메뉴 건너뛰기




Volumn 9, Issue 10, 2013, Pages 587-598

The podocyte slit diaphragm - From a thin grey line to a complex signalling hub

Author keywords

[No Author keywords available]

Indexed keywords

NEPHRIN;

EID: 84884670045     PISSN: 17595061     EISSN: 1759507X     Source Type: Journal    
DOI: 10.1038/nrneph.2013.169     Document Type: Review
Times cited : (193)

References (159)
  • 1
    • 0037207471 scopus 로고    scopus 로고
    • Cell biology of the glomerular podocyte
    • Pavenstädt, H., Kriz, W. & Kretzler, M. Cell biology of the glomerular podocyte. Physiol. Rev. 83, 253-307 (2003
    • (2003) Physiol. Rev , vol.83 , pp. 253-307
    • Pavenstädt, H.1    Kriz, W.2    Kretzler, M.3
  • 2
    • 0000214628 scopus 로고
    • Development of the human glomerulus
    • Potter, E. L. Development of the human glomerulus. Arch. Pathol. 80, 241-255 (1965
    • (1965) Arch. Pathol , vol.80 , pp. 241-255
    • Potter, E.L.1
  • 3
    • 0013623992 scopus 로고
    • Electron microscopy of the avian renal glomerulus
    • Pak Poy, R. K. & Robertson, J. S. Electron microscopy of the avian renal glomerulus. J. Biophys. Biochem. Cytol. 3, 183-192 (1957
    • (1957) J. Biophys. Biochem. Cytol , vol.3 , pp. 183-192
    • Pak Poy, R.K.1    Robertson, J.S.2
  • 4
    • 70449196077 scopus 로고
    • Electron microscopy of the marsupial renal glomerulus
    • Pak Poy, R. K. Electron microscopy of the marsupial renal glomerulus. Aust. J. Exp. Biol. Med. Sci. 35, 437-447 (1957
    • (1957) Aust. J. Exp. Biol. Med. Sci , vol.35 , pp. 437-447
    • Pak Poy, R.K.1
  • 5
    • 0002965693 scopus 로고
    • Glomerular permeability II ferritin transfer across the glomerular capillary wall in nephrotic rats
    • Farquhar, M. G. & Palade, G. E. Glomerular permeability. II. Ferritin transfer across the glomerular capillary wall in nephrotic rats. J. Exp. Med. 114, 699-716 (1961
    • (1961) J. Exp. Med , vol.114 , pp. 699-716
    • Farquhar, M.G.1    Palade, G.E.2
  • 6
    • 0001692552 scopus 로고
    • Aminonucleoside nephrosis i electron microscopic study of the renal lesion in rats
    • Vernier, R. L., Papermaster, B. W. & Good, R. A. Aminonucleoside nephrosis. I. Electron microscopic study of the renal lesion in rats. J. Exp. Med. 109, 115-126 (1959
    • (1959) J. Exp. Med , vol.109 , pp. 115-126
    • Vernier, R.L.1    Papermaster, B.W.2    Good, R.A.3
  • 7
    • 0016282517 scopus 로고
    • The permeability of glomerular capillaries to graded dextrans identification of the basement membrane as the primary filtration barrier
    • Caulfield, J. P. & Farquhar, M. G. The permeability of glomerular capillaries to graded dextrans. Identification of the basement membrane as the primary filtration barrier. J. Cell Biol. 63, 883-903 (1974
    • (1974) J. Cell Biol , vol.63 , pp. 883-903
    • Caulfield, J.P.1    Farquhar, M.G.2
  • 8
    • 0002965692 scopus 로고
    • Glomerular permeability i ferritin transfer across the normal glomerular capillary wall
    • Farquhar, M. G., Wissig, S. L. & Palade, G. E. Glomerular permeability. I. Ferritin transfer across the normal glomerular capillary wall. J. Exp. Med. 113, 47-66 (1961
    • (1961) J. Exp. Med , vol.113 , pp. 47-66
    • Farquhar, M.G.1    Wissig, S.L.2    Palade, G.E.3
  • 9
    • 0014920351 scopus 로고
    • An ultrastructural study of glomerular permeability in aminonucleoside nephrosis using catalase as a tracer protein
    • Venkatachalam, M. A., Cotran, R. S. & Karnovsky, M. J. An ultrastructural study of glomerular permeability in aminonucleoside nephrosis using catalase as a tracer protein. J. Exp. Med. 132, 1168-1180 (1970
    • (1970) J. Exp. Med , vol.132 , pp. 1168-1180
    • Venkatachalam, M.A.1    Cotran, R.S.2    Karnovsky, M.J.3
  • 10
    • 34548191832 scopus 로고
    • The fine structure of the renal glomerulus of the mouse
    • Yamada, E. The fine structure of the renal glomerulus of the mouse. J. Biophys. Biochem. Cytol. 1, 551-566 (1955
    • (1955) J. Biophys. Biochem. Cytol , vol.1 , pp. 551-566
    • Yamada, E.1
  • 11
    • 0014919039 scopus 로고
    • An ultrastructural study of glomerular permeability using catalase and peroxidase as tracer proteins
    • Venkatachalam, M. A., Karnovsky, M. J., Fahimi, H. D. & Cotran, R. S. An ultrastructural study of glomerular permeability using catalase and peroxidase as tracer proteins. J. Exp. Med. 132, 1153-1167 (1970
    • (1970) J. Exp. Med , vol.132 , pp. 1153-1167
    • Venkatachalam, M.A.1    Karnovsky, M.J.2    Fahimi, H.D.3    Cotran, R.S.4
  • 12
    • 0017540677 scopus 로고
    • A slit pore theory of capillary filtration based on electron micrographic data on the filtration pathway through the cellular layers of mammalian glomerular capillary walls
    • Hall, B. V. A slit pore theory of capillary filtration based on electron micrographic data on the filtration pathway through the cellular layers of mammalian glomerular capillary walls. Trans. Am. Microsc. Soc. 96, 413-438 (1977
    • (1977) Trans. Am. Microsc. Soc , vol.96 , pp. 413-438
    • Hall, B.V.1
  • 13
    • 0015953201 scopus 로고
    • Porous substructure of the glomerular slit diaphragm in the rat and mouse
    • Rodewald, R. & Karnovsky, M. J. Porous substructure of the glomerular slit diaphragm in the rat and mouse. J. Cell Biol. 60, 423-433 (1974
    • (1974) J. Cell Biol , vol.60 , pp. 423-433
    • Rodewald, R.1    Karnovsky, M.J.2
  • 14
    • 0016630232 scopus 로고
    • Substructure of the glomerular slit diaphragm in freeze-fractured normal rat kidney
    • Karnovsky, M. J. & Ryan, G. B. Substructure of the glomerular slit diaphragm in freeze-fractured normal rat kidney. J. Cell Biol. 65, 233-236 (1975
    • (1975) J. Cell Biol , vol.65 , pp. 233-236
    • Karnovsky, M.J.1    Ryan, G.B.2
  • 15
    • 0016264856 scopus 로고
    • Normal glomerular permeability and its modification by minimal change nephrotic syndrome
    • Robson, A. M., Giangiacomo, J., Kienstra, R. A., Naqvi, S. T. & Ingelfinger, J. R. Normal glomerular permeability and its modification by minimal change nephrotic syndrome. J. Clin. Invest. 54, 1190-1199 (1974
    • (1974) J. Clin. Invest , vol.54 , pp. 1190-1199
    • Robson, A.M.1    Giangiacomo, J.2    Kienstra, R.A.3    Naqvi, S.T.4    Ingelfinger, J.R.5
  • 16
    • 0017286132 scopus 로고
    • Alterations of the glomerular epithelium in acute aminonucleoside nephrosis evidence for formation of occluding junctions and epithelial cell detachment
    • Caulfield, J. P., Reid, J. J. & Farquhar, M. G. Alterations of the glomerular epithelium in acute aminonucleoside nephrosis. Evidence for formation of occluding junctions and epithelial cell detachment. Lab. Invest. 34, 43-59 (1976
    • (1976) Lab. Invest , vol.34 , pp. 43-59
    • Caulfield, J.P.1    Reid, J.J.2    Farquhar, M.G.3
  • 17
    • 34250006557 scopus 로고    scopus 로고
    • The spectrum of podocytopathies: A unifying view of glomerular diseases
    • Wiggins, R. C. The spectrum of podocytopathies: A unifying view of glomerular diseases. Kidney Int. 71, 1205-1214 (2007
    • (2007) Kidney Int , vol.71 , pp. 1205-1214
    • Wiggins, R.C.1
  • 18
    • 0032015551 scopus 로고    scopus 로고
    • Positionally cloned gene for a novel glomerular protein - Nephrin - is mutated in congenital nephrotic syndrome
    • Kestila, M. et al. Positionally cloned gene for a novel glomerular protein - Nephrin - is mutated in congenital nephrotic syndrome. Mol. Cell 1, 575-582 (1998
    • (1998) Mol. Cell , vol.1 , pp. 575-582
    • Kestila, M.1
  • 19
    • 33645749205 scopus 로고    scopus 로고
    • Nephrin strands contribute to a porous slit diaphragm scaffold as revealed by electron tomography
    • Wartiovaara, J. et al. Nephrin strands contribute to a porous slit diaphragm scaffold as revealed by electron tomography. J. Clin. Invest. 114, 1475-1483 (2004
    • (2004) J. Clin. Invest , vol.114 , pp. 1475-1483
    • Wartiovaara, J.1
  • 20
    • 78649829302 scopus 로고    scopus 로고
    • Imaging of the porous ultrastructure of the glomerular epithelial filtration slit
    • Gagliardini, E., Conti, S., Benigni, A., Remuzzi, G. & Remuzzi, A. Imaging of the porous ultrastructure of the glomerular epithelial filtration slit. J. Am. Soc. Nephrol. 21, 2081-2089 (2010
    • (2010) J. Am. Soc. Nephrol , vol.21 , pp. 2081-2089
    • Gagliardini, E.1    Conti, S.2    Benigni, A.3    Remuzzi, G.4    Remuzzi, A.5
  • 21
    • 0033529312 scopus 로고    scopus 로고
    • Nephrin is specifically located at the slit diaphragm of glomerular podocytes
    • Ruotsalainen, V. et al. Nephrin is specifically located at the slit diaphragm of glomerular podocytes. Proc. Natl Acad. Sci. USA 96, 7962-7967 (1999
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7962-7967
    • Ruotsalainen, V.1
  • 22
    • 0034034757 scopus 로고    scopus 로고
    • NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome
    • Boute, N. et al. NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome. Nat. Genet. 24, 349-354 (2000
    • (2000) Nat. Genet , vol.24 , pp. 349-354
    • Boute, N.1
  • 23
    • 0034948819 scopus 로고    scopus 로고
    • Proteinuria and perinatal lethality in mice lacking neph1, a novel protein with homology to nephrin
    • Donoviel, D. B. et al. Proteinuria and perinatal lethality in mice lacking Neph1, a novel protein with homology to nephrin. Mol. Cell Biol. 21, 4829-4836 (2001
    • (2001) Mol. Cell Biol , vol.21 , pp. 4829-4836
    • Donoviel, D.B.1
  • 24
    • 0038641811 scopus 로고    scopus 로고
    • Mice lacking the giant protocadherin mFAT1 exhibit renal slit junction abnormalities and a partially penetrant cyclopia and anophthalmia phenotype
    • Ciani, L., Patel, A., Allen, N. D. & ffrench-Constant, C. Mice lacking the giant protocadherin mFAT1 exhibit renal slit junction abnormalities and a partially penetrant cyclopia and anophthalmia phenotype. Mol. Cell Biol. 23, 3575-3582 (2003
    • (2003) Mol. Cell Biol , vol.23 , pp. 3575-3582
    • Ciani, L.1    Patel, A.2    Allen, N.D.3    Ffrench-Constant, C.4
  • 25
    • 22844436647 scopus 로고    scopus 로고
    • TrpC6 is a glomerular slit diaphragm-associated channel required for normal renal function
    • Reiser, J. et al. TrpC6 is a glomerular slit diaphragm-associated channel required for normal renal function. Nat. Genet. 37, 739-744 (2005
    • (2005) Nat. Genet , vol.37 , pp. 739-744
    • Reiser, J.1
  • 26
    • 20844461826 scopus 로고    scopus 로고
    • A mutation in the TrpC6 cation channel causes familial focal segmental glomerulosclerosis
    • Winn, M. P. et al. A mutation in the TrpC6 cation channel causes familial focal segmental glomerulosclerosis. Science 308, 1801-1804 (2005
    • (2005) Science , vol.308 , pp. 1801-1804
    • Winn, M.P.1
  • 27
    • 0033536599 scopus 로고    scopus 로고
    • Congenital nephrotic syndrome in mice lacking CD2-associated protein
    • Shih, N. Y. et al. Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science 286, 312-315 (1999
    • (1999) Science , vol.286 , pp. 312-315
    • Shih, N.Y.1
  • 28
    • 33751531864 scopus 로고    scopus 로고
    • Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible
    • Hinkes, B. et al. Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible. Nat. Genet. 38, 1397-1405 (2006
    • (2006) Nat. Genet , vol.38 , pp. 1397-1405
    • Hinkes, B.1
  • 29
    • 77955646179 scopus 로고    scopus 로고
    • Association of trypanolytic ApoL1 variants with kidney disease in African Americans
    • Genovese, G. et al. Association of trypanolytic ApoL1 variants with kidney disease in African Americans. Science 329, 841-845 (2010
    • (2010) Science , vol.329 , pp. 841-845
    • Genovese, G.1
  • 30
    • 0034051681 scopus 로고    scopus 로고
    • Mutations in ACTN4, encoding alpha actinin 4, cause familial focal segmental glomerulosclerosis
    • Kaplan, J. M. et al. Mutations in ACTN4, encoding alpha actinin 4, cause familial focal segmental glomerulosclerosis. Nat. Genet. 24, 251-256 (2000
    • (2000) Nat. Genet , vol.24 , pp. 251-256
    • Kaplan, J.M.1
  • 31
    • 80051544854 scopus 로고    scopus 로고
    • Disruption of PTPRO causes childhood-onset nephrotic syndrome
    • Ozaltin, F. et al. Disruption of PTPRO causes childhood-onset nephrotic syndrome. Am. J. Hum. Genet. 89, 139-147 (2011
    • (2011) Am. J. Hum. Genet , vol.89 , pp. 139-147
    • Ozaltin, F.1
  • 32
    • 34250668197 scopus 로고    scopus 로고
    • COQ2 nephropathy: A newly described inherited mitochondriopathy with primary renal involvement
    • Diomedi-Camassei, F. et al. COQ2 nephropathy: A newly described inherited mitochondriopathy with primary renal involvement. J. Am. Soc. Nephrol. 18, 2773-2780 (2007
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 2773-2780
    • Diomedi-Camassei, F.1
  • 33
    • 79955520308 scopus 로고    scopus 로고
    • COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness
    • Heeringa, S. F. et al. COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness. J. Clin. Invest. 121, 2013-2024 (2011
    • (2011) J. Clin. Invest , vol.121 , pp. 2013-2024
    • Heeringa, S.F.1
  • 34
    • 73349132341 scopus 로고    scopus 로고
    • Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis
    • Brown, E. J. et al. Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis. Nat. Genet. 42, 72-76 (2010
    • (2010) Nat. Genet , vol.42 , pp. 72-76
    • Brown, E.J.1
  • 35
    • 79960877647 scopus 로고    scopus 로고
    • MYO1E mutations and childhood familial focal segmental glomerulosclerosis
    • Mele, C. et al. MYO1E mutations and childhood familial focal segmental glomerulosclerosis. N. Engl. J. Med. 365, 295-306
    • N. Engl. J. Med , vol.365 , pp. 295-306
    • Mele, C.1
  • 36
    • 80053410497 scopus 로고    scopus 로고
    • Arhgap24 inactivates Rac1 in mouse podocytes, and a mutant form is associated with familial focal segmental glomerulosclerosis
    • Akilesh, S. et al. Arhgap24 inactivates Rac1 in mouse podocytes, and a mutant form is associated with familial focal segmental glomerulosclerosis. J. Clin. Invest. 121, 4127-4137 (2011
    • (2011) J. Clin. Invest , vol.121 , pp. 4127-4137
    • Akilesh, S.1
  • 37
    • 84878851636 scopus 로고    scopus 로고
    • ARHGDIA: A novel gene implicated in nephrotic syndrome
    • Gupta, I. R. et al. ARHGDIA: A novel gene implicated in nephrotic syndrome. J. Med. Genet. 50, 330-338 (2013
    • (2013) J. Med. Genet , vol.50 , pp. 330-338
    • Gupta, I.R.1
  • 38
    • 0026094584 scopus 로고
    • Germline mutations in the Wilms' tumour suppressor gene are associated with abnormal urogenital development in denys-drash syndrome
    • Pelletier, J. et al. Germline mutations in the Wilms' tumour suppressor gene are associated with abnormal urogenital development in Denys-Drash syndrome. Cell 67, 437-447 (1991
    • (1991) Cell , vol.67 , pp. 437-447
    • Pelletier, J.1
  • 39
    • 8444221929 scopus 로고    scopus 로고
    • Human laminin β2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities
    • Zenker, M. et al. Human laminin β2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities. Hum. Mol. Genet. 13, 2625-2632 (2004
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2625-2632
    • Zenker, M.1
  • 40
    • 0028989243 scopus 로고
    • Integrin β 4 mutations associated with junctional epidermolysis bullosa with pyloric atresia
    • Vidal, F. et al. Integrin β 4 mutations associated with junctional epidermolysis bullosa with pyloric atresia. Nat. Genet. 10, 229-234 (1995
    • (1995) Nat. Genet , vol.10 , pp. 229-234
    • Vidal, F.1
  • 41
    • 40849144062 scopus 로고    scopus 로고
    • Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP 2 deficiency causes myoclonus epilepsy and glomerulosclerosis
    • Berkovic, S. F. et al. Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP 2 deficiency causes myoclonus epilepsy and glomerulosclerosis. Am. J. Hum. Genet. 82, 673-684 (2008
    • (2008) Am. J. Hum. Genet , vol.82 , pp. 673-684
    • Berkovic, S.F.1
  • 42
    • 33845232634 scopus 로고    scopus 로고
    • Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations
    • Lopez, L. C. et al. Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations. Am. J. Hum. Genet. 79, 1125-1129 (2006
    • (2006) Am. J. Hum. Genet , vol.79 , pp. 1125-1129
    • Lopez, L.C.1
  • 43
    • 0025666322 scopus 로고
    • A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies
    • Goto, Y., Nonaka, I. & Horai, S. A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature 348, 651-653 (1990
    • (1990) Nature , vol.348 , pp. 651-653
    • Goto, Y.1    Nonaka, I.2    Horai, S.3
  • 44
    • 0021143782 scopus 로고
    • Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes: A distinctive clinical syndrome
    • Pavlakis, S. G., Phillips, P. C., DiMauro, S., DeVivo, D. C. & Rowland, L. P. Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes: A distinctive clinical syndrome. Ann. Neurol. 16, 481-488 (1984
    • (1984) Ann. Neurol , vol.16 , pp. 481-488
    • Pavlakis, S.G.1    Phillips, P.C.2    Dimauro, S.3    Devivo, D.C.4    Rowland, L.P.5
  • 45
    • 0031747153 scopus 로고    scopus 로고
    • Limb and kidney defects in Lmx1b mutant mice suggest an involvement of LMX1B in human nail patella syndrome
    • Chen, H. et al. Limb and kidney defects in Lmx1b mutant mice suggest an involvement of LMX1B in human nail patella syndrome. Nat. Genet. 19, 51-55 (1998
    • (1998) Nat. Genet , vol.19 , pp. 51-55
    • Chen, H.1
  • 46
    • 0031800728 scopus 로고    scopus 로고
    • Mutations in LMX1B cause abnormal skeletal patterning and renal dysplasia in nail patella syndrome
    • Dreyer, S. D. et al. Mutations in LMX1B cause abnormal skeletal patterning and renal dysplasia in nail patella syndrome. Nat. Genet. 19, 47-50 (1998
    • (1998) Nat. Genet , vol.19 , pp. 47-50
    • Dreyer, S.D.1
  • 47
    • 18544381908 scopus 로고    scopus 로고
    • Mutant chromatin remodeling protein SMARCAL1 causes Schimke immuno-osseous dysplasia
    • Boerkoel, C. F. et al. Mutant chromatin remodeling protein SMARCAL1 causes Schimke immuno-osseous dysplasia. Nat. Genet. 30, 215-220 (2002
    • (2002) Nat. Genet , vol.30 , pp. 215-220
    • Boerkoel, C.F.1
  • 48
    • 80955144198 scopus 로고    scopus 로고
    • Whole exome and whole genome sequencing
    • Bick, D. & Dimmock, D. Whole exome and whole genome sequencing. Curr. Opin. Paediatr. 23, 594-600 (2011
    • (2011) Curr. Opin. Paediatr , vol.23 , pp. 594-600
    • Bick, D.1    Dimmock, D.2
  • 49
    • 80555134774 scopus 로고    scopus 로고
    • Fishing for new glomerular disease-related genes
    • Mangos, S. & Reiser, J. Fishing for new glomerular disease-related genes. J. Am. Soc. Nephrol. 22, 1960-1962 (2011
    • (2011) J. Am. Soc. Nephrol , vol.22 , pp. 1960-1962
    • Mangos, S.1    Reiser, J.2
  • 50
    • 84857243208 scopus 로고    scopus 로고
    • Cell biology and pathology of podocytes
    • Greka, A. & Mundel, P. Cell biology and pathology of podocytes. Annu. Rev. Physiol. 74, 299-323 (2012
    • (2012) Annu. Rev. Physiol , vol.74 , pp. 299-323
    • Greka, A.1    Mundel, P.2
  • 51
    • 0037247603 scopus 로고    scopus 로고
    • Podocyte-specific expression of Cre recombinase in transgenic mice
    • Moeller, M. J., Sanden, S. K., Soofi, A., Wiggins, R. C. & Holzman, L. B. Podocyte-specific expression of Cre recombinase in transgenic mice. Genesis 35, 39-42 (2003
    • (2003) Genesis , vol.35 , pp. 39-42
    • Moeller, M.J.1    Sanden, S.K.2    Soofi, A.3    Wiggins, R.C.4    Holzman, L.B.5
  • 53
    • 18844411833 scopus 로고    scopus 로고
    • The slit diaphragm: A signalling platform to regulate podocyte function
    • Huber, T. B. & Benzing, T. The slit diaphragm: A signalling platform to regulate podocyte function. Curr. Opin. Nephrol. Hypertens. 14, 211-216 (2005
    • (2005) Curr. Opin. Nephrol. Hypertens , vol.14 , pp. 211-216
    • Huber, T.B.1    Benzing, T.2
  • 54
    • 80053439688 scopus 로고    scopus 로고
    • CD2AP in mouse and human podocytes controls a proteolytic programme that regulates cytoskeletal structure and cellular survival
    • Yaddanapudi, S. et al. CD2AP in mouse and human podocytes controls a proteolytic programme that regulates cytoskeletal structure and cellular survival. J. Clin. Invest. 121, 3965-3980 (2011
    • (2011) J. Clin. Invest , vol.121 , pp. 3965-3980
    • Yaddanapudi, S.1
  • 55
    • 0025008077 scopus 로고
    • The tight junction protein ZO 1 is concentrated along slit diaphragms of the glomerular epithelium
    • Schnabel, E., Anderson, J. M. & Farquhar, M. G. The tight junction protein ZO 1 is concentrated along slit diaphragms of the glomerular epithelium. J. Cell Biol. 111, 1255-1263 (1990
    • (1990) J. Cell Biol , vol.111 , pp. 1255-1263
    • Schnabel, E.1    Anderson, J.M.2    Farquhar, M.G.3
  • 56
    • 0033958396 scopus 로고    scopus 로고
    • The glomerular slit diaphragm is a modified adherens junction
    • Reiser, J., Kriz, W., Kretzler, M. & Mundel, P. The glomerular slit diaphragm is a modified adherens junction. J. Am. Soc. Nephrol. 11, 1-8 (2000
    • (2000) J. Am. Soc. Nephrol , vol.11 , pp. 1-8
    • Reiser, J.1    Kriz, W.2    Kretzler, M.3    Mundel, P.4
  • 57
    • 4344565772 scopus 로고    scopus 로고
    • Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin
    • Lehtonen, S., Lehtonen, E., Kudlicka, K., Holthofer, H. & Farquhar, M. G. Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin. Am. J. Pathol. 165, 923-936 (2004
    • (2004) Am. J. Pathol , vol.165 , pp. 923-936
    • Lehtonen, S.1    Lehtonen, E.2    Kudlicka, K.3    Holthofer, H.4    Farquhar, M.G.5
  • 59
    • 0037270882 scopus 로고    scopus 로고
    • NEPH1 defines a novel family of podocin interacting proteins
    • Sellin, L. et al. NEPH1 defines a novel family of podocin interacting proteins. FASEB J. 17, 115-117 (2003
    • (2003) FASEB J. , vol.17 , pp. 115-117
    • Sellin, L.1
  • 60
    • 0036841804 scopus 로고    scopus 로고
    • Upregulation of connexin43 in glomerular podocytes in response to injury
    • Yaoita, E. et al. Upregulation of connexin43 in glomerular podocytes in response to injury. Am. J. Pathol. 161, 1597-1606 (2002
    • (2002) Am. J. Pathol , vol.161 , pp. 1597-1606
    • Yaoita, E.1
  • 61
    • 77958090917 scopus 로고    scopus 로고
    • Proteomic analysis of the slit diaphragm complex: CLIC5 is a protein critical for podocyte morphology and function
    • Pierchala, B. A., Munoz, M. R. & Tsui, C. C. Proteomic analysis of the slit diaphragm complex: CLIC5 is a protein critical for podocyte morphology and function. Kidney Int. 78, 868-882 (2010
    • (2010) Kidney Int , vol.78 , pp. 868-882
    • Pierchala, B.A.1    Munoz, M.R.2    Tsui, C.C.3
  • 62
    • 0018171211 scopus 로고
    • Differentiation of epithelial foot processes and filtration slits: Sequential appearance of occluding junctions, epithelial polyanion, and slit membranes in developing glomeruli
    • Reeves, W., Caulfield, J. P. & Farquhar, M. G. Differentiation of epithelial foot processes and filtration slits: Sequential appearance of occluding junctions, epithelial polyanion, and slit membranes in developing glomeruli. Lab. Invest. 39, 90-100 (1978
    • (1978) Lab. Invest , vol.39 , pp. 90-100
    • Reeves, W.1    Caulfield, J.P.2    Farquhar, M.G.3
  • 63
    • 40949136456 scopus 로고    scopus 로고
    • Development of the renal glomerulus: Good neighbors and good fences
    • Quaggin, S. E. & Kreidberg, J. A. Development of the renal glomerulus: Good neighbors and good fences. Development 135, 609-620 (2008
    • (2008) Development , vol.135 , pp. 609-620
    • Quaggin, S.E.1    Kreidberg, J.A.2
  • 64
    • 0033634789 scopus 로고    scopus 로고
    • Role of nephrin in cell junction formation in human nephrogenesis
    • Ruotsalainen, V. et al. Role of nephrin in cell junction formation in human nephrogenesis. Am. J. Pathol. 157, 1905-1916 (2000
    • (2000) Am. J. Pathol , vol.157 , pp. 1905-1916
    • Ruotsalainen, V.1
  • 65
    • 0031749115 scopus 로고    scopus 로고
    • Involvement of R cadherin in the early stage of glomerulogenesis
    • Goto, S. et al. Involvement of R cadherin in the early stage of glomerulogenesis. J. Am. Soc. Nephrol. 9, 1234-1241 (1998
    • (1998) J. Am. Soc. Nephrol , vol.9 , pp. 1234-1241
    • Goto, S.1
  • 66
    • 0036171229 scopus 로고    scopus 로고
    • Genetic dissection of cadherin function during nephrogenesis
    • Dahl, U. et al. Genetic dissection of cadherin function during nephrogenesis. Mol. Cell Biol. 22, 1474-1487 (2002
    • (2002) Mol. Cell Biol , vol.22 , pp. 1474-1487
    • Dahl, U.1
  • 67
    • 34548487498 scopus 로고    scopus 로고
    • Podocin participates in the assembly of tight junctions between foot processes in nephrotic podocytes
    • Shono, A. et al. Podocin participates in the assembly of tight junctions between foot processes in nephrotic podocytes. J. Am. Soc. Nephrol. 18, 2525-2533 (2007
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 2525-2533
    • Shono, A.1
  • 68
    • 0026729987 scopus 로고
    • The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulphate-treated rats contain the tight junction protein ZO 1
    • Kurihara, H., Anderson, J. M., Kerjaschki, D. & Farquhar, M. G. The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulphate-treated rats contain the tight junction protein ZO 1. Am. J. Pathol. 141, 805-816 (1992
    • (1992) Am. J. Pathol , vol.141 , pp. 805-816
    • Kurihara, H.1    Anderson, J.M.2    Kerjaschki, D.3    Farquhar, M.G.4
  • 69
    • 25844519579 scopus 로고    scopus 로고
    • Organization of the pronephric filtration apparatus in zebrafish requires nephrin, podocin and the FERM domain protein mosaic eyes
    • Kramer-Zucker, A. G., Wiessner, S., Jensen, A. M. & Drummond, I. A. Organization of the pronephric filtration apparatus in zebrafish requires nephrin, podocin and the FERM domain protein mosaic eyes. Dev. Biol. 285, 316-329 (2005
    • (2005) Dev. Biol , vol.285 , pp. 316-329
    • Kramer-Zucker, A.G.1    Wiessner, S.2    Jensen, A.M.3    Drummond, I.A.4
  • 70
    • 84873366506 scopus 로고    scopus 로고
    • Cubilin and amnionless mediate protein reabsorption in drosophila nephrocytes
    • Zhang, F., Zhao, Y., Chao, Y., Muir, K. & Han, Z. Cubilin and amnionless mediate protein reabsorption in Drosophila nephrocytes. J. Am. Soc. Nephrol. 24, 209-216 (2013
    • (2013) J. Am. Soc. Nephrol , vol.24 , pp. 209-216
    • Zhang, F.1    Zhao, Y.2    Chao, Y.3    Muir, K.4    Han, Z.5
  • 71
    • 58249123367 scopus 로고    scopus 로고
    • The insect nephrocyte is a podocyte-like cell with a filtration slit diaphragm
    • Weavers, H. et al. The insect nephrocyte is a podocyte-like cell with a filtration slit diaphragm. Nature 457, 322-326 (2009
    • (2009) Nature , vol.457 , pp. 322-326
    • Weavers, H.1
  • 72
    • 69649091814 scopus 로고    scopus 로고
    • Sns and Kirre, the Drosophila orthologues of nephrin and Neph1, direct adhesion, fusion and formation of a slit diaphragm-like structure in insect nephrocytes
    • Zhuang, S. et al. Sns and Kirre, the Drosophila orthologues of nephrin and Neph1, direct adhesion, fusion and formation of a slit diaphragm-like structure in insect nephrocytes. Development 136, 2335-2344 (2009
    • (2009) Development , vol.136 , pp. 2335-2344
    • Zhuang, S.1
  • 73
    • 84873455805 scopus 로고    scopus 로고
    • The Drosophila nephrocyte: Back on stage
    • Na, J. & Cagan, R. The Drosophila nephrocyte: Back on stage. J. Am. Soc. Nephrol. 24, 161-163 (2013
    • (2013) J. Am. Soc. Nephrol , vol.24 , pp. 161-163
    • Na, J.1    Cagan, R.2
  • 74
    • 84863688902 scopus 로고    scopus 로고
    • Functional study of mammalian neph proteins in drosophila melanogaster
    • Helmstädter, M. et al. Functional study of mammalian Neph proteins in Drosophila melanogaster. PLoS ONE 7, e40300 (2012
    • (2012) PLoS ONE , vol.7
    • Helmstädter, M.1
  • 75
    • 60749106301 scopus 로고    scopus 로고
    • Flying podocytes
    • Simons, M. & Huber, T. B. Flying podocytes. Kidney Int. 75, 455-457 (2009
    • (2009) Kidney Int , vol.75 , pp. 455-457
    • Simons, M.1    Huber, T.B.2
  • 76
    • 1642634997 scopus 로고    scopus 로고
    • Synaptic specificity is generated by the synaptic guidepost protein SYG 2 and its receptor
    • Shen, K., Fetter, R. D. & Bargmann, C. I. Synaptic specificity is generated by the synaptic guidepost protein SYG 2 and its receptor, SYG 1. Cell 116, 869-881 (2004
    • (2004) SYG 1. Cell , vol.116 , pp. 869-881
    • Shen, K.1    Fetter, R.D.2    Bargmann, C.I.3
  • 77
    • 77955288636 scopus 로고    scopus 로고
    • A model organism approach: Defining the role of Neph proteins as regulators of neuron and kidney morphogenesis
    • Neumann-Haefelin, E. et al. A model organism approach: Defining the role of Neph proteins as regulators of neuron and kidney morphogenesis. Hum. Mol. Genet. 19, 2347-2359 (2010
    • (2010) Hum. Mol. Genet , vol.19 , pp. 2347-2359
    • Neumann-Haefelin, E.1
  • 78
    • 80051705567 scopus 로고    scopus 로고
    • Functional and spatial analysis of C elegans SYG 1 and SYG 2, orthologues of the Neph/nephrin cell adhesion module directing selective synaptogenesis
    • Wanner, N. et al. Functional and spatial analysis of C. elegans SYG 1 and SYG 2, orthologues of the Neph/nephrin cell adhesion module directing selective synaptogenesis. PLoS ONE 6, e23598 (2011
    • (2011) PLoS ONE , vol.6
    • Wanner, N.1
  • 79
    • 12444287604 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor, a tight junction membrane protein, is expressed in glomerular podocytes in the kidney
    • Nagai, M. et al. Coxsackievirus and adenovirus receptor, a tight junction membrane protein, is expressed in glomerular podocytes in the kidney. Lab. Invest. 83, 901-911 (2003
    • (2003) Lab. Invest , vol.83 , pp. 901-911
    • Nagai, M.1
  • 80
    • 22244466451 scopus 로고    scopus 로고
    • Cell junction-associated proteins IQGAP1, MAGI 2, CASK, spectrins, and α-actinin are components of the nephrin multiprotein complex
    • Lehtonen, S. et al. Cell junction-associated proteins IQGAP1, MAGI 2, CASK, spectrins, and α-actinin are components of the nephrin multiprotein complex. Proc. Natl Acad. Sci. USA 102, 9814-9819 (2005
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 9814-9819
    • Lehtonen, S.1
  • 81
    • 27944442887 scopus 로고    scopus 로고
    • MAGI 1 is a component of the glomerular slit diaphragm that is tightly associated with nephrin
    • Hirabayashi, S. et al. MAGI 1 is a component of the glomerular slit diaphragm that is tightly associated with nephrin. Lab. Invest. 85, 1528-1543 (2005
    • (2005) Lab. Invest , vol.85 , pp. 1528-1543
    • Hirabayashi, S.1
  • 82
    • 79960425136 scopus 로고    scopus 로고
    • Wnt/β-catenin pathway in podocytes integrates cell adhesion, differentiation, and survival
    • Kato, H. et al. Wnt/β-catenin pathway in podocytes integrates cell adhesion, differentiation, and survival. J. Biol. Chem. 286, 26003-26015 (2011
    • (2011) J. Biol. Chem , vol.286 , pp. 26003-26015
    • Kato, H.1
  • 83
    • 6344276685 scopus 로고    scopus 로고
    • Protocadherin FAT1 binds Ena/VASP proteins and is necessary for actin dynamics and cell polarization
    • Moeller, M. J. et al. Protocadherin FAT1 binds Ena/VASP proteins and is necessary for actin dynamics and cell polarization. EMBO J. 23, 3769-3779 (2004
    • (2004) EMBO J. , vol.23 , pp. 3769-3779
    • Moeller, M.J.1
  • 84
    • 0035097407 scopus 로고    scopus 로고
    • FAT is a component of glomerular slit diaphragms
    • Inoue, T. et al. FAT is a component of glomerular slit diaphragms. Kidney Int. 59, 1003-1012 (2001
    • (2001) Kidney Int , vol.59 , pp. 1003-1012
    • Inoue, T.1
  • 85
    • 33750132733 scopus 로고    scopus 로고
    • Redistribution of connexin43 expression in glomerular podocytes predicts poor renal prognosis in patients with type 2 diabetes and overt nephropathy
    • Sawai, K. et al. Redistribution of connexin43 expression in glomerular podocytes predicts poor renal prognosis in patients with type 2 diabetes and overt nephropathy. Nephrol. Dial. Transplant. 21, 2472-2477 (2006
    • (2006) Nephrol. Dial. Transplant , vol.21 , pp. 2472-2477
    • Sawai, K.1
  • 86
    • 84882245010 scopus 로고    scopus 로고
    • Molecular fingerprinting of the podocyte reveals novel gene and protein regulatory networks
    • Boerries, M. et al. Molecular fingerprinting of the podocyte reveals novel gene and protein regulatory networks. Kidney Int. 83, 1052-1064 (2013
    • (2013) Kidney Int , vol.83 , pp. 1052-1064
    • Boerries, M.1
  • 87
    • 0037743504 scopus 로고    scopus 로고
    • Fyn binds to and phosphorylates the kidney slit diaphragm component nephrin
    • Verma, R. et al. Fyn binds to and phosphorylates the kidney slit diaphragm component nephrin. J. Biol. Chem. 278, 20716-20723 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 20716-20723
    • Verma, R.1
  • 88
    • 0038788840 scopus 로고    scopus 로고
    • Nephrin and CD2AP associate with phosphoinositide 3 OH kinase and stimulate AKT-dependent signalling
    • Huber, T. B. et al. Nephrin and CD2AP associate with phosphoinositide 3 OH kinase and stimulate AKT-dependent signalling. Mol. Cell Biol. 23, 4917-4928 (2003
    • (2003) Mol. Cell Biol , vol.23 , pp. 4917-4928
    • Huber, T.B.1
  • 89
    • 0344413020 scopus 로고    scopus 로고
    • Nephrin promotes cell-cell adhesion through homophilic interactions
    • Khoshnoodi, J. et al. Nephrin promotes cell-cell adhesion through homophilic interactions. Am. J. Pathol. 163, 2337-2346 (2003
    • (2003) Am. J. Pathol , vol.163 , pp. 2337-2346
    • Khoshnoodi, J.1
  • 90
    • 0037379340 scopus 로고    scopus 로고
    • Homodimerization and heterodimerization of the glomerular podocyte proteins nephrin and Neph1
    • Gerke, P., Huber, T. B., Sellin, L., Benzing, T. & Walz, G. Homodimerization and heterodimerization of the glomerular podocyte proteins nephrin and Neph1. J. Am. Soc. Nephrol. 14, 918-926 (2003
    • (2003) J. Am. Soc. Nephrol , vol.14 , pp. 918-926
    • Gerke, P.1    Huber, T.B.2    Sellin, L.3    Benzing, T.4    Walz, G.5
  • 91
    • 0037805606 scopus 로고    scopus 로고
    • Nephrin and Neph1 co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers
    • Barletta, G. M., Kovari, I. A., Verma, R. K., Kerjaschki, D. & Holzman, L. B. Nephrin and Neph1 co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers. J. Biol. Chem. 278, 19266-19271 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 19266-19271
    • Barletta, G.M.1    Kovari, I.A.2    Verma, R.K.3    Kerjaschki, D.4    Holzman, L.B.5
  • 92
    • 53149104790 scopus 로고    scopus 로고
    • Neph-nephrin proteins bind the Par3-Par6 atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity
    • Hartleben, B. et al. Neph-nephrin proteins bind the Par3-Par6 atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity. J. Biol. Chem. 283, 23033-23038 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 23033-23038
    • Hartleben, B.1
  • 93
    • 0346121526 scopus 로고    scopus 로고
    • Molecular basis of the functional podocin-nephrin complex: Mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains
    • Huber, T. B. et al. Molecular basis of the functional podocin-nephrin complex: Mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains. Hum. Mol. Genet. 12, 3397-3405 (2003
    • (2003) Hum. Mol. Genet , vol.12 , pp. 3397-3405
    • Huber, T.B.1
  • 94
    • 37549036286 scopus 로고    scopus 로고
    • Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization
    • Garg, P., Verma, R., Nihalani, D., Johnstone, D. B. & Holzman, L. B. Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization. Mol. Cell Biol. 27, 8698-8712 (2007
    • (2007) Mol. Cell Biol , vol.27 , pp. 8698-8712
    • Garg, P.1    Verma, R.2    Nihalani, D.3    Johnstone, D.B.4    Holzman, L.B.5
  • 95
    • 0028839194 scopus 로고
    • A stomatin-like protein necessary for mechanosensation in C elegans
    • Huang, M., Gu, G., Ferguson, E. L. & Chalfie, M. A stomatin-like protein necessary for mechanosensation in C. elegans. Nature 378, 292-295 (1995
    • (1995) Nature , vol.378 , pp. 292-295
    • Huang, M.1    Gu, G.2    Ferguson, E.L.3    Chalfie, M.4
  • 96
    • 33751225687 scopus 로고    scopus 로고
    • Podocin and MEC 2 bind cholesterol to regulate the activity of associated ion channels
    • Huber, T. B. et al. Podocin and MEC 2 bind cholesterol to regulate the activity of associated ion channels. Proc. Natl Acad. Sci. USA 103, 17079-17086 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 17079-17086
    • Huber, T.B.1
  • 97
    • 0035210324 scopus 로고    scopus 로고
    • Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin
    • Schwarz, K. et al. Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin. J. Clin. Invest. 108, 1621-1629 (2001
    • (2001) J. Clin. Invest , vol.108 , pp. 1621-1629
    • Schwarz, K.1
  • 98
  • 99
    • 0042242818 scopus 로고    scopus 로고
    • Neph1 and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability
    • Liu, G. et al. Neph1 and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability. J. Clin. Invest. 112, 209-221 (2003
    • (2003) J. Clin. Invest , vol.112 , pp. 209-221
    • Liu, G.1
  • 100
    • 0036293340 scopus 로고    scopus 로고
    • Interaction of endogenous nephrin and CD2-associated protein in mouse epithelial M 1 cell line
    • Palmen, T. et al. Interaction of endogenous nephrin and CD2-associated protein in mouse epithelial M 1 cell line. J. Am. Soc. Nephrol. 13, 1766-1772 (2002
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 1766-1772
    • Palmen, T.1
  • 101
    • 0036014942 scopus 로고    scopus 로고
    • Nephrin TRAP mice lack slit diaphragms and show fibrotic glomeruli and cystic tubular lesions
    • Rantanen, M. et al. Nephrin TRAP mice lack slit diaphragms and show fibrotic glomeruli and cystic tubular lesions. J. Am. Soc. Nephrol. 13, 1586-1594 (2002
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 1586-1594
    • Rantanen, M.1
  • 102
    • 84857934769 scopus 로고    scopus 로고
    • Life without nephrin: It's for the birds
    • Miner, J. H. Life without nephrin: It's for the birds. J. Am. Soc. Nephrol. 23, 369-371 (2012
    • (2012) J. Am. Soc. Nephrol , vol.23 , pp. 369-371
    • Miner, J.H.1
  • 103
    • 0030175132 scopus 로고    scopus 로고
    • Functional morphology of the glomerular filtration barrier of Gallus gallus
    • Casotti, G. & Braun, E. J. Functional morphology of the glomerular filtration barrier of Gallus gallus. J. Morphol. 228, 327-334 (1996
    • (1996) J. Morphol , vol.228 , pp. 327-334
    • Casotti, G.1    Braun, E.J.2
  • 104
    • 0019025384 scopus 로고
    • Significance of comparative studies for renal physiology
    • Dantzler, W. H. Significance of comparative studies for renal physiology. Am. J. Physiol. 238, F437-F444 (1980
    • (1980) Am. J. Physiol , vol.238
    • Dantzler, W.H.1
  • 105
    • 84865770605 scopus 로고    scopus 로고
    • The challenge and response of podocytes to glomerular hypertension
    • Endlich, N. & Endlich, K. The challenge and response of podocytes to glomerular hypertension. Semin. Nephrol. 32, 327-341 (2012
    • (2012) Semin. Nephrol , vol.32 , pp. 327-341
    • Endlich, N.1    Endlich, K.2
  • 106
    • 84855433172 scopus 로고    scopus 로고
    • Blood pressure influences end-stage renal disease of Cd151 knockout mice
    • Sachs, N. et al. Blood pressure influences end-stage renal disease of Cd151 knockout mice. J. Clin. Invest. 122, 348-358 (2012
    • (2012) J. Clin. Invest , vol.122 , pp. 348-358
    • Sachs, N.1
  • 107
    • 0021323530 scopus 로고
    • Haemodynamic basis for glomerular injury in rats with desoxycorticosterone-salt hypertension
    • Dworkin, L. D., Hostetter, T. H., Rennke, H. G. & Brenner, B. M. Haemodynamic basis for glomerular injury in rats with desoxycorticosterone-salt hypertension. J. Clin. Invest. 73, 1448-1461 (1984
    • (1984) J. Clin. Invest , vol.73 , pp. 1448-1461
    • Dworkin, L.D.1    Hostetter, T.H.2    Rennke, H.G.3    Brenner, B.M.4
  • 108
    • 0021948044 scopus 로고
    • Control of glomerular hypertension limits glomerular injury in rats with reduced renal mass
    • Anderson, S., Meyer, T. W., Rennke, H. G. & Brenner, B. M. Control of glomerular hypertension limits glomerular injury in rats with reduced renal mass. J. Clin. Invest. 76, 612-619 (1985
    • (1985) J. Clin. Invest , vol.76 , pp. 612-619
    • Anderson, S.1    Meyer, T.W.2    Rennke, H.G.3    Brenner, B.M.4
  • 109
    • 65649133663 scopus 로고    scopus 로고
    • Sensitizing the slit diaphragm with TrpC6 ion channels
    • Moller, C. C., Flesche, J. & Reiser, J. Sensitizing the slit diaphragm with TrpC6 ion channels. J. Am. Soc. Nephrol. 20, 950-953 (2009
    • (2009) J. Am. Soc. Nephrol , vol.20 , pp. 950-953
    • Moller, C.C.1    Flesche, J.2    Reiser, J.3
  • 110
    • 84873328475 scopus 로고    scopus 로고
    • APKCλ/ι and aPKCζ contribute to podocyte differentiation and glomerular maturation
    • Hartleben, B. et al. aPKCλ/ι and aPKCζ contribute to podocyte differentiation and glomerular maturation. J. Am. Soc. Nephrol. 24, 253-267 (2013
    • (2013) J. Am. Soc. Nephrol , vol.24 , pp. 253-267
    • Hartleben, B.1
  • 111
    • 65249087940 scopus 로고    scopus 로고
    • Loss of podocyte aPKCλ/ι causes polarity defects and nephrotic syndrome
    • Huber, T. B. et al. Loss of podocyte aPKCλ/ι causes polarity defects and nephrotic syndrome. J. Am. Soc. Nephrol. 20, 798-806 (2009
    • (2009) J. Am. Soc. Nephrol , vol.20 , pp. 798-806
    • Huber, T.B.1
  • 112
    • 84860610274 scopus 로고    scopus 로고
    • Role of the polarity protein Scribble for podocyte differentiation and maintenance
    • Hartleben, B. et al. Role of the polarity protein Scribble for podocyte differentiation and maintenance. PLoS ONE 7, e36705 (2012
    • (2012) PLoS ONE , vol.7
    • Hartleben, B.1
  • 113
    • 0037631361 scopus 로고    scopus 로고
    • Neutralization of circulating vascular endothelial growth factor (VEGF) by anti-VEGF antibodies and soluble VEGF receptor 1 (sFlt 1) induces proteinuria
    • Sugimoto, H. et al. Neutralization of circulating vascular endothelial growth factor (VEGF) by anti-VEGF antibodies and soluble VEGF receptor 1 (sFlt 1) induces proteinuria. J. Biol. Chem. 278, 12605-12608 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 12605-12608
    • Sugimoto, H.1
  • 114
    • 0037370325 scopus 로고    scopus 로고
    • Glomerular-specific alterations of VEGF A expression lead to distinct congenital and acquired renal diseases
    • Eremina, V. et al. Glomerular-specific alterations of VEGF A expression lead to distinct congenital and acquired renal diseases. J. Clin. Invest. 111, 707-716 (2003
    • (2003) J. Clin. Invest , vol.111 , pp. 707-716
    • Eremina, V.1
  • 115
    • 0036014938 scopus 로고    scopus 로고
    • Loss of the VEGF164 and VEGF188 isoforms impairs postnatal glomerular angiogenesis and renal arteriogenesis in mice
    • Mattot, V. et al. Loss of the VEGF164 and VEGF188 isoforms impairs postnatal glomerular angiogenesis and renal arteriogenesis in mice. J. Am. Soc. Nephrol. 13, 1548-1560 (2002
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 1548-1560
    • Mattot, V.1
  • 116
    • 0038623780 scopus 로고    scopus 로고
    • Functional evidence that vascular endothelial growth factor may act as an autocrine factor on human podocytes
    • Foster, R. R. et al. Functional evidence that vascular endothelial growth factor may act as an autocrine factor on human podocytes. Am. J. Physiol. Renal Physiol. 284, F1263-F1273 (2003
    • (2003) Am. J. Physiol. Renal Physiol , vol.284
    • Foster, R.R.1
  • 118
    • 77957861954 scopus 로고    scopus 로고
    • Glomerular structure and function require paracrine, not autocrine, VEGF VEGFR 2 signalling
    • Sison, K. et al. Glomerular structure and function require paracrine, not autocrine, VEGF VEGFR 2 signalling. J. Am. Soc. Nephrol. 21, 1691-1701 (2010
    • (2010) J. Am. Soc. Nephrol , vol.21 , pp. 1691-1701
    • Sison, K.1
  • 119
    • 84867519785 scopus 로고    scopus 로고
    • Soluble FLT1 binds lipid microdomains in podocytes to control cell morphology and glomerular barrier function
    • Jin, J. et al. Soluble FLT1 binds lipid microdomains in podocytes to control cell morphology and glomerular barrier function. Cell 151, 384-399 (2012
    • (2012) Cell , vol.151 , pp. 384-399
    • Jin, J.1
  • 120
    • 79953840843 scopus 로고    scopus 로고
    • PKC α mediates β arrestin2 dependent nephrin endocytosis in hyperglycaemia
    • Quack, I. et al. PKC α mediates β arrestin2 dependent nephrin endocytosis in hyperglycaemia. J. Biol. Chem. 286, 12959-12970 (2011
    • (2011) J. Biol. Chem , vol.286 , pp. 12959-12970
    • Quack, I.1
  • 121
    • 33646401549 scopus 로고    scopus 로고
    • Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization
    • Verma, R. et al. Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization. J. Clin. Invest. 116, 1346-1359 (2006
    • (2006) J. Clin. Invest , vol.116 , pp. 1346-1359
    • Verma, R.1
  • 122
    • 0037707376 scopus 로고    scopus 로고
    • Clustering-induced tyrosine phosphorylation of nephrin by Src family kinases
    • Lahdenpera, J. et al. Clustering-induced tyrosine phosphorylation of nephrin by Src family kinases. Kidney Int. 64, 404-413 (2003
    • (2003) Kidney Int , vol.64 , pp. 404-413
    • Lahdenpera, J.1
  • 123
    • 0028953668 scopus 로고
    • Increased Tyr phosphorylation of ZO 1 during modification of tight junctions between glomerular foot processes
    • Kurihara, H., Anderson, J. M. & Farquhar, M. G. Increased Tyr phosphorylation of ZO 1 during modification of tight junctions between glomerular foot processes. Am. J. Physiol. 268, F514-F524 (1995
    • (1995) Am. J. Physiol , vol.268
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 124
    • 9644273952 scopus 로고    scopus 로고
    • SRC-family kinase Fyn phosphorylates the cytoplasmic domain of nephrin and modulates its interaction with podocin
    • Li, H., Lemay, S., Aoudjit, L., Kawachi, H. & Takano, T. SRC-family kinase Fyn phosphorylates the cytoplasmic domain of nephrin and modulates its interaction with podocin. J. Am. Soc. Nephrol. 15, 3006-3015 (2004
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 3006-3015
    • Li, H.1    Lemay, S.2    Aoudjit, L.3    Kawachi, H.4    Takano, T.5
  • 125
    • 39349104907 scopus 로고    scopus 로고
    • Nephrin mediates actin reorganization via phosphoinositide 3 kinase in podocytes
    • Zhu, J. et al. Nephrin mediates actin reorganization via phosphoinositide 3 kinase in podocytes. Kidney Int. 73, 556-566 (2008
    • (2008) Kidney Int , vol.73 , pp. 556-566
    • Zhu, J.1
  • 126
    • 77953835378 scopus 로고    scopus 로고
    • C mip impairs podocyte proximal signalling and induces heavy proteinuria
    • Zhang, S. Y. et al. c mip impairs podocyte proximal signalling and induces heavy proteinuria. Sci. Signal. 3, ra39 (2010
    • (2010) Sci. Signal , vol.3
    • Zhang, S.Y.1
  • 127
    • 77952558702 scopus 로고    scopus 로고
    • Occurrence of minimal change nephrotic syndrome in classical hodgkin lymphoma is closely related to the induction of c mip in hodgkin-reed sternberg cells and podocytes
    • Audard, V. et al. Occurrence of minimal change nephrotic syndrome in classical Hodgkin lymphoma is closely related to the induction of c mip in Hodgkin-Reed Sternberg cells and podocytes. Blood 115, 3756-3762 (2010
    • (2010) Blood , vol.115 , pp. 3756-3762
    • Audard, V.1
  • 128
    • 84865233803 scopus 로고    scopus 로고
    • Podocyte protein, nephrin, is a substrate of protein tyrosine phosphatase 1B
    • Aoudjit, L. et al. Podocyte protein, nephrin, is a substrate of protein tyrosine phosphatase 1B. J. Signal Transduct. 2011, 376543 (2011
    • (2011) J. Signal Transduct , vol.2011 , pp. 376543
    • Aoudjit, L.1
  • 129
    • 0033722475 scopus 로고    scopus 로고
    • Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate
    • Wharram, B. L. et al. Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate. J. Clin. Invest. 106, 1281-1290 (2000
    • (2000) J. Clin. Invest , vol.106 , pp. 1281-1290
    • Wharram, B.L.1
  • 130
    • 34848907421 scopus 로고    scopus 로고
    • Actin up: Regulation of podocyte structure and function by components of the actin cytoskeleton
    • Faul, C., Asanuma, K., Yanagida-Asanuma, E., Kim, K. & Mundel, P. Actin up: Regulation of podocyte structure and function by components of the actin cytoskeleton. Trends Cell Biol. 17, 428-437 (2007
    • (2007) Trends Cell Biol , vol.17 , pp. 428-437
    • Faul, C.1    Asanuma, K.2    Yanagida-Asanuma, E.3    Kim, K.4    Mundel, P.5
  • 131
    • 51349162919 scopus 로고    scopus 로고
    • The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A
    • Faul, C. et al. The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A. Nat. Med. 14, 931-938 (2008
    • (2008) Nat. Med , vol.14 , pp. 931-938
    • Faul, C.1
  • 132
    • 67649690129 scopus 로고    scopus 로고
    • Nck proteins maintain the adult glomerular filtration barrier
    • Jones, N. et al. Nck proteins maintain the adult glomerular filtration barrier. J. Am. Soc. Nephrol. 20, 1533-1543 (2009
    • (2009) J. Am. Soc. Nephrol , vol.20 , pp. 1533-1543
    • Jones, N.1
  • 133
    • 33645746950 scopus 로고    scopus 로고
    • Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes
    • Jones, N. et al. Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes. Nature 440, 818-823 (2006
    • (2006) Nature , vol.440 , pp. 818-823
    • Jones, N.1
  • 134
    • 84877098203 scopus 로고    scopus 로고
    • N WASP Is required for stabilization of podocyte foot processes
    • Schell, C. et al. N WASP Is required for stabilization of podocyte foot processes. J. Am. Soc. Nephrol. 24, 713-721 (2013
    • (2013) J. Am. Soc. Nephrol , vol.24 , pp. 713-721
    • Schell, C.1
  • 135
    • 67649778673 scopus 로고    scopus 로고
    • Phosphorylation of nephrin triggers Ca2+ signalling by recruitment and activation of phospholipase C γ1
    • Harita, Y. et al. Phosphorylation of nephrin triggers Ca2+ signalling by recruitment and activation of phospholipase C γ1. J. Biol. Chem. 284, 8951-8962 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 8951-8962
    • Harita, Y.1
  • 136
    • 79957605758 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent activation of TrpC6 regulated by PLC-γ1 and nephrin: Effect of mutations associated with focal segmental glomerulosclerosis
    • Kanda, S. et al. Tyrosine phosphorylation-dependent activation of TrpC6 regulated by PLC-γ1 and nephrin: Effect of mutations associated with focal segmental glomerulosclerosis. Mol. Biol. Cell 22, 1824-1835 (2011
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1824-1835
    • Kanda, S.1
  • 139
    • 0027981333 scopus 로고
    • 1 Phosphatidylinositol 3 kinase activity is required for insulin-stimulated glucose transport but not for RAS activation in CHO cells
    • Hara, K. et al. 1 Phosphatidylinositol 3 kinase activity is required for insulin-stimulated glucose transport but not for RAS activation in CHO cells. Proc. Natl Acad. Sci. USA 91, 7415-7419 (1994
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7415-7419
    • Hara, K.1
  • 140
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin 3 induced phosphorylation of BAD through the protein kinase Akt
    • del Peso, L., Gonzalez-Garcia, M., Page, C., Herrera, R. & Nunez, G. Interleukin 3 induced phosphorylation of BAD through the protein kinase Akt. Science 278, 687-689 (1997
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 141
    • 0034745353 scopus 로고    scopus 로고
    • Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER 2/neu-overexpressing cells
    • Zhou, B. P. et al. Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER 2/neu-overexpressing cells. Nat. Cell Biol. 3, 245-252 (2001
    • (2001) Nat. Cell Biol , vol.3 , pp. 245-252
    • Zhou, B.P.1
  • 142
    • 18644370396 scopus 로고    scopus 로고
    • Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27Kip1 by PKB/Akt-mediated phosphorylation in breast cancer
    • Viglietto, G. et al. Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27Kip1 by PKB/Akt-mediated phosphorylation in breast cancer. Nat. Med. 8, 1136-1144 (2002
    • (2002) Nat. Med , vol.8 , pp. 1136-1144
    • Viglietto, G.1
  • 143
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase 3 by insulin mediated by protein kinase B
    • Cross, D A., Alessi, D. R., Cohen, P., Andjelkovich, M. & Haemmings, B. A. Inhibition of glycogen synthase kinase 3 by insulin mediated by protein kinase B. Nature 378, 785-789 (1995
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Haemmings, B.A.5
  • 144
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki, K., Li, Y., Zhu, T., Wu, J. & Guan, K. L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4, 648-657 (2002
    • (2002) Nat. Cell Biol , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 145
    • 0032529189 scopus 로고    scopus 로고
    • Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE 1 PI3 kinase to the DAF 16 transcription factor
    • Paradis, S. & Ruvkun, G. Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE 1 PI3 kinase to the DAF 16 transcription factor. Genes Dev. 12, 2488-2498 (1998
    • (1998) Genes Dev , vol.12 , pp. 2488-2498
    • Paradis, S.1    Ruvkun, G.2
  • 146
    • 0033560896 scopus 로고    scopus 로고
    • Direct control of the forkhead transcription factor AFX by protein kinase B
    • Kops, G J. et al. Direct control of the Forkhead transcription factor AFX by protein kinase B. Nature 398, 630-634 (1999
    • (1999) Nature , vol.398 , pp. 630-634
    • Kops, G.J.1
  • 147
    • 33846429631 scopus 로고    scopus 로고
    • Transcriptional suppression of nephrin in podocytes by macrophages: Roles of inflammatory cytokines and involvement of the PI3K/Akt pathway
    • Takano, Y. et al. Transcriptional suppression of nephrin in podocytes by macrophages: Roles of inflammatory cytokines and involvement of the PI3K/Akt pathway. FEBS Lett. 581, 421-426 (2007
    • (2007) FEBS Lett , vol.581 , pp. 421-426
    • Takano, Y.1
  • 148
    • 72049124038 scopus 로고    scopus 로고
    • Phosphorylation of nephrin triggers its internalization by raft-mediated endocytosis
    • Qin, X. S. et al. Phosphorylation of nephrin triggers its internalization by raft-mediated endocytosis. J. Am. Soc. Nephrol. 20, 2534-2545 (2009
    • (2009) J. Am. Soc. Nephrol , vol.20 , pp. 2534-2545
    • Qin, X.S.1
  • 149
    • 33749019987 scopus 로고    scopus 로고
    • Β-Arrestin2 mediates nephrin endocytosis and impairs slit diaphragm integrity
    • Quack, I. et al. β-Arrestin2 mediates nephrin endocytosis and impairs slit diaphragm integrity. Proc. Natl Acad. Sci. USA 103, 14110-14115 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14110-14115
    • Quack, I.1
  • 150
    • 84862936145 scopus 로고    scopus 로고
    • Notch promotes dynamin-dependent endocytosis of nephrin
    • Waters, A. M. et al. Notch promotes dynamin-dependent endocytosis of nephrin. J. Am. Soc. Nephrol. 23, 27-35 (2012
    • (2012) J. Am. Soc. Nephrol , vol.23 , pp. 27-35
    • Waters, A.M.1
  • 151
    • 84877097595 scopus 로고    scopus 로고
    • Vps34 deficiency reveals the importance of endocytosis for podocyte homeostasis
    • Bechtel, W. et al. Vps34 deficiency reveals the importance of endocytosis for podocyte homeostasis. J. Am. Soc. Nephrol. 24, 727-743 (2013
    • (2013) J. Am. Soc. Nephrol , vol.24 , pp. 727-743
    • Bechtel, W.1
  • 152
    • 84870523768 scopus 로고    scopus 로고
    • Role of dynamin, synaptojanin, and endophilin in podocyte foot processes
    • Soda, K. et al. Role of dynamin, synaptojanin, and endophilin in podocyte foot processes. J. Clin. Invest. 122, 4401-4411 (2012
    • (2012) J. Clin. Invest , vol.122 , pp. 4401-4411
    • Soda, K.1
  • 153
    • 84857638284 scopus 로고    scopus 로고
    • Comparative analysis of Neph gene expression in mouse and chicken development
    • Volker, L. A. et al. Comparative analysis of Neph gene expression in mouse and chicken development. Histochem. Cell Biol. 137, 355-366 (2012
    • (2012) Histochem. Cell Biol , vol.137 , pp. 355-366
    • Volker, L.A.1
  • 154
    • 33947181051 scopus 로고    scopus 로고
    • The normal kidney filters nephrotic levels of albumin retrieved by proximal tubule cells: Retrieval is disrupted in nephrotic states
    • Russo, L. M. et al. The normal kidney filters nephrotic levels of albumin retrieved by proximal tubule cells: Retrieval is disrupted in nephrotic states. Kidney Int. 71, 504-513 (2007
    • (2007) Kidney Int , vol.71 , pp. 504-513
    • Russo, L.M.1
  • 155
    • 79956081242 scopus 로고    scopus 로고
    • Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane
    • Arif, E. et al. Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane. Mol. Cell Biol. 31, 2134-2150 (2011
    • (2011) Mol. Cell Biol , vol.31 , pp. 2134-2150
    • Arif, E.1
  • 156
    • 84858609721 scopus 로고    scopus 로고
    • Solution structure analysis of cytoplasmic domain of podocyte protein Neph1 using small/wide angle x ray scattering (SWAXS
    • Mallik, L. et al. Solution structure analysis of cytoplasmic domain of podocyte protein Neph1 using small/wide angle x ray scattering (SWAXS). J. Biol. Chem. 287, 9441-9453 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 9441-9453
    • Mallik, L.1
  • 157
    • 84857243208 scopus 로고    scopus 로고
    • Cell biology and pathology of podocytes
    • Greka, A. & Mundel, P. Cell biology and pathology of podocytes. Annu. Rev. Physiol. 74, 299-323 (2012
    • (2012) Annu. Rev. Physiol , vol.74 , pp. 299-323
    • Greka, A.1    Mundel, P.2
  • 158
    • 84865788310 scopus 로고    scopus 로고
    • Signalling from the podocyte intercellular junction to the actin cytoskeleton
    • George, B. & Holzman, L. B. Signalling from the podocyte intercellular junction to the actin cytoskeleton. Semin. Nephrol. 32, 307-318 (2012
    • (2012) Semin. Nephrol , vol.32 , pp. 307-318
    • George, B.1    Holzman, L.B.2
  • 159
    • 0038136885 scopus 로고    scopus 로고
    • CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility
    • Kim, J. M. et al. CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility. Science 300, 1298-1300 (2003
    • (2003) Science , vol.300 , pp. 1298-1300
    • Kim, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.