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Volumn 14, Issue 9, 2008, Pages 931-938

The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCINEURIN; CATHEPSIN L; CYCLOSPORIN A; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SYNAPTOPODIN; TRANSCRIPTION FACTOR NFAT;

EID: 51349162919     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.1857     Document Type: Article
Times cited : (824)

References (43)
  • 1
    • 0034126357 scopus 로고    scopus 로고
    • Getting a foothold in nephrotic syndrome
    • Somlo, S. & Mundel, P. Getting a foothold in nephrotic syndrome. Nat. Genet. 24, 333-335 (2000).
    • (2000) Nat. Genet , vol.24 , pp. 333-335
    • Somlo, S.1    Mundel, P.2
  • 2
    • 33645403170 scopus 로고    scopus 로고
    • Hereditary proteinuria syndromes and mechanisms of proteinuria
    • Tryggvason, K., Patrakka, J. & Wartiovaara, J. Hereditary proteinuria syndromes and mechanisms of proteinuria. N. Engl. J. Med. 354, 1387-1401 (2006).
    • (2006) N. Engl. J. Med , vol.354 , pp. 1387-1401
    • Tryggvason, K.1    Patrakka, J.2    Wartiovaara, J.3
  • 3
    • 33646068033 scopus 로고    scopus 로고
    • Nck links nephrin to actin in kidney podocytes
    • Tryggvason, K., Pikkarainen, T. & Patrakka, J. Nck links nephrin to actin in kidney podocytes. Cell 125, 221-224 (2006).
    • (2006) Cell , vol.125 , pp. 221-224
    • Tryggvason, K.1    Pikkarainen, T.2    Patrakka, J.3
  • 4
    • 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
  • 5
    • 0030816323 scopus 로고    scopus 로고
    • Synaptopodin: An actin-associated protein in telencephalic dendrites and renal podocytes
    • Mundel, P. et al. Synaptopodin: an actin-associated protein in telencephalic dendrites and renal podocytes. J. Cell Biol. 139, 193-204 (1997).
    • (1997) J. Cell Biol , vol.139 , pp. 193-204
    • Mundel, P.1
  • 6
    • 18244384042 scopus 로고    scopus 로고
    • Synaptopodin regulates the actin-bundling activity of α-actinin in an isoform-specific manner
    • Asanuma, K. et al. Synaptopodin regulates the actin-bundling activity of α-actinin in an isoform-specific manner. J. Clin. Invest. 115, 1188-1198 (2005).
    • (2005) J. Clin. Invest , vol.115 , pp. 1188-1198
    • Asanuma, K.1
  • 7
    • 33646406847 scopus 로고    scopus 로고
    • Bigenic mouse models of focal segmental glomerulosclerosis involving pairwise interaction of CD2AP, Fyn and synaptopodin
    • Huber, T.B. et al. Bigenic mouse models of focal segmental glomerulosclerosis involving pairwise interaction of CD2AP, Fyn and synaptopodin. J. Clin. Invest. 116, 1337-1345 (2006).
    • (2006) J. Clin. Invest , vol.116 , pp. 1337-1345
    • Huber, T.B.1
  • 8
    • 33744969296 scopus 로고    scopus 로고
    • Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling
    • Asanuma, K. et al. Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling. Nat. Cell Biol. 8, 485-491 (2006).
    • (2006) Nat. Cell Biol , vol.8 , pp. 485-491
    • Asanuma, K.1
  • 9
    • 34548324281 scopus 로고    scopus 로고
    • Synaptopodin protects against proteinuria by disrupting Cdc42-IRSp53-Mena signaling complexes in kidney podocytes
    • Yanagida-Asanuma, E. et al. Synaptopodin protects against proteinuria by disrupting Cdc42-IRSp53-Mena signaling complexes in kidney podocytes. Am. J. Pathol. 171, 415-427 (2007).
    • (2007) Am. J. Pathol , vol.171 , pp. 415-427
    • Yanagida-Asanuma, E.1
  • 10
    • 2442453767 scopus 로고    scopus 로고
    • Calcineurin: A central controller of signalling in eukaryotes
    • 343-348
    • Aramburu, J., Heitman, J. & Crabtree, G.R. Calcineurin: a central controller of signalling in eukaryotes. EMBO Rep. 5, 343-348 (2004).
    • (2004) EMBO Rep , vol.5
    • Aramburu, J.1    Heitman, J.2    Crabtree, G.R.3
  • 11
    • 0036234543 scopus 로고    scopus 로고
    • NFAT signaling: Choreographing the social lives of cells
    • Crabtree, G.R. & Olson, E.N. NFAT signaling: choreographing the social lives of cells. Cell 109 Suppl, S67-S79 (2002).
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Crabtree, G.R.1    Olson, E.N.2
  • 12
    • 33748929299 scopus 로고    scopus 로고
    • Calcineurin-NFAT signalling regulates pancreatic beta cell growth and function
    • Heit, J.J. et al. Calcineurin-NFAT signalling regulates pancreatic beta cell growth and function. Nature 443, 345-349 (2006).
    • (2006) Nature , vol.443 , pp. 345-349
    • Heit, J.J.1
  • 13
    • 38649106497 scopus 로고    scopus 로고
    • NFATc1 balances quiescence and proliferation of skin stem cells
    • Horsley, V., Aliprantis, A.O., Polak, L., Glimcher, L.H. & Fuchs, E. NFATc1 balances quiescence and proliferation of skin stem cells. Cell 132, 299-310 (2008).
    • (2008) Cell , vol.132 , pp. 299-310
    • Horsley, V.1    Aliprantis, A.O.2    Polak, L.3    Glimcher, L.H.4    Fuchs, E.5
  • 14
    • 23844515714 scopus 로고    scopus 로고
    • NFAT and Osterix cooperatively regulate bone formation
    • Koga, T. et al. NFAT and Osterix cooperatively regulate bone formation. Nat. Med. 11, 880-885 (2005).
    • (2005) Nat. Med , vol.11 , pp. 880-885
    • Koga, T.1
  • 15
    • 23744484424 scopus 로고    scopus 로고
    • Treatment of focal segmental glomerulosclerosis
    • Meyrier, A. Treatment of focal segmental glomerulosclerosis. Expert Opin. Pharmacother. 6, 1539-1549 (2005).
    • (2005) Expert Opin. Pharmacother , vol.6 , pp. 1539-1549
    • Meyrier, A.1
  • 16
    • 33846456191 scopus 로고    scopus 로고
    • Cyclosporin therapy in patients with Alport syndrome
    • Charbit, M. et al. Cyclosporin therapy in patients with Alport syndrome. Pediatr. Nephrol. 22, 57-63 (2007).
    • (2007) Pediatr. Nephrol , vol.22 , pp. 57-63
    • Charbit, M.1
  • 17
    • 0347418134 scopus 로고    scopus 로고
    • Cyclosporine A slows the progressive renal disease of alport syndrome (X-linked hereditary nephritis): Results from a canine model
    • Chen, D. et al. Cyclosporine A slows the progressive renal disease of alport syndrome (X-linked hereditary nephritis): results from a canine model. J. Am. Soc. Nephrol. 14, 690-698 (2003).
    • (2003) J. Am. Soc. Nephrol , vol.14 , pp. 690-698
    • Chen, D.1
  • 18
    • 85047691168 scopus 로고    scopus 로고
    • Induction of B7-1 in podocytes is associated with nephrotic syndrome
    • Reiser, J. et al. Induction of B7-1 in podocytes is associated with nephrotic syndrome. J. Clin. Invest. 113, 1390-1397 (2004).
    • (2004) J. Clin. Invest , vol.113 , pp. 1390-1397
    • Reiser, J.1
  • 20
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3-phosphopeptide binding specificity
    • Yaffe, M.B. et al. The structural basis for 14-3-3-phosphopeptide binding specificity. Cell 91, 961-971 (1997).
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1
  • 21
    • 36849051314 scopus 로고    scopus 로고
    • 2+-calmodulin-dependent kinase II and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes
    • 2+-calmodulin-dependent kinase II and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes. Mol. Cell. Biol. 27, 8215-8227 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 8215-8227
    • Faul, C.1    Dhume, A.2    Schecter, A.D.3    Mundel, P.4
  • 22
    • 0026632557 scopus 로고    scopus 로고
    • O'Keefe, S.J., Tamura, J., Kincaid, R.L., Tocci, M.J. & O'Neill, E.A. FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. Nature 357, 692-694 (1992).
    • O'Keefe, S.J., Tamura, J., Kincaid, R.L., Tocci, M.J. & O'Neill, E.A. FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. Nature 357, 692-694 (1992).
  • 23
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M.B. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513, 53-57 (2002).
    • (2002) FEBS Lett , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 24
    • 18844394800 scopus 로고    scopus 로고
    • Promotion of importin α-mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3
    • Faul, C. et al. Promotion of importin α-mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3. J. Cell Biol. 169, 415-424 (2005).
    • (2005) J. Cell Biol , vol.169 , pp. 415-424
    • Faul, C.1
  • 25
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A.J., Tanner, J.W., Allen, P.M. & Shaw, A.S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897 (1996).
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 26
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty, M.K. & Morrison, D.K. Unlocking the code of 14-3-3. J. Cell Sci. 117, 1875-1884 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 27
    • 0035977072 scopus 로고    scopus 로고
    • 14-3-3 proteins mediate an essential anti-apoptotic signal
    • Masters, S.C. & Fu, H. 14-3-3 proteins mediate an essential anti-apoptotic signal. J. Biol. Chem. 276, 45193-45200 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 45193-45200
    • Masters, S.C.1    Fu, H.2
  • 28
    • 4544377833 scopus 로고    scopus 로고
    • Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and a3 integrin
    • Reiser, J. et al. Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and a3 integrin. J. Biol. Chem. 279, 34827-34832 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 34827-34832
    • Reiser, J.1
  • 29
    • 34547654202 scopus 로고    scopus 로고
    • Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease
    • Sever, S. et al. Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease. J. Clin. Invest. 117, 2095-2104 (2007).
    • (2007) J. Clin. Invest , vol.117 , pp. 2095-2104
    • Sever, S.1
  • 30
    • 0038824700 scopus 로고    scopus 로고
    • Toward computer-based cleavage site prediction of cysteine endopeptidases
    • Lohmuller, T. et al. Toward computer-based cleavage site prediction of cysteine endopeptidases. Biol. Chem. 384, 899-909 (2003).
    • (2003) Biol. Chem , vol.384 , pp. 899-909
    • Lohmuller, T.1
  • 31
    • 0034660447 scopus 로고    scopus 로고
    • 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells
    • Cotelle, V. et al. 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells. EMBO J. 19, 2869-2876 (2000).
    • (2000) EMBO J , vol.19 , pp. 2869-2876
    • Cotelle, V.1
  • 32
    • 0025776521 scopus 로고
    • Evidence suggesting a role for cathepsin L in an experimental model of glomerulonephritis
    • Baricos, W.H. et al. Evidence suggesting a role for cathepsin L in an experimental model of glomerulonephritis. Arch. Biochem. Biophys. 288, 468-472 (1991).
    • (1991) Arch. Biochem. Biophys , vol.288 , pp. 468-472
    • Baricos, W.H.1
  • 33
    • 0020663062 scopus 로고
    • A severe combined immunodeficiency mutation in the mouse
    • Bosma, G.C., Custer, R.P. & Bosma, M.J. A severe combined immunodeficiency mutation in the mouse. Nature 301, 527-530 (1983).
    • (1983) Nature , vol.301 , pp. 527-530
    • Bosma, G.C.1    Custer, R.P.2    Bosma, M.J.3
  • 34
    • 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
  • 35
    • 14944375866 scopus 로고    scopus 로고
    • Impact of cyclosporin on podocyte ZO-1 expression in puromycin aminonucleoside nephrosis rats
    • Kim, B.S. et al. Impact of cyclosporin on podocyte ZO-1 expression in puromycin aminonucleoside nephrosis rats. Yonsei Med. J. 46, 141-148 (2005).
    • (2005) Yonsei Med. J , vol.46 , pp. 141-148
    • Kim, B.S.1
  • 36
    • 0042844707 scopus 로고    scopus 로고
    • Inducible podocyte-specific gene expression in transgenic mice
    • Shigehara, T. et al. Inducible podocyte-specific gene expression in transgenic mice. J. Am. Soc. Nephrol. 14, 1998-2003 (2003).
    • (2003) J. Am. Soc. Nephrol , vol.14 , pp. 1998-2003
    • Shigehara, T.1
  • 37
    • 15444378543 scopus 로고    scopus 로고
    • Cellular stability of serotonin N-acetyltransferase conferred by phosphonodifluoromethylene alanine (Pfa) substitution for Ser-205
    • Zheng, W. et al. Cellular stability of serotonin N-acetyltransferase conferred by phosphonodifluoromethylene alanine (Pfa) substitution for Ser-205. J. Biol. Chem. 280, 10462-10467 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 10462-10467
    • Zheng, W.1
  • 38
    • 33845317604 scopus 로고    scopus 로고
    • TRPC6 fulfills a calcineurin signaling circuit during pathologic cardiac remodeling
    • Kuwahara, K. et al. TRPC6 fulfills a calcineurin signaling circuit during pathologic cardiac remodeling. J. Clin. Invest. 116, 3114-3126 (2006).
    • (2006) J. Clin. Invest , vol.116 , pp. 3114-3126
    • Kuwahara, K.1
  • 39
    • 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
  • 40
    • 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
  • 41
    • 33846028228 scopus 로고    scopus 로고
    • Induction of TRPC6 channel in acquired forms of proteinuric kidney disease
    • Moller, C.C. et al. Induction of TRPC6 channel in acquired forms of proteinuric kidney disease. J. Am. Soc. Nephrol. 18, 29-36 (2007).
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 29-36
    • Moller, C.C.1
  • 42
    • 10844292763 scopus 로고    scopus 로고
    • Immunosuppressive drugs for kidney transplantation
    • Halloran, P.F. Immunosuppressive drugs for kidney transplantation. N. Engl. J. Med. 351, 2715-2729 (2004).
    • (2004) N. Engl. J. Med , vol.351 , pp. 2715-2729
    • Halloran, P.F.1
  • 43
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • Goulet, B. et al. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol. Cell 14, 207-219 (2004).
    • (2004) Mol. Cell , vol.14 , pp. 207-219
    • Goulet, B.1


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