메뉴 건너뛰기




Volumn 318, Issue 9, 2012, Pages 955-963

Podocytes: Gaining a foothold

Author keywords

Cytoskeleton; Glomerulus; Intercellular junction; Kidney; Podocyte

Indexed keywords

ADAPTOR PROTEIN; ALPHA ACTININ 4; ALPHA3 INTEGRIN; AUTOPHAGY PROTEIN 5; BETA CATENIN; BETA1 INTEGRIN; COFILIN; COFILIN 1; FOCAL ADHESION KINASE; INTEGRIN LINKED KINASE; LAMININ GAMMA1; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; MEGALIN; NCK PROTEIN; NEPHRIN; NOTCH1 RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE 3 KINASE; PODOCALYXIN; PODOCIN; PROTEIN KINASE FYN; PROTEIN P85; SYNAPTOPODIN; TRANSCRIPTION FACTOR NFAT; TRANSIENT RECEPTOR POTENTIAL CHANNEL 6; TYROSINE; UBIDECARENONE; WT1 PROTEIN;

EID: 84859838187     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.02.030     Document Type: Review
Times cited : (37)

References (82)
  • 1
    • 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. 1990, 111:1255-1263.
    • (1990) J. Cell Biol. , vol.111 , pp. 1255-1263
    • Schnabel, E.1    Anderson, J.M.2    Farquhar, M.G.3
  • 2
    • 0024573781 scopus 로고
    • Biogenesis of podocalyxin - the major glomerular sialoglycoprotein - in the newborn rat kidney
    • Schnabel E., Dekan G., Miettinen A., Farquhar M.G. Biogenesis of podocalyxin - the major glomerular sialoglycoprotein - in the newborn rat kidney. Eur. J. Cell Biol. 1989, 48:313-326.
    • (1989) Eur. J. Cell Biol. , vol.48 , pp. 313-326
    • Schnabel, E.1    Dekan, G.2    Miettinen, A.3    Farquhar, M.G.4
  • 5
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty G., Petersen C., Gao L., Macara I.G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2000, 2:531-539.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 6
    • 41549086164 scopus 로고    scopus 로고
    • Regulation of cell polarity during epithelial morphogenesis
    • Martin-Belmonte F., Mostov K. Regulation of cell polarity during epithelial morphogenesis. Curr. Opin. Cell Biol. 2008, 20:227-234.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 227-234
    • Martin-Belmonte, F.1    Mostov, K.2
  • 7
    • 0037392085 scopus 로고    scopus 로고
    • Prenatal diagnosis of congenital nephrotic syndrome (CNF, NPHS1)
    • Kestila M., Jarvela I. Prenatal diagnosis of congenital nephrotic syndrome (CNF, NPHS1). Prenat. Diagn. 2003, 23:323-324.
    • (2003) Prenat. Diagn. , vol.23 , pp. 323-324
    • Kestila, M.1    Jarvela, I.2
  • 9
    • 19944391600 scopus 로고    scopus 로고
    • Preferential adhesion mediated by Hibris and Roughest regulates morphogenesis and patterning in the Drosophila eye
    • Bao S., Cagan R. Preferential adhesion mediated by Hibris and Roughest regulates morphogenesis and patterning in the Drosophila eye. Dev. Cell 2005, 8:925-935.
    • (2005) Dev. Cell , vol.8 , pp. 925-935
    • Bao, S.1    Cagan, R.2
  • 10
    • 0035161741 scopus 로고    scopus 로고
    • Characterization of Drosophila hibris, a gene related to human nephrin
    • Dworak H.A., Charles M.A., Pellerano L.B., Sink H. Characterization of Drosophila hibris, a gene related to human nephrin. Development 2001, 128:4265-4276.
    • (2001) Development , vol.128 , pp. 4265-4276
    • Dworak, H.A.1    Charles, M.A.2    Pellerano, L.B.3    Sink, H.4
  • 11
    • 1642634997 scopus 로고    scopus 로고
    • Synaptic specificity is generated by the synaptic guidepost protein SYG-2 and its receptor, SYG-1
    • 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 2004, 116:869-881.
    • (2004) Cell , vol.116 , pp. 869-881
    • Shen, K.1    Fetter, R.D.2    Bargmann, C.I.3
  • 12
    • 0037423919 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein SYG-1 determines the location of specific synapses in C. elegans
    • Shen K., Bargmann C.I. The immunoglobulin superfamily protein SYG-1 determines the location of specific synapses in C. elegans. Cell 2003, 112:619-630.
    • (2003) Cell , vol.112 , pp. 619-630
    • Shen, K.1    Bargmann, C.I.2
  • 13
    • 52049108702 scopus 로고    scopus 로고
    • Functional dissection of SYG-1 and SYG-2, cell adhesion molecules required for selective synaptogenesis in C. elegans
    • Chao D.L., Shen K. Functional dissection of SYG-1 and SYG-2, cell adhesion molecules required for selective synaptogenesis in C. elegans. Mol. Cell. Neurosci. 2008, 39:248-257.
    • (2008) Mol. Cell. Neurosci. , vol.39 , pp. 248-257
    • Chao, D.L.1    Shen, K.2
  • 14
    • 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. 2003, 278:19266-19271.
    • (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
  • 15
    • 58149138860 scopus 로고    scopus 로고
    • Bidirectional modulation of synaptic functions by Eph/ephrin signaling
    • Klein R. Bidirectional modulation of synaptic functions by Eph/ephrin signaling. Nat. Neurosci. 2009, 12:15-20.
    • (2009) Nat. Neurosci. , vol.12 , pp. 15-20
    • Klein, R.1
  • 16
    • 78349252732 scopus 로고    scopus 로고
    • Eph/ephrin molecules-a hub for signaling and endocytosis
    • Pitulescu M.E., Adams R.H. Eph/ephrin molecules-a hub for signaling and endocytosis. Genes Dev. 2010, 24:2480-2492.
    • (2010) Genes Dev. , vol.24 , pp. 2480-2492
    • Pitulescu, M.E.1    Adams, R.H.2
  • 17
    • 77949484882 scopus 로고    scopus 로고
    • A role of receptor Notch in ligand cis-inhibition in Drosophila
    • Becam I., Fiuza U.M., Arias A.M., Milan M. A role of receptor Notch in ligand cis-inhibition in Drosophila. Curr. Biol. 2010, 20:554-560.
    • (2010) Curr. Biol. , vol.20 , pp. 554-560
    • Becam, I.1    Fiuza, U.M.2    Arias, A.M.3    Milan, M.4
  • 18
    • 68849110194 scopus 로고    scopus 로고
    • Cis-Inhibition of Notch by endogenous Delta biases the outcome of lateral inhibition
    • Miller A.C., Lyons E.L., Herman T.G. cis-Inhibition of Notch by endogenous Delta biases the outcome of lateral inhibition. Curr. Biol. 2009, 19:1378-1383.
    • (2009) Curr. Biol. , vol.19 , pp. 1378-1383
    • Miller, A.C.1    Lyons, E.L.2    Herman, T.G.3
  • 19
    • 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. 2007, 27:8698-8712.
    • (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
  • 20
    • 33646401549 scopus 로고    scopus 로고
    • Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization
    • Verma R., Kovari I., Soofi A., Nihalani D., Patrie K., Holzman L.B. Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization. J. Clin. Invest. 2006, 116:1346-1359.
    • (2006) J. Clin. Invest. , vol.116 , pp. 1346-1359
    • Verma, R.1    Kovari, I.2    Soofi, A.3    Nihalani, D.4    Patrie, K.5    Holzman, L.B.6
  • 25
    • 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. 2004, 15:3006-3015.
    • (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
  • 27
  • 30
    • 17144405654 scopus 로고    scopus 로고
    • Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir
    • Campellone K.G., Leong J.M. Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir. Mol. Microbiol. 2005, 56:416-432.
    • (2005) Mol. Microbiol. , vol.56 , pp. 416-432
    • Campellone, K.G.1    Leong, J.M.2
  • 36
    • 79956071512 scopus 로고    scopus 로고
    • Podocyte-specific deletion of Myh9 encoding nonmuscle myosin heavy chain 2A predisposes mice to glomerulopathy
    • Johnstone D.B., Zhang J., George B., Leon C., Gachet C., Wong H., Parekh R., Holzman L.B. Podocyte-specific deletion of Myh9 encoding nonmuscle myosin heavy chain 2A predisposes mice to glomerulopathy. Mol. Cell. Biol. 2011, 31:2162-2170.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2162-2170
    • Johnstone, D.B.1    Zhang, J.2    George, B.3    Leon, C.4    Gachet, C.5    Wong, H.6    Parekh, R.7    Holzman, L.B.8
  • 38
    • 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., Wagner M.C., Johnstone D.B., Wong H.N., George B., Pruthi P.A., Lazzara M.J., Nihalani D. Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane. Mol. Cell. Biol. 2011, 31:2134-2150.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2134-2150
    • Arif, E.1    Wagner, M.C.2    Johnstone, D.B.3    Wong, H.N.4    George, B.5    Pruthi, P.A.6    Lazzara, M.J.7    Nihalani, D.8
  • 40
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • Krendel M., Osterweil E.K., Mooseker M.S. Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett. 2007, 581:644-650.
    • (2007) FEBS Lett. , vol.581 , pp. 644-650
    • Krendel, M.1    Osterweil, E.K.2    Mooseker, M.S.3
  • 43
    • 37849026460 scopus 로고    scopus 로고
    • Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus
    • Kanasaki K., Kanda Y., Palmsten K., Tanjore H., Lee S.B., Lebleu V.S., Gattone V.H., Kalluri R. Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus. Dev. Biol. 2008, 313:584-593.
    • (2008) Dev. Biol. , vol.313 , pp. 584-593
    • Kanasaki, K.1    Kanda, Y.2    Palmsten, K.3    Tanjore, H.4    Lee, S.B.5    Lebleu, V.S.6    Gattone, V.H.7    Kalluri, R.8
  • 45
    • 0032787837 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK): a regulator of integrin and growth-factor signalling
    • Dedhar S., Williams B., Hannigan G. Integrin-linked kinase (ILK): a regulator of integrin and growth-factor signalling. Trends Cell Biol. 1999, 9:319-323.
    • (1999) Trends Cell Biol. , vol.9 , pp. 319-323
    • Dedhar, S.1    Williams, B.2    Hannigan, G.3
  • 48
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • Owen J.D., Ruest P.J., Fry D.W., Hanks S.K. Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. Mol. Cell. Biol. 1999, 19:4806-4818.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 49
    • 0036357414 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration
    • Panetti T.S. Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration. Front. Biosci. 2002, 7:d143-d150.
    • (2002) Front. Biosci. , vol.7
    • Panetti, T.S.1
  • 50
    • 76849100707 scopus 로고    scopus 로고
    • Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis
    • Luo M., Guan J.L. Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis. Cancer Lett. 2010, 289:127-139.
    • (2010) Cancer Lett. , vol.289 , pp. 127-139
    • Luo, M.1    Guan, J.L.2
  • 51
    • 58349108303 scopus 로고    scopus 로고
    • Mammary epithelial-specific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells
    • Luo M., Fan H., Nagy T., Wei H., Wang C., Liu S., Wicha M.S., Guan J.L. Mammary epithelial-specific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells. Cancer Res. 2009, 69:466-474.
    • (2009) Cancer Res. , vol.69 , pp. 466-474
    • Luo, M.1    Fan, H.2    Nagy, T.3    Wei, H.4    Wang, C.5    Liu, S.6    Wicha, M.S.7    Guan, J.L.8
  • 57
    • 34248374374 scopus 로고    scopus 로고
    • Placental ischemia and soluble fms-like tyrosine kinase 1: cause or consequence of preeclampsia?
    • Karumanchi S.A., Epstein F.H. Placental ischemia and soluble fms-like tyrosine kinase 1: cause or consequence of preeclampsia?. Kidney Int. 2007, 71:959-961.
    • (2007) Kidney Int. , vol.71 , pp. 959-961
    • Karumanchi, S.A.1    Epstein, F.H.2
  • 58
    • 85168832555 scopus 로고    scopus 로고
    • Parietal epithelial cells: their role in health and disease
    • Romagnani P. Parietal epithelial cells: their role in health and disease. Contrib. Nephrol. 2011, 169:23-36.
    • (2011) Contrib. Nephrol. , vol.169 , pp. 23-36
    • Romagnani, P.1
  • 59
    • 77952561383 scopus 로고    scopus 로고
    • Glomerular epithelial stem cells: the good, the bad, and the ugly
    • Lasagni L., Romagnani P. Glomerular epithelial stem cells: the good, the bad, and the ugly. J. Am. Soc. Nephrol. 2010, 21:1612-1619.
    • (2010) J. Am. Soc. Nephrol. , vol.21 , pp. 1612-1619
    • Lasagni, L.1    Romagnani, P.2
  • 62
    • 33645266951 scopus 로고    scopus 로고
    • Podocyte hypertrophy, "adaptation," and "decompensation" associated with glomerular enlargement and glomerulosclerosis in the aging rat: prevention by calorie restriction
    • Wiggins J.E., Goyal M., Sanden S.K., Wharram B.L., Shedden K.A., Misek D.E., Kuick R.D., Wiggins R.C. Podocyte hypertrophy, "adaptation," and "decompensation" associated with glomerular enlargement and glomerulosclerosis in the aging rat: prevention by calorie restriction. J. Am. Soc. Nephrol. 2005, 16:2953-2966.
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 2953-2966
    • Wiggins, J.E.1    Goyal, M.2    Sanden, S.K.3    Wharram, B.L.4    Shedden, K.A.5    Misek, D.E.6    Kuick, R.D.7    Wiggins, R.C.8
  • 63
    • 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. 2007, 71:1205-1214.
    • (2007) Kidney Int. , vol.71 , pp. 1205-1214
    • Wiggins, R.C.1
  • 66
    • 79952352658 scopus 로고    scopus 로고
    • Dynamics of the Rho-family small GTPases in actin regulation and motility
    • Spiering D., Hodgson L. Dynamics of the Rho-family small GTPases in actin regulation and motility. Cell Adh. Migr. 2011, 5:170-180.
    • (2011) Cell Adh. Migr. , vol.5 , pp. 170-180
    • Spiering, D.1    Hodgson, L.2
  • 67
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science (New York, N.Y.) 1998, 279:509-514.
    • (1998) Science (New York, N.Y.) , vol.279 , pp. 509-514
    • Hall, A.1
  • 69
    • 33744969296 scopus 로고    scopus 로고
    • Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling
    • Asanuma K., Yanagida-Asanuma E., Faul C., Tomino Y., Kim K., Mundel P. Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling. Nat. Cell Biol. 2006, 8:485-491.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 485-491
    • Asanuma, K.1    Yanagida-Asanuma, E.2    Faul, C.3    Tomino, Y.4    Kim, K.5    Mundel, P.6
  • 72
    • 15044350668 scopus 로고    scopus 로고
    • The expanding TOR signaling network
    • Martin D.E., Hall M.N. The expanding TOR signaling network. Curr. Opin. Cell Biol. 2005, 17:158-166.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 158-166
    • Martin, D.E.1    Hall, M.N.2
  • 73
    • 33645738458 scopus 로고    scopus 로고
    • Complexity of the TOR signaling network
    • Inoki K., Guan K.L. Complexity of the TOR signaling network. Trends Cell Biol. 2006, 16:206-212.
    • (2006) Trends Cell Biol. , vol.16 , pp. 206-212
    • Inoki, K.1    Guan, K.L.2
  • 77
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • Levine B., Klionsky D.J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 2004, 6:463-477.
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 81
    • 79953834002 scopus 로고    scopus 로고
    • Implications of autophagy for glomerular aging and disease
    • Weide T., Huber T.B. Implications of autophagy for glomerular aging and disease. Cell Tissue Res. 2011, 343:467-473.
    • (2011) Cell Tissue Res. , vol.343 , pp. 467-473
    • Weide, T.1    Huber, T.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.