid 39139919)
    • (2004) Journal of Cell Science , vol.117 , Issue.15 , pp. 3353-3365
    • Cha, B.1    Kenworthy, A.2    Murtazina, R.3    Donowitz, M.4
  • 6
    • 77955663406 scopus 로고    scopus 로고
    • The soluble intracellular domain of megalin does not affect renal proximal tubular function in vivo
    • A. Christ, S. Terryn, V. Schmidt, E.I. Christensen, M.R. Huska, and M.A. Andrade-Navarro The soluble intracellular domain of megalin does not affect renal proximal tubular function in vivo Kidney Int 78 2010 473 477
    • (2010) Kidney Int , vol.78 , pp. 473-477
    • Christ, A.1    Terryn, S.2    Schmidt, V.3    Christensen, E.I.4    Huska, M.R.5    Andrade-Navarro, M.A.6
  • 7
    • 0035006545 scopus 로고    scopus 로고
    • Megalin and cubilin: Synergistic endocytic receptors in renal proximal tubule
    • E.I. Christensen, and H. Birn Megalin and cubilin: synergistic endocytic receptors in renal proximal tubule Am J Physiol Renal Physiol 280 2001 F562 F573
    • (2001) Am J Physiol Renal Physiol , vol.280
    • Christensen, E.I.1    Birn, H.2
  • 11
    • 79959337007 scopus 로고    scopus 로고
    • Alterations in the proteome of the NHERF2 knockout mouse jejunal brush border membrane vesicles
    • M. Donowitz, S. Singh, P. Singh, M. Chakraborty, Y. Chen, and R. Murtazina Alterations in the proteome of the NHERF2 knockout mouse jejunal brush border membrane vesicles Physiol Genomics 43 2011 674 684
    • (2011) Physiol Genomics , vol.43 , pp. 674-684
    • Donowitz, M.1    Singh, S.2    Singh, P.3    Chakraborty, M.4    Chen, Y.5    Murtazina, R.6
  • 12
    • 15544373016 scopus 로고    scopus 로고
    • Renal tubule albumin transport
    • DOI 10.1146/annurev.physiol.67.031103.154845
    • M. Gekle Renal tubule albumin transport Ann Rev Physiol 67 2005 573 594 (Pubitemid 40404502)
    • (2005) Annual Review of Physiology , vol.67 , pp. 573-594
    • Gekle, M.1
  • 13
    • 0033231441 scopus 로고    scopus 로고
    • + exchange impairs receptor-mediated albumin endocytosis in renal proximal tubule-derived epithelial cells from opossum
    • DOI 10.1111/j.1469-7793.1999.00709.x
    • + exchange impairs receptor-mediated albumin endocytosis in renal proximal tubule-derived epithelial cells from opossum J Physiol 520 1999 709 721 (Pubitemid 29533030)
    • (1999) Journal of Physiology , vol.520 , Issue.3 , pp. 709-721
    • Gekle, M.1    Drumm, K.2    Mildenberger, S.3    Freudinger, R.4    Gassner, B.5    Silbernagl, S.6
  • 14
    • 0035868903 scopus 로고    scopus 로고
    • + exchanger-3 interferes with apical receptor-mediated endocytosis via vesicle fusion
    • DOI 10.1111/j.1469-7793.2001.0619h.x
    • + exchanger-3 interferes with apical receptor-mediated endocytosis via vesicle fusion J Physiol 531 2001 619 629 (Pubitemid 32243744)
    • (2001) Journal of Physiology , vol.531 , Issue.3 , pp. 619-629
    • Gekle, M.1    Freudinger, R.2    Mildenberger, S.3
  • 17
    • 33645851042 scopus 로고    scopus 로고
    • ClC-5: A chloride channel with multiple roles in renal tubular albumin uptake
    • D.H. Hryciw, J. Ekberg, C.A. Pollock, and P. Poronnik ClC-5: A chloride channel with multiple roles in renal tubular albumin uptake Int J Biochem Cell Biol 38 2005 1036 1042
    • (2005) Int J Biochem Cell Biol , vol.38 , pp. 1036-1042
    • Hryciw, D.H.1    Ekberg, J.2    Pollock, C.A.3    Poronnik, P.4
  • 18
  • 20
    • 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
    • DOI 10.1021/bi0103516
    • A.G. Lau, and R.A. Hall Oligomerization of NHERF-1 and NHERF-2 PDZ domains: differential regulation by association with receptor carboxyl-termini and by phosphorylation Biochemistry 40 2001 8572 8580 (Pubitemid 32667264)
    • (2001) Biochemistry , vol.40 , Issue.29 , pp. 8572-8580
    • Lau, A.G.1    Hall, R.A.2
  • 23
    • 27344445124 scopus 로고    scopus 로고
    • Macromolecular complexes of cystic fibrosis transmembrane conductance regulator and its interacting partners
    • DOI 10.1016/j.pharmthera.2005.04.004, PII S0163725805000793
    • C. Li, and A.P. Naren Macromolecular complexes of cystic fibrosis transmembrane conductance regulator and its interacting partners Pharmacol Ther 108 2005 208 223 (Pubitemid 41527085)
    • (2005) Pharmacology and Therapeutics , vol.108 , Issue.2 , pp. 208-223
    • Li, C.1    Naren, A.P.2
  • 24
    • 79959566612 scopus 로고    scopus 로고
    • Chloride channel (CLC)-5 is necessary for exocytic trafficking of NHE3
    • Z. Lin, S. Jin, X. Duan, T. Wang, S. Martini, and P. Hulamm Chloride channel (CLC)-5 is necessary for exocytic trafficking of NHE3 J Biol Chem 286 2011 22833 22845
    • (2011) J Biol Chem , vol.286 , pp. 22833-22845
    • Lin, Z.1    Jin, S.2    Duan, X.3    Wang, T.4    Martini, S.5    Hulamm, P.6
  • 28
    • 0344875494 scopus 로고    scopus 로고
    • The Adaptor Protein ARH Escorts Megalin to and through Endosomes
    • DOI 10.1091/mbc.E03-06-0385
    • M. Nagai, T. Meerloo, T. Takeda, and M.G. Farquhar The adaptor protein ARH escorts megalin to and through endosomes Mol Biol Cell 14 2003 4984 4996 (Pubitemid 37484812)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.12 , pp. 4984-4996
    • Nagai, M.1    Meerloo, T.2    Takeda, T.3    Farquhar, M.G.4
  • 29
    • 77953555147 scopus 로고    scopus 로고
    • Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis
    • G. Novarino, S. Weinert, G. Rickheit, and T.J. Jentsch Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis Science 328 2010 1398 1401
    • (2010) Science , vol.328 , pp. 1398-1401
    • Novarino, G.1    Weinert, S.2    Rickheit, G.3    Jentsch, T.J.4
  • 31
    • 34250629350 scopus 로고    scopus 로고
    • Albumin transport and processing by the proximal tubule: Physiology and pathophysiology
    • DOI 10.1097/MNH.0b013e3281eb9059, PII 0004155220070700000012
    • C.A. Pollock, and P. Poronnik Albumin transport and processing by the proximal tubule: physiology and pathophysiology Curr Opin Nephrol Hypertens 16 2007 359 364 (Pubitemid 46944335)
    • (2007) Current Opinion in Nephrology and Hypertension , vol.16 , Issue.4 , pp. 359-364
    • Pollock, C.A.1    Poronnik, P.2
  • 32
    • 75149152495 scopus 로고    scopus 로고
    • CLC-5 and KIF3B interact to facilitate CLC-5 plasma membrane expression, endocytosis, and microtubular transport: Relevance to pathophysiology of Dent's disease
    • A.A. Reed, N.Y. Loh, S. Terryn, J.D. Lippiat, C. Partridge, and J. Galvanovskis CLC-5 and KIF3B interact to facilitate CLC-5 plasma membrane expression, endocytosis, and microtubular transport: relevance to pathophysiology of Dent's disease Am J Physiol Renal Physiol 298 2010 F365 F380
    • (2010) Am J Physiol Renal Physiol , vol.298
    • Reed, A.A.1    Loh, N.Y.2    Terryn, S.3    Lippiat, J.D.4    Partridge, C.5    Galvanovskis, J.6
  • 33
    • 33947181051 scopus 로고    scopus 로고
    • The normal kidney filters nephrotic levels of albumin retrieved by proximal tubule cells: Retrieval is disrupted in nephrotic states
    • DOI 10.1038/sj.ki.5002041, PII 5002041
    • L.M. Russo, R.M. Sandoval, M. McKee, T.M. Osicka, A.B. Collins, and D. Brown The normal kidney filters nephrotic levels of albumin retrieved by proximal tubule cells: retrieval is disrupted in nephrotic states Kidney Int 71 2007 504 513 (Pubitemid 46398675)
    • (2007) Kidney International , vol.71 , Issue.6 , pp. 504-513
    • Russo, L.M.1    Sandoval, R.M.2    McKee, M.3    Osicka, T.M.4    Collins, A.B.5    Brown, D.6    Molitoris, B.A.7    Comper, W.D.8
  • 35
    • 2942691984 scopus 로고    scopus 로고
    • Examination of megalin in renal tubular epithelium from patients with Dent disease
    • DOI 10.1007/s00467-004-1445-9
    • Y. Santo, H. Hirai, M. Shima, M. Yamagata, T. Michigami, and S. Nakajima Examination of megalin in renal tubular epithelium from patients with Dent disease Pediatr Nephrol 19 2004 612 615 (Pubitemid 38771730)
    • (2004) Pediatric Nephrology , vol.19 , Issue.6 , pp. 612-615
    • Santo, Y.1    Hirai, H.2    Shima, M.3    Yamagata, M.4    Michigami, T.5    Nakajima, S.6    Ozono, K.7
  • 37
    • 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
    • DOI 10.1021/bi000064m
    • E.J. Weinman, D. Steplock, M. Donowitz, and S. Shenolikar NHERF associations with sodium-hydrogen exchanger isoform 3 (NHE3) and ezrin are essential for cAMP-mediated phosphorylation and inhibition of NHE3 Biochemistry 38 2000 6123 6129 (Pubitemid 30327087)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6123-6129
    • Weinman, E.J.1    Steplock, D.2    Donowitz, M.3    Shenolikar, S.4
  • 38
    • 0037040897 scopus 로고    scopus 로고
    • + exchanger isoform 3 revisited: The roles of SGK1 and NHERF2
    • DOI 10.1074/jbc.M107768200
    • + exchanger isoform 3 revisited. The roles of SGK1 and NHERF2 J Biol Chem 277 2002 7676 7683 (Pubitemid 34968213)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 7676-7683
    • Chris Yun, C.1    Chen, Y.2    Lang, F.3
  • 41
    • 80054900664 scopus 로고    scopus 로고
    • + and fluid absorption: A macromolecular complex perspective
    • + and fluid absorption: a macromolecular complex perspective Am J Physiol Cell Physiol 301 2011 C982 C983
    • (2011) Am J Physiol Cell Physiol , vol.301
    • Zhang, W.1    Naren, A.P.2


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