Role of polycystins in renal tubulogenesis

Trends in Cell Biology

Volumn 13, Issue 9, 2003, Pages 484-492

  Boletta, Alessandra ^a   Germino, Gregory G ^b  

^a DULBECCO TELETHON INSTITUTE   (Italy)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; POLYCYSTIN;

AUTOSOMAL DISORDER; CELL ACTIVITY; COMPLEX FORMATION; HUMAN; IN VITRO STUDY; IN VIVO STUDY; KIDNEY POLYCYSTIC DISEASE; KIDNEY TUBULE; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; REVIEW; SIGNAL TRANSDUCTION;

EID: 0142106807     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(03)00169-7     Document Type: Review

References (76)

1. Gabow P.A. Autosomal dominant polycystic kidney disease. New Engl. J. Med. 329:1993;332-342.
2. Hughes J., et al. The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains. Nat. Genet. 10:1995;151-160.
3. Boletta A., et al. Biochemical characterization of bona fide polycystin-1 in vitro and in vivo. Am. J. Kidney Dis. 38:2001;1421-1429.
4. Hanaoka K., et al. Co-assembly of polycystin-1 and -2 produces unique cation-permeable currents. Nature. 408:2000;990-994.
5. Newby L.J., et al. Identification, characterization, and localization of a novel kidney polycystin-1-polycystin-2 complex. J. Biol. Chem. 277:2002;20763-20773.
6. Sandford R., et al. The polycystins: a novel class of membrane-associated proteins involved in renal cystic disease. Cell. Mol. Life Sci. 56:1999;567-579.
7. Qian F., et al. PKD1 interacts with PKD2 through a probable coiled-coil domain. Nat. Genet. 16:1997;179-183.
8. Tsiokas L., et al. Homo- and heterodimeric interactions between the gene products of PKD1 and PKD2. Proc. Natl. Acad. Sci. U. S. A. 94:1997;6965-6970.
9. Parnell S.C., et al. The polycystic kidney disease-1 protein, polycystin-1, binds and activates heterotrimeric G-proteins in vitro. Biochem. Biophys. Res. Commun. 251:1998;625-631.
10. Parnell S.C., et al. Polycystin-1 activation of c-Jun N-terminal kinase and AP-1 is mediated by heterotrimeric G proteins. J. Biol. Chem. 277:2002;19566-19572.
11. Delmas P., et al. Constitutive activation of G-proteins by polycystin-1 is antagonized by polycystin-2. J. Biol. Chem. 277:2002;11276-11283.
12. Mochizuki T., et al. PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein. Science. 272:1996;1339-1342.
13. Tsiokas L., et al. Specific association of the gene product of PKD2 with the TRPC1 channel. Proc. Natl. Acad. Sci. U. S. A. 96:1999;3934-3939.
14. Montell C. Physiology, phylogeny and functions of the TRP superfamily of cation channels. Science STKE. 2001;. http://stke.sciencemag.org/cgi/content/ full/OC_sigtrans;2001/90/re1.
15. 2-permeable nonselective cation channel. Proc. Natl. Acad. Sci. U. S. A. 98:2001;1182-1187.
16. 2+-permeable cation channel in renal epithelia. Mol. Cell. Biol. 23:2003;2600-2607.
17. Koulen P., et al. Polycystin-2 is an intracellular calcium release channel. Nat. Cell Biol. 4:2002;191-197.
18. Baert L. Hereditary polycystic kidney disease (adult form): a microdissection study of two cases at an early stage of the disease. Kidney Int. 13:1978;519-525.
19. Qian F., et al. The molecular basis of focal cyst formation in human autosomal dominant polycystic kidney disease type I. Cell. 87:1996;979-987.
20. Pei Y., et al. Somatic PKD2 mutations in individual kidney and liver cysts support a 'two-hit' model of cystogenesis in type 2 autosomal dominant polycystic kidney disease. J. Am. Soc. Nephrol. 10:1999;1524-1529.
21. Lu W., et al. Perinatal lethality with kidney and pancreas defects in mice with a targeted PKD1 mutation. Nat. Genet. 17:1997;179-181.
22. Wu G., et al. Somatic inactivation of Pkd2 results in polycystic kidney disease. Cell. 93:1998;177-188.
23. Wu G., et al. Trans-heterozygous Pkd1 and Pkd2 mutations modify expression of polycystic kidney disease. Hum. Mol. Genet. 11:2002;1845-1854.
24. Watnick T., et al. Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations. Nat. Genet. 25:2000;143-144.
25. Koptides M., et al. Genetic evidence for a trans-heterozygous model for cystogenesis in autosomal dominant polycystic kidney disease. Hum. Mol. Genet. 9:2000;447-452.
26. Gabow P.A. Polycystic kidney disease: clues to pathogenesis. Kidney Int. 4:1991;989-996.
27. Chauvet V., et al. Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development. Am. J. Pathol. 160:2002;973-983.
28. van Adelsberg J. Peptides from the PKD repeats of polycystin, the PKD1 gene product, modulate pattern formation in the developing kidney. Dev. Genet. 24:1999;299-308.
29. Mah S.P., et al. Kidney development in cadherin-6 mutants: delayed mesenchyme-to-epithelial conversion and loss of nephrons. Dev. Biol. 223:2000;38-53.
30. Dahl U., et al. Genetic dissection of cadherin function during nephrogenesis. Mol. Cell. Biol. 22:2002;1474-1487.
31. Boletta A., et al. Polycystin-1, the gene product of PKD1, induces resistance to apoptosis and spontaneous tubulogenesis in MDCK cells. Mol. Cell. 6:2000;1267-1273.
32. Montesano R., et al. Induction of epithelial tubular morphogenesis in vitro by fibroblast-derived soluble factors. Cell. 66:1991;697-711.
33. O'Brien L.E., et al. Building epithelial architecture: insights from three-dimensional culture models. Nat. Rev. Mol. Cell Biol. 3:2002;531-537.
34. waf and regulation of the cell cycle via direct activation of the JAK/STAT signaling pathway in a process requiring PKD2. Cell. 109:2002;157-168.
35. MacDermot K.D., et al. Prenatal diagnosis of autosomal dominant polycystic kidney disease (PKD1) presenting in utero and prognosis for very early onset disease. J. Med. Genet. 35:1998;13-16.
36. Bukanov N., et al. Functional polycystin-1 expression is developmentally regulated during epithelial morphogenesis in vitro: downregulation and loss of membrane localization during cystogenesis. Hum. Mol. Genet. 11:2002;923-936.
37. Nickel C., et al. The polycystin-1 C-terminal fragment triggers branching morphogenesis and migration of tubular kidney epithelial cells. J. Clin. Invest. 109:2002;481-489.
38. Arnould T., et al. The polycystic kidney disease 1 gene product mediates protein kinase C alpha-dependent and c-Jun N-terminal kinase-dependent activation of the transcription factor AP-1. J. Biol. Chem. 273:1998;6013-6018.
39. Kim E., et al. The polycystic kidney disease 1 gene product modulates Wnt signaling. J. Biol. Chem. 274:1999;4947-4953.
40. Dressler G.R. Tubulogenesis in the developing kidney. Trends Cell Biol. 12:2002;390-395.
41. Derman M.P., et al. HGF-mediated chemotaxis and tubulogenesis require activation of the phosphatidylinositol 3-kinase. Am. J. Physiol. 268:1995;F1211-F1217.
42. Tang M.J., et al. Ureteric bud outgrowth in response to RET activation is mediated by phosphatidylinositol 3-kinase. Dev. Biol. 243:2002;128-136.
43. Boccaccio C., et al. Induction of epithelial tubules by growth factor HGF depends on the STAT pathway. Nature. 391:1998;285-288.
44. Barasch J., et al. Mesenchymal to epithelial conversion in rat metanephros is induced by LIF. Cell. 99:1999;377-386.
45. Qian F., et al. Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations. Proc. Natl. Acad. Sci. U. S. A. 99:2002;16981-16986.
46. Gallagher A.R., et al. The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 97:2000;4017-4022.
47. Lehtonen S., et al. In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2. J. Biol. Chem. 275:2000;32888-32893.
48. Li Q., et al. Polycystin-2 associates with tropomyosin-1, an actin microfilament component. J. Mol. Biol. 325:2003;949-962.
49. Li Q., et al. Polycystin-2 interacts with troponin I, an angiogenesis inhibitor. Biochemistry. 42:2003;450-457.
50. Ibraghimov-Beskrovnaya O., et al. Strong homophilic interactions of the Ig-like domains of polycystin-1, the protein product of an autosomal dominant polycystic kidney disease gene, PKD1. Hum. Mol. Genet. 9:2000;1641-1649.
51. Charron A.J., et al. Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells. J. Cell Biol. 149:2000;111-124.
52. Gumbiner B.M. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell. 84:1996;345-357.
53. Bukanov N.O., et al. A modified two-step phage display selection for isolation of polycystin-1 ligands. Funct. Integr. Genomics. 1:2000;193-199.
54. Malhas A.N., et al. Interaction of the leucine-rich repeats of polycystin-1 with extracellular matrix proteins: possible role in cell proliferation. J. Am. Soc. Nephrol. 13:2002;19-26.
55. Pazour G., et al. Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr. Biol. 12:2002;R378-R380.
56. Yoder B.K., et al. The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J. Am. Soc. Nephrol. 13:2002;2508-2516.
57. Nauli S.M., et al. Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat. Genet. 33:2003;129-137.
58. Pazour G.J., Rosenbaum J.L. Intraflagellar transport and cilia-dependent diseases. Trends Cell Biol. 12:2002;551-555.
59. Pazour G.J., Witman G.B. The vertebrate primary cilium is a sensory organelle. Curr. Opin. Cell Biol. 15:2003;105-110.
60. Praetorius H., Spring K.R. Bending the MDCK cell primary cilium increases intracellular calcium. J. Membr. Biol. 184:2001;71-79.
61. + channels in MDCK cells. J. Membr. Biol. 191:2003;193-200.
62. Tucker R.W., Pardee A.B. Centriole ciliation is related to quiescence and DNA synthesis in 3T3 cells. Cell. 17:1979;527-535.
63. Pazour G.J., et al. Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene Tg737, are required for assembly of cilia and flagella. J. Cell Biol. 151:2000;709-718.
64. Murcia N.S., et al. The Oak Ridge polycystic kidney (orpk) disease gene is required for left-right axis determination. Development. 127:2000;2347-2355.
65. Hirokawa N. Stirring up development with the heterotrimeric kinesis KIF3. Traffic. 1:2000;29-34.
66. Lin F., et al. Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease. Proc. Natl. Acad. Sci. U. S. A. 100:2003;5286-5291.
67. Hildebrandt F., Omram H. New insights: nephronophthisis-medullary cystic kidney disease. Pediatr. Nephrol. 16:2001;168-176.
68. Ostrowski L.E., et al. A proteomic analysis of human cilia: identification of novel components. Mol. Cell. Proteomics. 1:2002;451-465.
69. Mollet G., et al. The gene mutated in juvenile nephronophthisis type 4 encodes a novel protein that interacts with nephrocystin. Nat. Genet. 32:2002;300-305.
70. Wu G., et al. Cardiac defects and renal failure in mice with targeted mutations in Pkd2. Nat. Genet. 24:2000;75-78.
71. Pennekamp P., et al. The ion channel polycystin-2 is required for left-right axis determination in mice. Curr. Biol. 12:2002;938-943.
72. Watanabe D., et al. The left-right determinant Inversin is a component of node monocilia and other 9+0 cilia. Development. 130:2003;1725-1734.
73. Brown N.E., Murcia N.S. Delayed cystogenesis and increased ciliogenesis associated with the re-expression of polaris in Tg737 mutant mice. Kidney Int. 63:2003;1220-1229.
74. Germino G., Chapman A. Scriver C.R., et al. The Metabolic and Molecular Bases of Inherited Disease. 8th edn The Metabolic and Molecular Bases of Inherited Disease. 2001;5467-5492 McGraw-Hill.
75. Hou X., et al. Cystin, a novel cilia-associated protein, is disrupted in the cpk mouse model of polycystic kidney disease. J. Clin. Invest. 109:2002;533-540.
76. Romio L., et al. OFD1, the gene mutated in oral-facial-digital syndrome type 1, is expressed in the metanephros and in human embryonic renal mesenchymal cells. J. Am. Soc. Nephrol. 14:2003;680-689.