The insect nephrocyte is a podocyte-like cell with a filtration slit diaphragm

Nature

Volumn 457, Issue 7227, 2009, Pages 322-326

  Weavers, Helen ^a   Prieto Sánchez, Silvia ^b   Grawe, Ferdinand ^c   Garcia López, Amparo ^d   Artero, Ruben ^d   Wilsch Bräuninger, Michaela ^e   Ruiz Gómez, Mar ^b   Skaer, Helen ^a   Denholm, Barry ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b CENTRO DE BIOLOGÍA MOLECULAR SEVERO OCHOA   (Spain)

^c HEINRICH HEINE UNIVERSITY   (Germany)

^d UNIVERSITY OF VALENCIA   (Spain)

^e MAX PLANCK INSTITUTE OF MOLECULAR CELL BIOLOGY AND GENETICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CD2 ASSOCIATED PROTEIN; NEPHRIN; PODOCIN; PROTEIN ZO1;

CYTOLOGY; EXCRETION; FLY; GENE EXPRESSION; INSECT;

ANIMAL CELL; ARTICLE; CELL FUNCTION; CELL SEPARATION; CONTROLLED STUDY; DIAPHRAGM; DROSOPHILA MELANOGASTER; KIDNEY CELL; NONHUMAN; PHENOTYPE; PODOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION;

ANIMALS; CELL LINE; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; IMMUNOGLOBULINS; MEMBRANE PROTEINS; MUSCLE PROTEINS; PODOCYTES;

DROSOPHILA MELANOGASTER; HEXAPODA; INVERTEBRATA; VERTEBRATA;

EID: 58249123367     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07526     Document Type: Article

References (32)

1. Smith, H. W. From Fish to Philosopher (Little, Brown, 1953).
2. Ruppert, E. E. Evolutionary origin of the vertebrate nephron. Am. Zool. 34, 542-533 (1994).
3. Rodewald, R. & Karnovsky, M. J. Porous substructure of the glomerular slit diaphragm in the rat and mouse. J. Cell Biol. 60, 423-433 (1974).
4. 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).
5. Patrakka, J. et al. Congenital nephrotic syndrome (NPHS1): features resulting from different mutations in Finnish patients. Kidney Int. 58, 972-980 (2000).
6. Berridge, M. J. & Oschman, J. L. Transporting Epithelia 11-15 (Academic, 1972).
7. Crossley, A. C. in Comprehensive Insect Physiology, Biochemistry and Pharmacology (eds Kerkut, G. A. & Gilbert, L. I.) 487-515 (Pergamon, 1985).
8. Kowalevsky, A. Ein Beitrag zur Kenntnis der Excretions-organe. Biol. Centralbl. 9, 74-79 (1889).
9. Locke, M. & Russell, V. W. in Microscopic Anatomy of Invertebrates (eds Harrison, F. W. & Locke, M.) 687-709 (Wiley, 1998).
10. 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).
11. Sellin, L. et al. NEPH1 defines a novel family of podocin interacting proteins. FASEB J. 17, 115-117 (2003).
12. Ruotsalainen, V. et al. Nephrin is specifically located at the slit diaphragm of glomerular podocytes. Proc. Natl Acad. Sci. USA 96, 7962-7967 (1999).
13. 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).
14. 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).
15. Khoshnoodi, J. et al. Nephrin promotes cell-cell adhesion through homophilic interactions. Am. J. Pathol. 163, 2337-2346 (2003).
16. 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).
17. 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).
18. Tepass, U. & Hartenstein, V. The development of cellular junctions in the Drosophila embryo. Dev. Biol. 161, 563-596 (1994).
19. Rugendorff, A., Younossi-Hartenstein, A. & Hartenstein, V. Embryonic origin and differentiation of the Drosophila heart. Rouxs Arch. Dev. Biol. 203, 266-280 (1994).
20. Huber, T. B. et al. The carboxyl terminus of Neph family members binds to the PDZ domain protein zonula occludens-1. J. Biol. Chem. 278, 13417-13421 (2003).
21. Shih, N. Y. et al. Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science 286, 312-315 (1999).
22. Shih, N. Y. et al. CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain. Am. J. Pathol. 159, 2303-2308 (2001).
23. Boute, N. et al. NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome. Nature Genet. 24, 349-354 (2000).
24. Kim, J. M. et al. CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility. Science 300, 1298-1300 (2003).
25. 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).
26. Galletta, B. J., Chakravarti, M., Banerjee, R. & Abmayr, S. M. SNS: Adhesive properties, localization requirements and ectodomain dependence in S2 cells and embryonic myoblasts. Mech. Dev. 121, 1455-1468 (2004).
27. 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).
28. Akilesh, S. et al. Podocytes use FcRn to clear IgG from the glomerular basement membrane. Proc. Natl Acad. Sci. USA 105, 967-972 (2008).
29. Das, D., Aradhya, R., Ashoka, D. & Inamdar, M. Post-embryonic pericardial cells of Drosophila are required for overcoming toxic stress but not for cardiac function or adult development. Cell Tissue Res. 331, 565-570 (2008).
30. Huber, T. B. & Benzing, T. The slit diaphragm: a signaling platform to regulate podocyte function. Curr. Opin. Nephrol. Hypertens. 14, 211-216 (2005).
31. Nagel, A. C., Maier, D. & Preiss, A. Green fluorescent protein as a convenient and versatile marker for studies on functional genomics in Drosophila. Dev. Genes Evol. 212, 93-98 (2002).
32. Strunkelnberg, M. et al. rst and its paralogue kirre act redundantly during embryonic muscle development in Drosophila. Development 128, 4229-4239 (2001).