메뉴 건너뛰기




Volumn 88, Issue 4, 2015, Pages 699-710

A polycystin-centric view of cyst formation and disease: The polycystins revisited

Author keywords

ADPKD; PKD1; PKD2; polycystin 1; polycystin 2; TRPP2

Indexed keywords

CALCIUM; POLYCYSTIN; POLYCYSTIN 1; POLYCYSTIN 2; POLYCYSTIC KIDNEY DISEASE 1 PROTEIN; POLYCYSTIC KIDNEY DISEASE 2 PROTEIN;

EID: 84942983407     PISSN: 00852538     EISSN: 15231755     Source Type: Journal    
DOI: 10.1038/ki.2015.207     Document Type: Review
Times cited : (145)

References (198)
  • 1
    • 84929589777 scopus 로고    scopus 로고
    • Autosomal dominant polycystic kidney disease: The changing face of clinical management
    • Ong AC, Devuyst O, Knebelmann B et al. Autosomal dominant polycystic kidney disease: the changing face of clinical management. Lancet 2015; 385: 1993-2002.
    • (2015) Lancet , vol.385 , pp. 1993-2002
    • Ong, A.C.1    Devuyst, O.2    Knebelmann, B.3
  • 2
    • 84884580497 scopus 로고    scopus 로고
    • New treatments for autosomal dominant polycystic kidney disease
    • Chang MY, Ong AC. New treatments for autosomal dominant polycystic kidney disease. Br J Clin Pharmacol 2013; 76: 524-535.
    • (2013) Br J Clin Pharmacol , vol.76 , pp. 524-535
    • Chang, M.Y.1    Ong, A.C.2
  • 3
    • 84893266233 scopus 로고    scopus 로고
    • Evidence of a third ADPKD locus is not supported by re-analysis of designated PKD3 families
    • Paul BM, Consugar MB, Ryan Lee M et al. Evidence of a third ADPKD locus is not supported by re-analysis of designated PKD3 families. Kidney Int 2014; 85: 383-392.
    • (2014) Kidney Int , vol.85 , pp. 383-392
    • Paul, B.M.1    Consugar, M.B.2    Ryan Lee, M.3
  • 4
    • 84878695560 scopus 로고    scopus 로고
    • Type of PKD1 mutation influences renal outcome in ADPKD
    • Cornec-Le Gall E, Audrezet MP, Chen JM et al. Type of PKD1 mutation influences renal outcome in ADPKD. J Am Soc Nephrol 2013; 24: 1006-1013.
    • (2013) J Am Soc Nephrol , vol.24 , pp. 1006-1013
    • Cornec-Le Gall, E.1    Audrezet, M.P.2    Chen, J.M.3
  • 5
    • 16244414299 scopus 로고    scopus 로고
    • Molecular pathogenesis of ADPKD: The polycystin complex gets complex
    • Ong AC, Harris PC. Molecular pathogenesis of ADPKD: the polycystin complex gets complex. Kidney Int 2005; 67: 1234-1247.
    • (2005) Kidney Int , vol.67 , pp. 1234-1247
    • Ong, A.C.1    Harris, P.C.2
  • 6
    • 0033021438 scopus 로고    scopus 로고
    • Coordinate expression of the autosomal dominant polycystic kidney disease proteins, polycystin-2 and polycystin-1, in normal and cystic tissue
    • Ong AC, Ward CJ, Butler RJ et al. Coordinate expression of the autosomal dominant polycystic kidney disease proteins, polycystin-2 and polycystin-1, in normal and cystic tissue. Am J Pathol 1999; 154: 1721-1729.
    • (1999) Am J Pathol , vol.154 , pp. 1721-1729
    • Ong, A.C.1    Ward, C.J.2    Butler, R.J.3
  • 7
    • 0034095229 scopus 로고    scopus 로고
    • Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene
    • Foggensteiner L, Bevan AP, Thomas R et al. Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene. J Am Soc Nephrol 2000; 11: 814-827.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 814-827
    • Foggensteiner, L.1    Bevan, A.P.2    Thomas, R.3
  • 8
    • 0034191924 scopus 로고    scopus 로고
    • Distinct and common developmental expression patterns of the murine Pkd2 and Pkd1 genes
    • Guillaume R, Trudel M. Distinct and common developmental expression patterns of the murine Pkd2 and Pkd1 genes. Mech Dev 2000; 93: 179-183.
    • (2000) Mech Dev , vol.93 , pp. 179-183
    • Guillaume, R.1    Trudel, M.2
  • 9
    • 0030909957 scopus 로고    scopus 로고
    • PKD1 interacts with PKD2 through a probable coiled-coil domain
    • Qian F, Germino FJ, Cai Y et al. PKD1 interacts with PKD2 through a probable coiled-coil domain. Nat Genet 1997; 16: 179-183.
    • (1997) Nat Genet , vol.16 , pp. 179-183
    • Qian, F.1    Germino, F.J.2    Cai, Y.3
  • 10
    • 0030979629 scopus 로고    scopus 로고
    • Homo-and heterodimeric interactions between the gene products of PKD1 and PKD2
    • USA
    • Tsiokas L, Kim E, Arnould T et al. Homo-and heterodimeric interactions between the gene products of PKD1 and PKD2. Proc Natl Acad Sci USA 1997; 94: 6965-6970.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 6965-6970
    • Tsiokas, L.1    Kim, E.2    Arnould, T.3
  • 11
    • 0037036350 scopus 로고    scopus 로고
    • Identification, characterization, and localization of a novel kidney polycystin-1-polycystin-2 complex
    • Newby LJ, Streets AJ, Zhao Y et al. Identification, characterization, and localization of a novel kidney polycystin-1-polycystin-2 complex. J Biol Chem 2002; 277: 20763-20773.
    • (2002) J Biol Chem , vol.277 , pp. 20763-20773
    • Newby, L.J.1    Streets, A.J.2    Zhao, Y.3
  • 12
    • 0033214702 scopus 로고    scopus 로고
    • Identification and characterization of polycystin-2, the PKD2 gene product
    • Cai Y, Maeda Y, Cedzich A et al. Identification and characterization of polycystin-2, the PKD2 gene product. J Biol Chem 1999; 274: 28557-28565.
    • (1999) J Biol Chem , vol.274 , pp. 28557-28565
    • Cai, Y.1    Maeda, Y.2    Cedzich, A.3
  • 13
    • 0036122434 scopus 로고    scopus 로고
    • Polycystin-2 is an intracellular calcium release channel
    • Koulen P, Cai Y, Geng L et al. Polycystin-2 is an intracellular calcium release channel. Nat Cell Biol 2002; 4: 191-197.
    • (2002) Nat Cell Biol , vol.4 , pp. 191-197
    • Koulen, P.1    Cai, Y.2    Geng, L.3
  • 14
    • 77950536515 scopus 로고    scopus 로고
    • A polycystin-2 (TRPP2) dimerization domain essential for the function of heteromeric polycystin complexes
    • Giamarchi A, Feng S, Rodat-Despoix L et al. A polycystin-2 (TRPP2) dimerization domain essential for the function of heteromeric polycystin complexes. EMBO J 2010; 29: 1176-1191.
    • (2010) EMBO J , vol.29 , pp. 1176-1191
    • Giamarchi, A.1    Feng, S.2    Rodat-Despoix, L.3
  • 15
    • 84861481586 scopus 로고    scopus 로고
    • Polycystin-1 and polycystin-2 are both required to amplify inositol-trisphosphate-induced Ca(2+) release
    • Mekahli D, Sammels E, Luyten T et al. Polycystin-1 and polycystin-2 are both required to amplify inositol-trisphosphate-induced Ca(2+) release. Cell Calcium 2012; 51: 452-458.
    • (2012) Cell Calcium , vol.51 , pp. 452-458
    • Mekahli, D.1    Sammels, E.2    Luyten, T.3
  • 16
    • 0031252295 scopus 로고    scopus 로고
    • Perinatal lethality with kidney and pancreas defects in mice with a targetted Pkd1 mutation
    • Lu W, Peissel B, Babakhanlou H et al. Perinatal lethality with kidney and pancreas defects in mice with a targetted Pkd1 mutation. Nat Genet 1997; 17: 179-181.
    • (1997) Nat Genet , vol.17 , pp. 179-181
    • Lu, W.1    Peissel, B.2    Babakhanlou, H.3
  • 17
    • 0033989173 scopus 로고    scopus 로고
    • Cardiac defects and renal failure in mice with targeted mutations in Pkd2
    • Wu G, Markowitz GS, Li L et al. Cardiac defects and renal failure in mice with targeted mutations in Pkd2. Nat Genet 2000; 24: 75-78.
    • (2000) Nat Genet , vol.24 , pp. 75-78
    • Wu, G.1    Markowitz, G.S.2    Li, L.3
  • 18
    • 0030887477 scopus 로고    scopus 로고
    • Molecular basis of renal cyst formation-one hit or two
    • Ong AC, Harris PC. Molecular basis of renal cyst formation-one hit or two? Lancet 1997; 349: 1039-1040.
    • (1997) Lancet , vol.349 , pp. 1039-1040
    • Ong, A.C.1    Harris, P.C.2
  • 19
    • 0030582668 scopus 로고    scopus 로고
    • The molecular basis of focal cyst formation in human autosomal dominant polycystic kidney disease type i
    • Qian F, Watnick TJ, Onuchic LF et al. The molecular basis of focal cyst formation in human autosomal dominant polycystic kidney disease type I. Cell 1996; 87: 979-987.
    • (1996) Cell , vol.87 , pp. 979-987
    • Qian, F.1    Watnick, T.J.2    Onuchic, L.F.3
  • 20
    • 0032132758 scopus 로고    scopus 로고
    • Somatic mutation in individual liver cysts supports a two-hit model of cystogenesis in autosomal dominant polycystic kidney disease
    • Watnick TJ, Torres VE, Gandolph MA et al. Somatic mutation in individual liver cysts supports a two-hit model of cystogenesis in autosomal dominant polycystic kidney disease. Mol Cell 1998; 2: 247-251.
    • (1998) Mol Cell , vol.2 , pp. 247-251
    • Watnick, T.J.1    Torres, V.E.2    Gandolph, M.A.3
  • 21
    • 0033033706 scopus 로고    scopus 로고
    • Somatic PKD2 mutations in individual kidney and liver cysts support a "two-hit" model of cystogenesis in type 2 autosomal dominant polycystic kidney disease
    • Pei Y, Watnick T, He N 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 1999; 10: 1524-1529.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1524-1529
    • Pei, Y.1    Watnick, T.2    He, N.3
  • 22
    • 0032540226 scopus 로고    scopus 로고
    • Somatic inactivation of Pkd2 results in polycystic kidney disease
    • Wu G, D'Agati V, Cai Y et al. Somatic inactivation of Pkd2 results in polycystic kidney disease. Cell 1998; 93: 177-188.
    • (1998) Cell , vol.93 , pp. 177-188
    • Wu, G.1    D'Agati, V.2    Cai, Y.3
  • 23
    • 36849037019 scopus 로고    scopus 로고
    • A critical developmental switch defines the kinetics of kidney cyst formation after loss of Pkd1
    • Piontek K, Menezes LF, Garcia-Gonzalez MA et al. A critical developmental switch defines the kinetics of kidney cyst formation after loss of Pkd1. Nat Med 2007; 13: 1490-1495.
    • (2007) Nat Med , vol.13 , pp. 1490-1495
    • Piontek, K.1    Menezes, L.F.2    Garcia-Gonzalez, M.A.3
  • 24
    • 36249030528 scopus 로고    scopus 로고
    • Kidneyspecific inactivation of the Pkd1 gene induces rapid cyst formation in developing kidneys and a slow onset of disease in adult mice
    • Lantinga-van Leeuwen IS, Leonhard WN, van der Wal A et al. Kidneyspecific inactivation of the Pkd1 gene induces rapid cyst formation in developing kidneys and a slow onset of disease in adult mice. Hum Mol Genet 2007; 16: 3188-3196.
    • (2007) Hum Mol Genet , vol.16 , pp. 3188-3196
    • Lantinga-Van Leeuwen, I.S.1    Leonhard, W.N.2    Van Der Wal, A.3
  • 25
    • 33750689517 scopus 로고    scopus 로고
    • Cyst number but not the rate of cystic growth is associated with the mutated gene in autosomal dominant polycystic kidney disease
    • Harris PC, Bae KT, Rossetti S et al. Cyst number but not the rate of cystic growth is associated with the mutated gene in autosomal dominant polycystic kidney disease. J Am Soc Nephrol 2006; 17: 3013-3019.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 3013-3019
    • Harris, P.C.1    Bae, K.T.2    Rossetti, S.3
  • 26
    • 19944406428 scopus 로고    scopus 로고
    • Lowering of Pkd1 expression is sufficient to cause polycystic kidney disease
    • Lantinga-van Leeuwen IS, Dauwerse JG, Baelde HJ et al. Lowering of Pkd1 expression is sufficient to cause polycystic kidney disease. Hum Mol Genet 2004; 13: 3069-3077.
    • (2004) Hum Mol Genet , vol.13 , pp. 3069-3077
    • Lantinga-Van Leeuwen, I.S.1    Dauwerse, J.G.2    Baelde, H.J.3
  • 27
    • 30344471203 scopus 로고    scopus 로고
    • Defining a link with autosomaldominant polycystic kidney disease in mice with congenitally low expression of Pkd1
    • Jiang ST, Chiou YY, Wang E et al. Defining a link with autosomaldominant polycystic kidney disease in mice with congenitally low expression of Pkd1. Am J Pathol 2006; 168: 205-220.
    • (2006) Am J Pathol , vol.168 , pp. 205-220
    • Jiang, S.T.1    Chiou, Y.Y.2    Wang, E.3
  • 28
    • 16844375093 scopus 로고    scopus 로고
    • Pkd1 regulates immortalized proliferation of renal tubular epithelial cells through p53 induction and JNK activation
    • Nishio S, Hatano M, Nagata M et al. Pkd1 regulates immortalized proliferation of renal tubular epithelial cells through p53 induction and JNK activation. J Clin Invest 2005; 115: 910-918.
    • (2005) J Clin Invest , vol.115 , pp. 910-918
    • Nishio, S.1    Hatano, M.2    Nagata, M.3
  • 29
    • 0034120144 scopus 로고    scopus 로고
    • Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations
    • Watnick T, He N, Wang K et al. Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations. Nat Genet 2000; 25: 143-144.
    • (2000) Nat Genet , vol.25 , pp. 143-144
    • Watnick, T.1    He, N.2    Wang, K.3
  • 30
    • 0034639655 scopus 로고    scopus 로고
    • Genetic evidence for a transheterozygous model for cystogenesis in autosomal dominant polycystic kidney disease
    • Koptides M, Mean R, Demetriou K et al. Genetic evidence for a transheterozygous model for cystogenesis in autosomal dominant polycystic kidney disease. Hum Mol Genet 2000; 9: 447-452.
    • (2000) Hum Mol Genet , vol.9 , pp. 447-452
    • Koptides, M.1    Mean, R.2    Demetriou, K.3
  • 31
    • 0037306642 scopus 로고    scopus 로고
    • Molecular cytogenetic aberrations in autosomal dominant polycystic kidney disease tissue
    • Gogusev J, Murakami I, Doussau M et al. Molecular cytogenetic aberrations in autosomal dominant polycystic kidney disease tissue. J Am Soc Nephrol 2003; 14: 359-366.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 359-366
    • Gogusev, J.1    Murakami, I.2    Doussau, M.3
  • 32
    • 63949086532 scopus 로고    scopus 로고
    • Incompletely penetrant PKD1 alleles suggest a role for gene dosage in cyst initiation in polycystic kidney disease
    • Rossetti S, Kubly VJ, Consugar MB et al. Incompletely penetrant PKD1 alleles suggest a role for gene dosage in cyst initiation in polycystic kidney disease. Kidney Int 2009; 75: 848-855.
    • (2009) Kidney Int , vol.75 , pp. 848-855
    • Rossetti, S.1    Kubly, V.J.2    Consugar, M.B.3
  • 33
    • 77954598398 scopus 로고    scopus 로고
    • Incompletely penetrant PKD1 alleles mimic the renal manifestations of ARPKD
    • Vujic M, Heyer CM, Ars E et al. Incompletely penetrant PKD1 alleles mimic the renal manifestations of ARPKD. J Am Soc Nephrol 2010; 21: 1097-1102.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 1097-1102
    • Vujic, M.1    Heyer, C.M.2    Ars, E.3
  • 34
    • 80555136788 scopus 로고    scopus 로고
    • Mutations in multiple PKD genes may explain early and severe polycystic kidney disease
    • Bergmann C, von Bothmer J, Ortiz Bruchle N et al. Mutations in multiple PKD genes may explain early and severe polycystic kidney disease. J Am Soc Nephrol 2011; 22: 2047-2056.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 2047-2056
    • Bergmann, C.1    Von Bothmer, J.2    Ortiz Bruchle, N.3
  • 35
    • 84856019824 scopus 로고    scopus 로고
    • Neonatal onset autosomal dominant polycystic kidney disease (ADPKD) in a patient homozygous for a PKD2 missense mutation due to uniparental disomy
    • Losekoot M, Ruivenkamp CA, Tholens AP et al. Neonatal onset autosomal dominant polycystic kidney disease (ADPKD) in a patient homozygous for a PKD2 missense mutation due to uniparental disomy. J Med Genet 2012; 49: 37-40.
    • (2012) J Med Genet , vol.49 , pp. 37-40
    • Losekoot, M.1    Ruivenkamp, C.A.2    Tholens, A.P.3
  • 36
    • 84868613964 scopus 로고    scopus 로고
    • Functional polycystin-1 dosage governs autosomal dominant polycystic kidney disease severity
    • Hopp K, Ward CJ, Hommerding CJ et al. Functional polycystin-1 dosage governs autosomal dominant polycystic kidney disease severity. J Clin Invest 2012; 122: 4257-4273.
    • (2012) J Clin Invest , vol.122 , pp. 4257-4273
    • Hopp, K.1    Ward, C.J.2    Hommerding, C.J.3
  • 37
    • 77249114260 scopus 로고    scopus 로고
    • Variability in gene expression underlies incomplete penetrance
    • Raj A, Rifkin SA, Andersen E et al. Variability in gene expression underlies incomplete penetrance. Nature 2010; 463: 913-918.
    • (2010) Nature , vol.463 , pp. 913-918
    • Raj, A.1    Rifkin, S.A.2    Andersen, E.3
  • 38
    • 0032822326 scopus 로고    scopus 로고
    • Polycystin-1 expression in PKD1, early-onset PKD1, and TSC2/PKD1 cystic tissue
    • Ong AC, Harris PC, Davies DR et al. Polycystin-1 expression in PKD1, early-onset PKD1, and TSC2/PKD1 cystic tissue. Kidney Int 1999; 56: 1324-1333.
    • (1999) Kidney Int , vol.56 , pp. 1324-1333
    • Ong, A.C.1    Harris, P.C.2    Davies, D.R.3
  • 39
    • 72049098241 scopus 로고    scopus 로고
    • Pkd1 haploinsufficiency increases renal damage and induces microcyst formation following ischemia/ reperfusion
    • Bastos AP, Piontek K, Silva AM et al. Pkd1 haploinsufficiency increases renal damage and induces microcyst formation following ischemia/ reperfusion. J Am Soc Nephrol 2009; 20: 2389-2402.
    • (2009) J Am Soc Nephrol , vol.20 , pp. 2389-2402
    • Bastos, A.P.1    Piontek, K.2    Silva, A.M.3
  • 40
    • 67649884993 scopus 로고    scopus 로고
    • Toxic tubular injury in kidneys from Pkd1-deletion mice accelerates cystogenesis accompanied by dysregulated planar cell polarity and canonical Wnt signaling pathways
    • Happe H, Leonhard WN, van der Wal A et al. Toxic tubular injury in kidneys from Pkd1-deletion mice accelerates cystogenesis accompanied by dysregulated planar cell polarity and canonical Wnt signaling pathways. Hum Mol Genet 2009; 18: 2532-2542.
    • (2009) Hum Mol Genet , vol.18 , pp. 2532-2542
    • Happe, H.1    Leonhard, W.N.2    Van Der Wal, A.3
  • 41
    • 79959725455 scopus 로고    scopus 로고
    • A genetic interaction network of five genes for human polycystic kidney and liver diseases defines polycystin-1 as the central determinant of cyst formation
    • Fedeles SV, Tian X, Gallagher AR et al. A genetic interaction network of five genes for human polycystic kidney and liver diseases defines polycystin-1 as the central determinant of cyst formation. Nat Genet 2011; 43: 639-647.
    • (2011) Nat Genet , vol.43 , pp. 639-647
    • Fedeles, S.V.1    Tian, X.2    Gallagher, A.R.3
  • 42
    • 61349143028 scopus 로고    scopus 로고
    • Inactivation of Pkd1 in principal cells causes a more severe cystic kidney disease than in intercalated cells
    • Raphael KL, Strait KA, Stricklett PK et al. Inactivation of Pkd1 in principal cells causes a more severe cystic kidney disease than in intercalated cells. Kidney Int 2009; 75: 626-633.
    • (2009) Kidney Int , vol.75 , pp. 626-633
    • Raphael, K.L.1    Strait, K.A.2    Stricklett, P.K.3
  • 43
    • 84930455461 scopus 로고    scopus 로고
    • Scattered deletion of PKD1 in kidneys causes a cystic snowball effect and recapitulates polycystic kidney disease
    • Leonhard WN, Zandbergen M, Veraar K et al. Scattered deletion of PKD1 in kidneys causes a cystic snowball effect and recapitulates polycystic kidney disease. J Am Soc Nephrol 2014; 26: 1322-1333.
    • (2014) J Am Soc Nephrol , vol.26 , pp. 1322-1333
    • Leonhard, W.N.1    Zandbergen, M.2    Veraar, K.3
  • 44
    • 84908574596 scopus 로고    scopus 로고
    • The HNF1B score is a simple tool to select patients for HNF1B gene analysis
    • Faguer S, Chassaing N, Bandin F et al. The HNF1B score is a simple tool to select patients for HNF1B gene analysis. Kidney Int 2014; 86: 1007-1015.
    • (2014) Kidney Int , vol.86 , pp. 1007-1015
    • Faguer, S.1    Chassaing, N.2    Bandin, F.3
  • 45
    • 2342508500 scopus 로고    scopus 로고
    • A transcriptional network in polycystic kidney disease
    • Gresh L, Fischer E, Reimann A et al. A transcriptional network in polycystic kidney disease. EMBO J 2004; 23: 1657-1668.
    • (2004) EMBO J , vol.23 , pp. 1657-1668
    • Gresh, L.1    Fischer, E.2    Reimann, A.3
  • 46
    • 84879526558 scopus 로고    scopus 로고
    • MiR-17 ~ 92 miRNA cluster promotes kidney cyst growth in polycystic kidney disease
    • USA
    • Patel V, Williams D, Hajarnis S et al. miR-17 ~ 92 miRNA cluster promotes kidney cyst growth in polycystic kidney disease. Proc Natl Acad Sci USA 2013; 110: 10765-10770.
    • (2013) Proc Natl Acad Sci , vol.110 , pp. 10765-10770
    • Patel, V.1    Williams, D.2    Hajarnis, S.3
  • 47
    • 77958016655 scopus 로고    scopus 로고
    • Progressive renal distortion by multiple cysts in transgenic mice expressing artificial microRNAs against Pkd1
    • Wang E, Hsieh-Li HM, Chiou YY et al. Progressive renal distortion by multiple cysts in transgenic mice expressing artificial microRNAs against Pkd1. J Pathol 2010; 222: 238-248.
    • (2010) J Pathol , vol.222 , pp. 238-248
    • Wang, E.1    Hsieh-Li, H.M.2    Chiou, Y.Y.3
  • 48
    • 77950502479 scopus 로고    scopus 로고
    • The RNA-binding protein bicaudal C regulates polycystin 2 in the kidney by antagonizing miR-17 activity
    • Tran U, Zakin L, Schweickert A et al. The RNA-binding protein bicaudal C regulates polycystin 2 in the kidney by antagonizing miR-17 activity. Development 2010; 137: 1107-1116.
    • (2010) Development , vol.137 , pp. 1107-1116
    • Tran, U.1    Zakin, L.2    Schweickert, A.3
  • 49
    • 0034652247 scopus 로고    scopus 로고
    • Polycystin 1 is required for the structural integrity of blood vessels
    • USA
    • Kim K, Drummond I, Ibraghimov-Beskrovnaya O et al. Polycystin 1 is required for the structural integrity of blood vessels. Proc Natl Acad Sci USA 2000; 97: 1731-1736.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 1731-1736
    • Kim, K.1    Drummond, I.2    Ibraghimov-Beskrovnaya, O.3
  • 50
    • 84873471538 scopus 로고    scopus 로고
    • Diagnosis and management of polycystic liver disease
    • Gevers TJ, Drenth JP. Diagnosis and management of polycystic liver disease. Nat Rev Gastroenterol Hepatol 2013; 10: 101-108.
    • (2013) Nat Rev Gastroenterol Hepatol , vol.10 , pp. 101-108
    • Gevers, T.J.1    Drenth, J.P.2
  • 51
    • 0037830054 scopus 로고    scopus 로고
    • Association of mutation position in polycystic kidney disease 1 (PKD1) gene and development of a vascular phenotype
    • Rossetti S, Chauveau D, Kubly V et al. Association of mutation position in polycystic kidney disease 1 (PKD1) gene and development of a vascular phenotype. Lancet 2003; 361: 2196-2201.
    • (2003) Lancet , vol.361 , pp. 2196-2201
    • Rossetti, S.1    Chauveau, D.2    Kubly, V.3
  • 52
    • 36249019263 scopus 로고    scopus 로고
    • Risk of intracranial aneurysm bleeding in autosomal-dominant polycystic kidney disease
    • Ring T, Spiegelhalter D. Risk of intracranial aneurysm bleeding in autosomal-dominant polycystic kidney disease. Kidney Int 2007; 72: 1400-1402.
    • (2007) Kidney Int , vol.72 , pp. 1400-1402
    • Ring, T.1    Spiegelhalter, D.2
  • 53
    • 70349434788 scopus 로고    scopus 로고
    • Screening for intracranial aneurysms in ADPKD
    • Ong AC. Screening for intracranial aneurysms in ADPKD. BMJ 2009; 339: b3763.
    • (2009) BMJ , vol.339 , pp. b3763
    • Ong, A.C.1
  • 54
    • 84910115880 scopus 로고    scopus 로고
    • Sudden death due to subarachnoid haemorrhage in an infant with autosomal dominant polycystic kidney disease
    • Thong KM, Ong AC. Sudden death due to subarachnoid haemorrhage in an infant with autosomal dominant polycystic kidney disease. Nephrol Dial Transplant 2014; 29: iv121-iv123.
    • (2014) Nephrol Dial Transplant , vol.29 , pp. iv121-iv123
    • Thong, K.M.1    Ong, A.C.2
  • 55
    • 77952491724 scopus 로고    scopus 로고
    • Pkd1 transgenic mice: Adult model of polycystic kidney disease with extrarenal and renal phenotypes
    • Kurbegovic A, Cote O, Couillard M et al. Pkd1 transgenic mice: Adult model of polycystic kidney disease with extrarenal and renal phenotypes. Hum Mol Genet 2010; 19: 1174-1189.
    • (2010) Hum Mol Genet , vol.19 , pp. 1174-1189
    • Kurbegovic, A.1    Cote, O.2    Couillard, M.3
  • 56
    • 0043133391 scopus 로고    scopus 로고
    • Pkd2 haploinsufficiency alters intracellular calcium regulation in vascular smooth muscle cells
    • Qian Q, Hunter LW, Li M et al. Pkd2 haploinsufficiency alters intracellular calcium regulation in vascular smooth muscle cells. Hum Mol Genet 2003; 12: 1875-1880.
    • (2003) Hum Mol Genet , vol.12 , pp. 1875-1880
    • Qian, Q.1    Hunter, L.W.2    Li, M.3
  • 57
    • 35148840431 scopus 로고    scopus 로고
    • Pathogenic sequence for dissecting aneurysm formation in a hypomorphic polycystic kidney disease 1 mouse model
    • Hassane S, Claij N, Lantinga-van Leeuwen IS et al. Pathogenic sequence for dissecting aneurysm formation in a hypomorphic polycystic kidney disease 1 mouse model. Arterioscler Thromb Vasc Biol 2007; 27: 2177-2183.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2177-2183
    • Hassane, S.1    Claij, N.2    Lantinga-Van Leeuwen, I.S.3
  • 58
    • 78650770897 scopus 로고    scopus 로고
    • Pkd1-inactivation in vascular smooth muscle cells and adaptation to hypertension
    • Hassane S, Claij N, Jodar M et al. Pkd1-inactivation in vascular smooth muscle cells and adaptation to hypertension. Lab Invest 2011; 91: 24-32.
    • (2011) Lab Invest , vol.91 , pp. 24-32
    • Hassane, S.1    Claij, N.2    Jodar, M.3
  • 59
    • 84871914247 scopus 로고    scopus 로고
    • Pkd2 mesenteric vessels exhibit a primary defect in endothelium-dependent vasodilatation restored by rosiglitazone
    • Brookes ZL, Ruff L, Upadhyay VS et al. Pkd2 mesenteric vessels exhibit a primary defect in endothelium-dependent vasodilatation restored by rosiglitazone. Am J Physiol Heart Circ Physiol 2013; 304: H33-H41.
    • (2013) Am J Physiol Heart Circ Physiol , vol.304 , pp. H33-H41
    • Brookes, Z.L.1    Ruff, L.2    Upadhyay, V.S.3
  • 60
    • 84899985698 scopus 로고    scopus 로고
    • Pkd1 regulates lymphatic vascular morphogenesis during development
    • Coxam B, Sabine A, Bower NI et al. Pkd1 regulates lymphatic vascular morphogenesis during development. Cell Rep 2014; 7: 623-633.
    • (2014) Cell Rep , vol.7 , pp. 623-633
    • Coxam, B.1    Sabine, A.2    Bower, N.I.3
  • 61
    • 84899956827 scopus 로고    scopus 로고
    • Polycystin signaling is required for directed endothelial cell migration and lymphatic development
    • Outeda P, Huso DL, Fisher SA et al. Polycystin signaling is required for directed endothelial cell migration and lymphatic development. Cell Rep 2014; 7: 634-644.
    • (2014) Cell Rep , vol.7 , pp. 634-644
    • Outeda, P.1    Huso, D.L.2    Fisher, S.A.3
  • 63
    • 0028051871 scopus 로고
    • Deletion of the TSC2 and PKD1 genes associated with severe infantile polycystic kidney disease-a contiguous gene syndrome
    • Brook-Carter PT, Peral B, Ward CJ et al. Deletion of the TSC2 and PKD1 genes associated with severe infantile polycystic kidney disease-a contiguous gene syndrome. Nat Genet 1994; 8: 328-332.
    • (1994) Nat Genet , vol.8 , pp. 328-332
    • Brook-Carter, P.T.1    Peral, B.2    Ward, C.J.3
  • 64
    • 16944367389 scopus 로고    scopus 로고
    • Renal cystic disease in tuberous sclerosis: Role of the polycystic kidney disease 1 gene
    • Sampson JR, Maheshwar MM, Aspinwall R et al. Renal cystic disease in tuberous sclerosis: role of the polycystic kidney disease 1 gene. Am J Hum Genet 1997; 61: 843-851.
    • (1997) Am J Hum Genet , vol.61 , pp. 843-851
    • Sampson, J.R.1    Maheshwar, M.M.2    Aspinwall, R.3
  • 65
    • 57649243069 scopus 로고    scopus 로고
    • The tuberous sclerosis proteins regulate formation of the primary cilium via a rapamycin-insensitive and polycystin 1-independent pathway
    • Hartman TR, Liu D, Zilfou JT et al. The tuberous sclerosis proteins regulate formation of the primary cilium via a rapamycin-insensitive and polycystin 1-independent pathway. Hum Mol Genet 2008; 18: 151-163.
    • (2008) Hum Mol Genet , vol.18 , pp. 151-163
    • Hartman, T.R.1    Liu, D.2    Zilfou, J.T.3
  • 66
    • 66149098514 scopus 로고    scopus 로고
    • Defects in cell polarity underlie TSC and ADPKD-associated cystogenesis
    • Bonnet CS, Aldred M, von Ruhland C et al. Defects in cell polarity underlie TSC and ADPKD-associated cystogenesis. Hum Mol Genet 2009; 18: 2166-2176.
    • (2009) Hum Mol Genet , vol.18 , pp. 2166-2176
    • Bonnet, C.S.1    Aldred, M.2    Von Ruhland, C.3
  • 67
    • 0035019467 scopus 로고    scopus 로고
    • Tuberindependent membrane localization of polycystin-1: A functional link between polycystic kidney disease and the TSC2 tumor suppressor gene
    • Kleymenova E, Ibraghimov-Beskrovnaya O, Kugoh H et al. Tuberindependent membrane localization of polycystin-1: A functional link between polycystic kidney disease and the TSC2 tumor suppressor gene. Mol Cell 2001; 7: 823-832.
    • (2001) Mol Cell , vol.7 , pp. 823-832
    • Kleymenova, E.1    Ibraghimov-Beskrovnaya, O.2    Kugoh, H.3
  • 68
    • 40449103145 scopus 로고    scopus 로고
    • Fibrocystin/polyductin modulates renal tubular formation by regulating polycystin-2 expression and function
    • Kim I, Fu Y, Hui K et al. Fibrocystin/polyductin modulates renal tubular formation by regulating polycystin-2 expression and function. J Am Soc Nephrol 2008; 19: 455-468.
    • (2008) J Am Soc Nephrol , vol.19 , pp. 455-468
    • Kim, I.1    Fu, Y.2    Hui, K.3
  • 69
    • 0035125616 scopus 로고    scopus 로고
    • Bilineal disease and transheterozygotes in autosomal dominant polycystic kidney disease
    • Pei Y, Paterson AD, Wang KR et al. Bilineal disease and transheterozygotes in autosomal dominant polycystic kidney disease. Am J Hum Genet 2001; 68: 355-363.
    • (2001) Am J Hum Genet , vol.68 , pp. 355-363
    • Pei, Y.1    Paterson, A.D.2    Wang, K.R.3
  • 70
    • 84863081434 scopus 로고    scopus 로고
    • A missense mutation in PKD1 attenuates the severity of renal disease
    • Pei Y, Lan Z, Wang K et al. A missense mutation in PKD1 attenuates the severity of renal disease. Kidney Int 2012; 81: 412-417.
    • (2012) Kidney Int , vol.81 , pp. 412-417
    • Pei, Y.1    Lan, Z.2    Wang, K.3
  • 71
    • 84922157174 scopus 로고    scopus 로고
    • Polycystin-1 maturation requires polycystin-2 in a dose-dependent manner
    • Gainullin VG, Hopp K, Ward CJ et al. Polycystin-1 maturation requires polycystin-2 in a dose-dependent manner. J Clin Invest 2015; 125: 607-620.
    • (2015) J Clin Invest , vol.125 , pp. 607-620
    • Gainullin, V.G.1    Hopp, K.2    Ward, C.J.3
  • 72
    • 84901411100 scopus 로고    scopus 로고
    • N-glycosylation determines the abundance of the transient receptor potential channel TRPP2
    • Hofherr A, Wagner C, Fedeles S et al. N-glycosylation determines the abundance of the transient receptor potential channel TRPP2. J Biol Chem 2014; 289: 14854-14867.
    • (2014) J Biol Chem , vol.289 , pp. 14854-14867
    • Hofherr, A.1    Wagner, C.2    Fedeles, S.3
  • 73
    • 0037371324 scopus 로고    scopus 로고
    • Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease
    • Li A, Davila S, Furu L et al. Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease. Am J Hum Genet 2003; 72: 691-703.
    • (2003) Am J Hum Genet , vol.72 , pp. 691-703
    • Li, A.1    Davila, S.2    Furu, L.3
  • 74
    • 84858792464 scopus 로고    scopus 로고
    • A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis
    • Arac D, Boucard AA, Bolliger MF et al. A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis. EMBO J 2012; 31: 1364-1378.
    • (2012) EMBO J , vol.31 , pp. 1364-1378
    • Arac, D.1    Boucard, A.A.2    Bolliger, M.F.3
  • 75
    • 36749047485 scopus 로고    scopus 로고
    • Essential role of cleavage of Polycystin-1 at G protein-coupled receptor proteolytic site for kidney tubular structure
    • USA
    • Yu S, Hackmann K, Gao J et al. Essential role of cleavage of Polycystin-1 at G protein-coupled receptor proteolytic site for kidney tubular structure. Proc Natl Acad Sci USA 2007; 104: 18688-18693.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 18688-18693
    • Yu, S.1    Hackmann, K.2    Gao, J.3
  • 76
    • 78650482131 scopus 로고    scopus 로고
    • Polycystin-1 surface localization is stimulated by polycystin-2 and cleavage at the G protein-coupled receptor proteolytic site
    • Chapin HC, Rajendran V, Caplan MJ. Polycystin-1 surface localization is stimulated by polycystin-2 and cleavage at the G protein-coupled receptor proteolytic site. Mol Biol Cell 2010; 21: 4338-4348.
    • (2010) Mol Biol Cell , vol.21 , pp. 4338-4348
    • Chapin, H.C.1    Rajendran, V.2    Caplan, M.J.3
  • 77
    • 84923279651 scopus 로고    scopus 로고
    • Ciliary membrane proteins traffic through the Golgi via a Rabep1/GGA1/Arl3-dependent mechanism
    • Kim H, Xu H, Yao Q et al. Ciliary membrane proteins traffic through the Golgi via a Rabep1/GGA1/Arl3-dependent mechanism. Nat Commun 2014; 5: 5482.
    • (2014) Nat Commun , vol.5 , pp. 5482
    • Kim, H.1    Xu, H.2    Yao, Q.3
  • 78
    • 84915779680 scopus 로고    scopus 로고
    • Novel functional complexity of polycystin-1 by GPS cleavage in vivo: Role in polycystic kidney disease
    • Kurbegovic A, Kim H, Xu H et al. Novel functional complexity of polycystin-1 by GPS cleavage in vivo: role in polycystic kidney disease. Mol Cell Biol 2014; 34: 3341-3353.
    • (2014) Mol Cell Biol , vol.34 , pp. 3341-3353
    • Kurbegovic, A.1    Kim, H.2    Xu, H.3
  • 79
    • 0033555277 scopus 로고    scopus 로고
    • The structure of a PKD domain from polycystin-1: Implications for polycystic kidney disease
    • Bycroft M, Bateman A, Clarke J et al. The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease. EMBO J 1999; 18: 297-305.
    • (1999) EMBO J , vol.18 , pp. 297-305
    • Bycroft, M.1    Bateman, A.2    Clarke, J.3
  • 80
    • 0036774262 scopus 로고    scopus 로고
    • Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins
    • Jing H, Takagi J, Liu JH et al. Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins. Structure 2002; 10: 1453-1464.
    • (2002) Structure , vol.10 , pp. 1453-1464
    • Jing, H.1    Takagi, J.2    Liu, J.H.3
  • 81
    • 28844435249 scopus 로고    scopus 로고
    • The nanomechanics of polycystin-1 extracellular region
    • Qian F, Wei W, Germino G et al. The nanomechanics of polycystin-1 extracellular region. J Biol Chem 2005; 280: 40723-40730.
    • (2005) J Biol Chem , vol.280 , pp. 40723-40730
    • Qian, F.1    Wei, W.2    Germino, G.3
  • 82
    • 19444372522 scopus 로고    scopus 로고
    • The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction
    • Forman JR, Qamar S, Paci E et al. The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction. J Mol Biol 2005; 349: 861-871.
    • (2005) J Mol Biol , vol.349 , pp. 861-871
    • Forman, J.R.1    Qamar, S.2    Paci, E.3
  • 83
    • 71049121056 scopus 로고    scopus 로고
    • Non-native interactions are critical for mechanical strength in PKD domains
    • Forman JR, Yew ZT, Qamar S et al. Non-native interactions are critical for mechanical strength in PKD domains. Structure 2009; 17: 1582-1590.
    • (2009) Structure , vol.17 , pp. 1582-1590
    • Forman, J.R.1    Yew, Z.T.2    Qamar, S.3
  • 84
    • 67650544382 scopus 로고    scopus 로고
    • Homophilic and heterophilic polycystin 1 interactions regulate E-cadherin recruitment and junction assembly in MDCK cells
    • Streets AJ, Wagner BE, Harris PC et al. Homophilic and heterophilic polycystin 1 interactions regulate E-cadherin recruitment and junction assembly in MDCK cells. J Cell Sci 2009; 122: 1410-1417.
    • (2009) J Cell Sci , vol.122 , pp. 1410-1417
    • Streets, A.J.1    Wagner, B.E.2    Harris, P.C.3
  • 85
    • 0037868262 scopus 로고    scopus 로고
    • Functional analysis of PKD1 transgenic lines reveals a direct role for polycystin-1 in mediating cell-cell adhesion
    • Streets AJ, Newby LJ, O'Hare MJ et al. Functional analysis of PKD1 transgenic lines reveals a direct role for polycystin-1 in mediating cell-cell adhesion. J Am Soc Nephrol 2003; 14: 1804-1815.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 1804-1815
    • Streets, A.J.1    Newby, L.J.2    O'Hare, M.J.3
  • 86
    • 0034214837 scopus 로고    scopus 로고
    • Strong homophilic interactions of the Ig-like domains of polycystin-1, the protein product of an autosomal dominant polycystic kidney disease gene, PKD1
    • Ibraghimov-Beskrovnaya O, Bukanov NO, Donohue LC 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 2000; 9: 1641-1649.
    • (2000) Hum Mol Genet , vol.9 , pp. 1641-1649
    • Ibraghimov-Beskrovnaya, O.1    Bukanov, N.O.2    Donohue, L.C.3
  • 87
    • 0033607040 scopus 로고    scopus 로고
    • The PLAT domain: A new piece in the PKD1 puzzle
    • Bateman A, Sandford R. The PLAT domain: A new piece in the PKD1 puzzle. Curr Biol 1999; 9: R588-R590.
    • (1999) Curr Biol , vol.9 , pp. R588-R590
    • Bateman, A.1    Sandford, R.2
  • 88
    • 0033607014 scopus 로고    scopus 로고
    • A latrophilin/CL-1-like GPS domain in polycystin-1
    • Ponting CP, Hofmann K, Bork P. A latrophilin/CL-1-like GPS domain in polycystin-1. Curr Biol 1999; 9: R585-R588.
    • (1999) Curr Biol , vol.9 , pp. R585-R588
    • Ponting, C.P.1    Hofmann, K.2    Bork, P.3
  • 89
    • 58149181482 scopus 로고    scopus 로고
    • Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain
    • Recacha R, Boulet A, Jollivet F et al. Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain. Structure 2009; 17: 21-30.
    • (2009) Structure , vol.17 , pp. 21-30
    • Recacha, R.1    Boulet, A.2    Jollivet, F.3
  • 90
    • 84862661138 scopus 로고    scopus 로고
    • Structure of a calcium-dependent 11Rlipoxygenase suggests a mechanism for Ca2+ regulation
    • Eek P, Jarving R, Jarving I et al. Structure of a calcium-dependent 11Rlipoxygenase suggests a mechanism for Ca2+ regulation. J Biol Chem 2012; 287: 22377-22386.
    • (2012) J Biol Chem , vol.287 , pp. 22377-22386
    • Eek, P.1    Jarving, R.2    Jarving, I.3
  • 91
    • 12844254280 scopus 로고    scopus 로고
    • ATP-2 interacts with the PLAT domain of LOV-1 and is involved in Caenorhabditis elegans polycystin signaling
    • Hu J, Barr MM. ATP-2 interacts with the PLAT domain of LOV-1 and is involved in Caenorhabditis elegans polycystin signaling. Mol Biol Cell 2005; 16: 458-469.
    • (2005) Mol Biol Cell , vol.16 , pp. 458-469
    • Hu, J.1    Barr, M.M.2
  • 92
    • 84861880031 scopus 로고    scopus 로고
    • Protein phosphatase-1alpha interacts with and dephosphorylates polycystin-1
    • Parnell SC, Puri S, Wallace DP et al. Protein phosphatase-1alpha interacts with and dephosphorylates polycystin-1. PLoS One 2012; 7: e36798.
    • (2012) PLoS One , vol.7 , pp. e36798
    • Parnell, S.C.1    Puri, S.2    Wallace, D.P.3
  • 93
    • 84877056647 scopus 로고    scopus 로고
    • Hyperphosphorylation of polycystin-2 at a critical residue in disease reveals an essential role for polycystin-1-regulated dephosphorylation
    • Streets AJ, Wessely O, Peters DJ et al. Hyperphosphorylation of polycystin-2 at a critical residue in disease reveals an essential role for polycystin-1-regulated dephosphorylation. Hum Mol Genet 2013; 22: 1924-1939.
    • (2013) Hum Mol Genet , vol.22 , pp. 1924-1939
    • Streets, A.J.1    Wessely, O.2    Peters, D.J.3
  • 94
    • 33645769011 scopus 로고    scopus 로고
    • The mTOR pathway is regulated by polycystin-1, and its inhibition reverses renal cystogenesis in polycystic kidney disease
    • USA
    • Shillingford JM, Murcia NS, Larson CH et al. The mTOR pathway is regulated by polycystin-1, and its inhibition reverses renal cystogenesis in polycystic kidney disease. Proc Natl Acad Sci USA 2006; 103: 5466-5471.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 5466-5471
    • Shillingford, J.M.1    Murcia, N.S.2    Larson, C.H.3
  • 95
    • 53349173236 scopus 로고    scopus 로고
    • Polycystin-1 C-terminal tail associates with beta-catenin and inhibits canonical Wnt signaling
    • Lal M, Song X, Pluznick JL et al. Polycystin-1 C-terminal tail associates with beta-catenin and inhibits canonical Wnt signaling. Hum Mol Genet 2008; 17: 3105-3117.
    • (2008) Hum Mol Genet , vol.17 , pp. 3105-3117
    • Lal, M.1    Song, X.2    Pluznick, J.L.3
  • 96
    • 0037133954 scopus 로고    scopus 로고
    • PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2
    • Bhunia AK, Piontek K, Boletta A et al. PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2. Cell 2002; 109: 157-168.
    • (2002) Cell , vol.109 , pp. 157-168
    • Bhunia, A.K.1    Piontek, K.2    Boletta, A.3
  • 97
    • 0035970112 scopus 로고    scopus 로고
    • Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2 +-permeable nonselective cation channel
    • USA
    • Gonzalez-Perret S, Kim K, Ibarra C et al. Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2 +-permeable nonselective cation channel. Proc Natl Acad Sci USA 2001; 98: 1182-1187.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 1182-1187
    • Gonzalez-Perret, S.1    Kim, K.2    Ibarra, C.3
  • 98
    • 24344482068 scopus 로고    scopus 로고
    • PKD2 functions as an epidermal growth factor-activated plasma membrane channel
    • Ma R, Li WP, Rundle D et al. PKD2 functions as an epidermal growth factor-activated plasma membrane channel. Mol Cell Biol 2005; 25: 8285-8298.
    • (2005) Mol Cell Biol , vol.25 , pp. 8285-8298
    • Ma, R.1    Li, W.P.2    Rundle, D.3
  • 99
    • 18244402941 scopus 로고    scopus 로고
    • A unified nomenclature for the superfamily of TRP cation channels
    • Montell C, Birnbaumer L, Flockerzi V et al. A unified nomenclature for the superfamily of TRP cation channels. Mol Cell 2002; 9: 229-231.
    • (2002) Mol Cell , vol.9 , pp. 229-231
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 100
    • 84891818486 scopus 로고    scopus 로고
    • Strategies targeting cAMP signaling in the treatment of polycystic kidney disease
    • Torres VE, Harris PC. Strategies targeting cAMP signaling in the treatment of polycystic kidney disease. J Am Soc Nephrol 2014; 25: 18-32.
    • (2014) J Am Soc Nephrol , vol.25 , pp. 18-32
    • Torres, V.E.1    Harris, P.C.2
  • 101
    • 67650860463 scopus 로고    scopus 로고
    • Structural and molecular basis of the assembly of the TRPP2/PKD1 complex
    • USA
    • Yu Y, Ulbrich MH, Li MH et al. Structural and molecular basis of the assembly of the TRPP2/PKD1 complex. Proc Natl Acad Sci USA 2009; 106: 11558-11563.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 11558-11563
    • Yu, Y.1    Ulbrich, M.H.2    Li, M.H.3
  • 102
    • 63149089847 scopus 로고    scopus 로고
    • The multimeric structure of polycystin-2 (TRPP2): Structural-functional correlates of homo-and hetero-multimers with TRPC1
    • Zhang P, Luo Y, Chasan B et al. The multimeric structure of polycystin-2 (TRPP2): structural-functional correlates of homo-and hetero-multimers with TRPC1. Hum Mol Genet 2009; 18: 1238-1251.
    • (2009) Hum Mol Genet , vol.18 , pp. 1238-1251
    • Zhang, P.1    Luo, Y.2    Chasan, B.3
  • 103
    • 57649128301 scopus 로고    scopus 로고
    • Identification and functional characterization of an N-terminal oligomerization domain for polycystin
    • Feng S, Okenka GM, Bai CX et al. Identification and functional characterization of an N-terminal oligomerization domain for polycystin-J Biol Chem 2008; 283: 28471-28479.
    • (2008) J Biol Chem , vol.283 , pp. 28471-28479
    • Feng, S.1    Okenka, G.M.2    Bai, C.X.3
  • 104
    • 79956300184 scopus 로고    scopus 로고
    • A single amino acid residue constitutes the third dimerization domain essential for the assembly and function of the tetrameric polycystin-2 (TRPP2) channel
    • Feng S, Rodat-Despoix L, Delmas P et al. A single amino acid residue constitutes the third dimerization domain essential for the assembly and function of the tetrameric polycystin-2 (TRPP2) channel. J Biol Chem 2011; 286: 18994-19000.
    • (2011) J Biol Chem , vol.286 , pp. 18994-19000
    • Feng, S.1    Rodat-Despoix, L.2    Delmas, P.3
  • 105
    • 77952717195 scopus 로고    scopus 로고
    • Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity
    • USA
    • Petri ET, Celic A, Kennedy SD et al. Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity. Proc Natl Acad Sci USA 2010; 107: 9176-9181.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 9176-9181
    • Petri, E.T.1    Celic, A.2    Kennedy, S.D.3
  • 106
    • 69949188700 scopus 로고    scopus 로고
    • Ca2+-dependent conformational changes in a C-terminal cytosolic domain of polycystin-2
    • Schumann F, Hoffmeister H, Bader R et al. Ca2+-dependent conformational changes in a C-terminal cytosolic domain of polycystin-2. J Biol Chem 2009; 284: 24372-24383.
    • (2009) J Biol Chem , vol.284 , pp. 24372-24383
    • Schumann, F.1    Hoffmeister, H.2    Bader, R.3
  • 107
    • 84880373765 scopus 로고    scopus 로고
    • Calcium transport and local pool regulate polycystin-2 (TRPP2) function in human syncytiotrophoblast
    • Cantero Mdel R, Cantiello HF. Calcium transport and local pool regulate polycystin-2 (TRPP2) function in human syncytiotrophoblast. Biophys J 2013; 105: 365-375.
    • (2013) Biophys J , vol.105 , pp. 365-375
    • Cantero Mdel, R.1    Cantiello, H.F.2
  • 108
    • 33646764178 scopus 로고    scopus 로고
    • Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif
    • Geng L, Okuhara D, Yu Z et al. Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif. J Cell Sci 2006; 119: 1383-1395.
    • (2006) J Cell Sci , vol.119 , pp. 1383-1395
    • Geng, L.1    Okuhara, D.2    Yu, Z.3
  • 109
    • 79951903269 scopus 로고    scopus 로고
    • Polycystin-2 takes different routes to the somatic and ciliary plasma membrane
    • Hoffmeister H, Babinger K, Gurster S et al. Polycystin-2 takes different routes to the somatic and ciliary plasma membrane. J Cell Biol 2011; 192: 631-645.
    • (2011) J Cell Biol , vol.192 , pp. 631-645
    • Hoffmeister, H.1    Babinger, K.2    Gurster, S.3
  • 110
    • 84867336373 scopus 로고    scopus 로고
    • Cilia at the node of mouse embryos sense fluid flow for left-right determination via Pkd2
    • Yoshiba S, Shiratori H, Kuo IY et al. Cilia at the node of mouse embryos sense fluid flow for left-right determination via Pkd2. Science 2012; 338: 226-231.
    • (2012) Science , vol.338 , pp. 226-231
    • Yoshiba, S.1    Shiratori, H.2    Kuo, I.Y.3
  • 111
    • 80052827000 scopus 로고    scopus 로고
    • A conserved signal and GTPase complex are required for the ciliary transport of polycystin-1
    • Ward HH, Brown-Glaberman U, Wang J et al. A conserved signal and GTPase complex are required for the ciliary transport of polycystin-1. Mol Biol Cell 2011; 22: 3289-3305.
    • (2011) Mol Biol Cell , vol.22 , pp. 3289-3305
    • Ward, H.H.1    Brown-Glaberman, U.2    Wang, J.3
  • 112
    • 84915775893 scopus 로고    scopus 로고
    • Altered trafficking and stability of polycystins underlie polycystic kidney disease
    • Cai Y, Fedeles SV, Dong K et al. Altered trafficking and stability of polycystins underlie polycystic kidney disease. J Clin Invest 2014; 124: 5129-5144.
    • (2014) J Clin Invest , vol.124 , pp. 5129-5144
    • Cai, Y.1    Fedeles, S.V.2    Dong, K.3
  • 113
    • 33646155954 scopus 로고    scopus 로고
    • Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro
    • Streets AJ, Moon DJ, Kane ME et al. Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro. Hum Mol Genet 2006; 15: 1465-1473.
    • (2006) Hum Mol Genet , vol.15 , pp. 1465-1473
    • Streets, A.J.1    Moon, D.J.2    Kane, M.E.3
  • 114
    • 84873497162 scopus 로고    scopus 로고
    • Intracellular calcium release modulates polycystin-2 trafficking
    • Miyakawa A, Ibarra C, Malmersjo S et al. Intracellular calcium release modulates polycystin-2 trafficking. BMC Nephrol 2013; 14: 34.
    • (2013) BMC Nephrol , vol.14 , pp. 34
    • Miyakawa, A.1    Ibarra, C.2    Malmersjo, S.3
  • 115
    • 2442605494 scopus 로고    scopus 로고
    • Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812
    • Cai Y, Anyatonwu G, Okuhara D et al. Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812. J Biol Chem 2004; 279: 19987-19995.
    • (2004) J Biol Chem , vol.279 , pp. 19987-19995
    • Cai, Y.1    Anyatonwu, G.2    Okuhara, D.3
  • 116
    • 78649637949 scopus 로고    scopus 로고
    • Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity
    • Streets AJ, Needham AJ, Gill SK et al. Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity. Mol Biol Cell 2010; 21: 3853-3865.
    • (2010) Mol Biol Cell , vol.21 , pp. 3853-3865
    • Streets, A.J.1    Needham, A.J.2    Gill, S.K.3
  • 117
    • 20144383835 scopus 로고    scopus 로고
    • Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation
    • Kottgen M, Benzing T, Simmen T et al. Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. EMBO J 2005; 24: 705-716.
    • (2005) EMBO J , vol.24 , pp. 705-716
    • Kottgen, M.1    Benzing, T.2    Simmen, T.3
  • 118
    • 80052264443 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatases are novel components of a polycystin complex
    • Boucher CA, Ward HH, Case RL et al. Receptor protein tyrosine phosphatases are novel components of a polycystin complex. Biochim Biophys Acta 2011; 1812: 1225-1238.
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 1225-1238
    • Boucher, C.A.1    Ward, H.H.2    Case, R.L.3
  • 119
    • 40449102218 scopus 로고    scopus 로고
    • NEK8 mutations affect ciliary and centrosomal localization and may cause nephronophthisis
    • Otto EA, Trapp ML, Schultheiss UT et al. NEK8 mutations affect ciliary and centrosomal localization and may cause nephronophthisis. J Am Soc Nephrol 2008; 19: 587-592.
    • (2008) J Am Soc Nephrol , vol.19 , pp. 587-592
    • Otto, E.A.1    Trapp, M.L.2    Schultheiss, U.T.3
  • 120
    • 0036931712 scopus 로고    scopus 로고
    • A defect in a novel Nek-family kinase causes cystic kidney disease in the mouse and in zebrafish
    • Liu S, Lu W, Obara T et al. A defect in a novel Nek-family kinase causes cystic kidney disease in the mouse and in zebrafish. Development 2002; 129: 5839-5846.
    • (2002) Development , vol.129 , pp. 5839-5846
    • Liu, S.1    Lu, W.2    Obara, T.3
  • 121
    • 84864915551 scopus 로고    scopus 로고
    • A novel mutation causing nephronophthisis in the Lewis polycystic kidney rat localises to a conserved RCC1 domain in Nek8
    • McCooke JK, Appels R, Barrero RA et al. A novel mutation causing nephronophthisis in the Lewis polycystic kidney rat localises to a conserved RCC1 domain in Nek8. BMC Genomics 2012; 13: 393.
    • (2012) BMC Genomics , vol.13 , pp. 393
    • McCooke, J.K.1    Appels, R.2    Barrero, R.A.3
  • 122
    • 40449121293 scopus 로고    scopus 로고
    • Nek8 regulates the expression and localization of polycystin-1 and polycystin-2
    • Sohara E, Luo Y, Zhang J et al. Nek8 regulates the expression and localization of polycystin-1 and polycystin-2. J Am Soc Nephrol 2008; 19: 469-476.
    • (2008) J Am Soc Nephrol , vol.19 , pp. 469-476
    • Sohara, E.1    Luo, Y.2    Zhang, J.3
  • 123
    • 84881028445 scopus 로고    scopus 로고
    • ANKS6 is a central component of a nephronophthisis module linking NEK8 to INVS and NPHP3
    • Hoff S, Halbritter J, Epting D et al. ANKS6 is a central component of a nephronophthisis module linking NEK8 to INVS and NPHP3. Nat Genet 2013; 45: 951-956.
    • (2013) Nat Genet , vol.45 , pp. 951-956
    • Hoff, S.1    Halbritter, J.2    Epting, D.3
  • 124
    • 3543069403 scopus 로고    scopus 로고
    • Siah-1 interacts with the intracellular region of polycystin-1 and affects its stability via the ubiquitin-proteasome pathway
    • Kim H, Jeong W, Ahn K et al. Siah-1 interacts with the intracellular region of polycystin-1 and affects its stability via the ubiquitin-proteasome pathway. J Am Soc Nephrol 2004; 15: 2042-2049.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 2042-2049
    • Kim, H.1    Jeong, W.2    Ahn, K.3
  • 125
    • 34548719323 scopus 로고    scopus 로고
    • TAZ promotes PC2 degradation through a SCFbeta-Trcp E3 ligase complex
    • Tian Y, Kolb R, Hong JH et al. TAZ promotes PC2 degradation through a SCFbeta-Trcp E3 ligase complex. Mol Cell Biol 2007; 27: 6383-6395.
    • (2007) Mol Cell Biol , vol.27 , pp. 6383-6395
    • Tian, Y.1    Kolb, R.2    Hong, J.H.3
  • 126
    • 41149112349 scopus 로고    scopus 로고
    • Multiple renal cysts, urinary concentration defects, and pulmonary emphysematous changes in mice lacking TAZ
    • Makita R, Uchijima Y, Nishiyama K et al. Multiple renal cysts, urinary concentration defects, and pulmonary emphysematous changes in mice lacking TAZ. Am J Physiol Renal Physiol 2008; 294: F542-F553.
    • (2008) Am J Physiol Renal Physiol , vol.294 , pp. F542-F553
    • Makita, R.1    Uchijima, Y.2    Nishiyama, K.3
  • 127
    • 79955626244 scopus 로고    scopus 로고
    • Nek1 and TAZ interact to maintain normal levels of polycystin 2
    • Yim H, Sung CK, You J et al. Nek1 and TAZ interact to maintain normal levels of polycystin 2. J Am Soc Nephrol 2011; 22: 832-837.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 832-837
    • Yim, H.1    Sung, C.K.2    You, J.3
  • 128
    • 84904043132 scopus 로고    scopus 로고
    • YAP/TAZ incorporation in the betacatenin destruction complex orchestrates the Wnt response
    • Azzolin L, Panciera T, Soligo S et al. YAP/TAZ incorporation in the betacatenin destruction complex orchestrates the Wnt response. Cell 2014; 158: 157-170.
    • (2014) Cell , vol.158 , pp. 157-170
    • Azzolin, L.1    Panciera, T.2    Soligo, S.3
  • 129
    • 41849135419 scopus 로고    scopus 로고
    • Polycystin-2 is regulated by endoplasmic reticulum-associated degradation
    • Liang G, Li Q, Tang Y et al. Polycystin-2 is regulated by endoplasmic reticulum-associated degradation. Hum Mol Genet 2008; 17: 1109-1119.
    • (2008) Hum Mol Genet , vol.17 , pp. 1109-1119
    • Liang, G.1    Li, Q.2    Tang, Y.3
  • 130
    • 77249164094 scopus 로고    scopus 로고
    • PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERPmediated degradation
    • Gao H, Wang Y, Wegierski T et al. PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERPmediated degradation. Hum Mol Genet 2010; 19: 16-24.
    • (2010) Hum Mol Genet , vol.19 , pp. 16-24
    • Gao, H.1    Wang, Y.2    Wegierski, T.3
  • 131
    • 73549122173 scopus 로고    scopus 로고
    • Pkd2 dosage influences cellular repair responses following ischemia-reperfusion injury
    • Prasad S, McDaid JP, Tam FW et al. Pkd2 dosage influences cellular repair responses following ischemia-reperfusion injury. Am J Pathol 2009; 175: 1493-1503.
    • (2009) Am J Pathol , vol.175 , pp. 1493-1503
    • Prasad, S.1    McDaid, J.P.2    Tam, F.W.3
  • 132
    • 0036900629 scopus 로고    scopus 로고
    • Polycystin-2 expression is increased following experimental ischaemic renal injury
    • Zhao Y, Haylor JL, Ong AC. Polycystin-2 expression is increased following experimental ischaemic renal injury. Nephrol Dial Transplant 2002; 17: 2138-2144.
    • (2002) Nephrol Dial Transplant , vol.17 , pp. 2138-2144
    • Zhao, Y.1    Haylor, J.L.2    Ong, A.C.3
  • 133
    • 84855952173 scopus 로고    scopus 로고
    • The gamma-secretase cleavage product of polycystin-1 regulates TCF and CHOP-mediated transcriptional activation through a p300-dependent mechanism
    • Merrick D, Chapin H, Baggs JE et al. The gamma-secretase cleavage product of polycystin-1 regulates TCF and CHOP-mediated transcriptional activation through a p300-dependent mechanism. Dev Cell 2012; 22: 197-210.
    • (2012) Dev Cell , vol.22 , pp. 197-210
    • Merrick, D.1    Chapin, H.2    Baggs, J.E.3
  • 134
    • 29744470060 scopus 로고    scopus 로고
    • Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease
    • Low SH, Vasanth S, Larson CH et al. Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease. Dev Cell 2006; 10: 57-69.
    • (2006) Dev Cell , vol.10 , pp. 57-69
    • Low, S.H.1    Vasanth, S.2    Larson, C.H.3
  • 135
    • 77957882874 scopus 로고    scopus 로고
    • Identification of a polycystin-1 cleavage product, P100, that regulates store operated Ca entry through interactions with STIM1
    • Woodward OM, Li Y, Yu S et al. Identification of a polycystin-1 cleavage product, P100, that regulates store operated Ca entry through interactions with STIM1. PLoS One 2010; 5: e12305.
    • (2010) PLoS One , vol.5 , pp. e12305
    • Woodward, O.M.1    Li, Y.2    Yu, S.3
  • 136
    • 0037334326 scopus 로고    scopus 로고
    • Polycystic kidney disease-the ciliary connection
    • Ong AC, Wheatley DN. Polycystic kidney disease-the ciliary connection. Lancet 2003; 361: 774-776.
    • (2003) Lancet , vol.361 , pp. 774-776
    • Ong, A.C.1    Wheatley, D.N.2
  • 137
    • 84893407429 scopus 로고    scopus 로고
    • The roles of evolutionarily conserved functional modules in cilia-related trafficking
    • Sung CH, Leroux MR. The roles of evolutionarily conserved functional modules in cilia-related trafficking. Nat Cell Biol 2013; 15: 1387-1397.
    • (2013) Nat Cell Biol , vol.15 , pp. 1387-1397
    • Sung, C.H.1    Leroux, M.R.2
  • 139
    • 0035806961 scopus 로고    scopus 로고
    • The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway
    • Barr MM, DeModena J, Braun D et al. The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway. Curr Biol 2001; 11: 1341-1346.
    • (2001) Curr Biol , vol.11 , pp. 1341-1346
    • Barr, M.M.1    Demodena, J.2    Braun, D.3
  • 140
    • 0033598394 scopus 로고    scopus 로고
    • A polycystic kidney-disease gene homologue required for male mating behaviour in C elegans
    • Barr MM, Sternberg PW. A polycystic kidney-disease gene homologue required for male mating behaviour in C. elegans. Nature 1999; 401: 386-389.
    • (1999) Nature , vol.401 , pp. 386-389
    • Barr, M.M.1    Sternberg, P.W.2
  • 141
    • 0034735526 scopus 로고    scopus 로고
    • Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella
    • Pazour GJ, Dickert BL, Vucica Y et al. Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella. J Cell Biol 2000; 151: 709-718.
    • (2000) J Cell Biol , vol.151 , pp. 709-718
    • Pazour, G.J.1    Dickert, B.L.2    Vucica, Y.3
  • 142
    • 0034987372 scopus 로고    scopus 로고
    • The C elegans homolog of the murine cystic kidney disease gene Tg737 functions in a ciliogenic pathway and is disrupted in osm-5 mutant worms
    • Haycraft CJ, Swoboda P, Taulman PD et al. The C. elegans homolog of the murine cystic kidney disease gene Tg737 functions in a ciliogenic pathway and is disrupted in osm-5 mutant worms. Development 2001; 128: 1493-1505.
    • (2001) Development , vol.128 , pp. 1493-1505
    • Haycraft, C.J.1    Swoboda, P.2    Taulman, P.D.3
  • 143
    • 0036785149 scopus 로고    scopus 로고
    • The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia
    • Yoder BK, Hou X, Guay-Woodford LM. The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J Am Soc Nephrol 2002; 13: 2508-2516.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2508-2516
    • Yoder, B.K.1    Hou, X.2    Guay-Woodford, L.M.3
  • 144
    • 0037019017 scopus 로고    scopus 로고
    • Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease
    • Pazour GJ, San Agustin JT, Follit JA et al. Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr Biol 2002; 12: R378-R380.
    • (2002) Curr Biol , vol.12 , pp. R378-R380
    • Pazour, G.J.1    San Agustin, J.T.2    Follit, J.A.3
  • 145
    • 0037884961 scopus 로고    scopus 로고
    • Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease
    • USA
    • Lin F, Hiesberger T, Cordes K et al. Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease. Proc Natl Acad Sci USA 2003; 100: 5286-5291.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 5286-5291
    • Lin, F.1    Hiesberger, T.2    Cordes, K.3
  • 146
    • 0142168748 scopus 로고    scopus 로고
    • Defects in cholangiocyte fibrocystin expression and ciliary structure in the PCK rat
    • Masyuk TV, Huang BQ, Ward CJ et al. Defects in cholangiocyte fibrocystin expression and ciliary structure in the PCK rat. Gastroenterology 2003; 125: 1303-1310.
    • (2003) Gastroenterology , vol.125 , pp. 1303-1310
    • Masyuk, T.V.1    Huang, B.Q.2    Ward, C.J.3
  • 147
    • 84890100093 scopus 로고    scopus 로고
    • Primary cilia and renal cysts: Does length matter
    • Ong AC. Primary cilia and renal cysts: does length matter? Nephrol Dial Transplant 2013; 28: 2661-2663.
    • (2013) Nephrol Dial Transplant , vol.28 , pp. 2661-2663
    • Ong, A.C.1
  • 148
    • 34250012834 scopus 로고    scopus 로고
    • A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis
    • Nachury MV, Loktev AV, Zhang Q et al. A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis. Cell 2007; 129: 1201-1213.
    • (2007) Cell , vol.129 , pp. 1201-1213
    • Nachury, M.V.1    Loktev, A.V.2    Zhang, Q.3
  • 149
    • 84863992161 scopus 로고    scopus 로고
    • Scoring a backstage pass: Mechanisms of ciliogenesis and ciliary access
    • Garcia-Gonzalo FR, Reiter JF. Scoring a backstage pass: mechanisms of ciliogenesis and ciliary access. J Cell Biol 2012; 197: 697-709.
    • (2012) J Cell Biol , vol.197 , pp. 697-709
    • Garcia-Gonzalo, F.R.1    Reiter, J.F.2
  • 150
    • 0035498717 scopus 로고    scopus 로고
    • Bending the MDCK cell primary cilium increases intracellular calcium
    • Praetorius HA, Spring KR. Bending the MDCK cell primary cilium increases intracellular calcium. J Membr Biol 2001; 184: 71-79.
    • (2001) J Membr Biol , vol.184 , pp. 71-79
    • Praetorius, H.A.1    Spring, K.R.2
  • 151
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
    • Nauli SM, Alenghat FJ, Luo Y et al. Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat Genet 2003; 33: 129-137.
    • (2003) Nat Genet , vol.33 , pp. 129-137
    • Nauli, S.M.1    Alenghat, F.J.2    Luo, Y.3
  • 152
    • 33847792873 scopus 로고    scopus 로고
    • Human ADPKD primary cyst epithelial cells with a novel, single codon deletion in the PKD1 gene exhibit defective ciliary polycystin localization and loss of flow-induced Ca2+ signaling
    • Xu C, Rossetti S, Jiang L et al. Human ADPKD primary cyst epithelial cells with a novel, single codon deletion in the PKD1 gene exhibit defective ciliary polycystin localization and loss of flow-induced Ca2+ signaling. Am J Physiol Renal Physiol 2007; 292: F930-F945.
    • (2007) Am J Physiol Renal Physiol , vol.292 , pp. F930-F945
    • Xu, C.1    Rossetti, S.2    Jiang, L.3
  • 153
    • 49749145631 scopus 로고    scopus 로고
    • TRPP2 and TRPV4 form a polymodal sensory channel complex
    • Kottgen M, Buchholz B, Garcia-Gonzalez MA et al. TRPP2 and TRPV4 form a polymodal sensory channel complex. J Cell Biol 2008; 182: 437-447.
    • (2008) J Cell Biol , vol.182 , pp. 437-447
    • Kottgen, M.1    Buchholz, B.2    Garcia-Gonzalez, M.A.3
  • 154
    • 0038784537 scopus 로고    scopus 로고
    • Two populations of node monocilia initiate left-right asymmetry in the mouse
    • McGrath J, Somlo S, Makova S et al. Two populations of node monocilia initiate left-right asymmetry in the mouse. Cell 2003; 114: 61-73.
    • (2003) Cell , vol.114 , pp. 61-73
    • McGrath, J.1    Somlo, S.2    Makova, S.3
  • 155
    • 79955162632 scopus 로고    scopus 로고
    • Pkd1l1 establishes left-right asymmetry and physically interacts with Pkd2
    • Field S, Riley KL, Grimes DT et al. Pkd1l1 establishes left-right asymmetry and physically interacts with Pkd2. Development 2011; 138: 1131-1142.
    • (2011) Development , vol.138 , pp. 1131-1142
    • Field, S.1    Riley, K.L.2    Grimes, D.T.3
  • 156
    • 79955141781 scopus 로고    scopus 로고
    • Pkd1l1 complexes with Pkd2 on motile cilia and functions to establish the left-right axis
    • Kamura K, Kobayashi D, Uehara Y et al. Pkd1l1 complexes with Pkd2 on motile cilia and functions to establish the left-right axis. Development 2011; 138: 1121-1129.
    • (2011) Development , vol.138 , pp. 1121-1129
    • Kamura, K.1    Kobayashi, D.2    Uehara, Y.3
  • 157
    • 0037018850 scopus 로고    scopus 로고
    • The ion channel polycystin-2 is required for left-right axis determination in mice
    • Pennekamp P, Karcher C, Fischer A et al. The ion channel polycystin-2 is required for left-right axis determination in mice. Curr Biol 2002; 12: 938-943.
    • (2002) Curr Biol , vol.12 , pp. 938-943
    • Pennekamp, P.1    Karcher, C.2    Fischer, A.3
  • 158
    • 33645950434 scopus 로고    scopus 로고
    • Lack of a laterality phenotype in Pkd1 knock-out embryos correlates with absence of polycystin-1 in nodal cilia
    • Karcher C, Fischer A, Schweickert A et al. Lack of a laterality phenotype in Pkd1 knock-out embryos correlates with absence of polycystin-1 in nodal cilia. Differentiation 2005; 73: 425-432.
    • (2005) Differentiation , vol.73 , pp. 425-432
    • Karcher, C.1    Fischer, A.2    Schweickert, A.3
  • 159
    • 84890345523 scopus 로고    scopus 로고
    • Primary cilia are specialized calcium signalling organelles
    • Delling M, DeCaen PG, Doerner JF et al. Primary cilia are specialized calcium signalling organelles. Nature 2013; 504: 311-314.
    • (2013) Nature , vol.504 , pp. 311-314
    • Delling, M.1    Decaen, P.G.2    Doerner, J.F.3
  • 160
    • 84890352250 scopus 로고    scopus 로고
    • Direct recording and molecular identification of the calcium channel of primary cilia
    • DeCaen PG, Delling M, Vien TN et al. Direct recording and molecular identification of the calcium channel of primary cilia. Nature 2013; 504: 315-318.
    • (2013) Nature , vol.504 , pp. 315-318
    • Decaen, P.G.1    Delling, M.2    Vien, T.N.3
  • 161
    • 79960590689 scopus 로고    scopus 로고
    • Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases
    • USA
    • Choi YH, Suzuki A, Hajarnis S et al. Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases. Proc Natl Acad Sci USA 2011; 108: 10679-10684.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 10679-10684
    • Choi, Y.H.1    Suzuki, A.2    Hajarnis, S.3
  • 162
    • 58849146635 scopus 로고    scopus 로고
    • Vasopressin receptormediated functional signaling pathway in primary cilia of renal epithelial cells
    • Raychowdhury MK, Ramos AJ, Zhang P et al. Vasopressin receptormediated functional signaling pathway in primary cilia of renal epithelial cells. Am J Physiol Renal Physiol 2009; 296: F87-F97.
    • (2009) Am J Physiol Renal Physiol , vol.296 , pp. F87-F97
    • Raychowdhury, M.K.1    Ramos, A.J.2    Zhang, P.3
  • 163
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • USA
    • Pisitkun T, Shen RF, Knepper MA. Identification and proteomic profiling of exosomes in human urine. Proc Natl Acad Sci USA 2004; 101: 13368-13373.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 164
    • 59949104184 scopus 로고    scopus 로고
    • Characterization of PKD protein-positive exosome-like vesicles
    • Hogan MC, Manganelli L, Woollard JR et al. Characterization of PKD protein-positive exosome-like vesicles. J Am Soc Nephrol 2009; 20: 278-288.
    • (2009) J Am Soc Nephrol , vol.20 , pp. 278-288
    • Hogan, M.C.1    Manganelli, L.2    Woollard, J.R.3
  • 165
    • 82655181482 scopus 로고    scopus 로고
    • Epitope-tagged Pkhd1 tracks the processing, secretion, and localization of fibrocystin
    • Bakeberg JL, Tammachote R, Woollard JR et al. Epitope-tagged Pkhd1 tracks the processing, secretion, and localization of fibrocystin. J Am Soc Nephrol 2011; 22: 2266-2277.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 2266-2277
    • Bakeberg, J.L.1    Tammachote, R.2    Woollard, J.R.3
  • 166
    • 29444450890 scopus 로고    scopus 로고
    • Defective planar cell polarity in polycystic kidney disease
    • Fischer E, Legue E, Doyen A et al. Defective planar cell polarity in polycystic kidney disease. Nat Genet 2006; 38: 21-23.
    • (2006) Nat Genet , vol.38 , pp. 21-23
    • Fischer, E.1    Legue, E.2    Doyen, A.3
  • 167
    • 20944435539 scopus 로고    scopus 로고
    • Inversin, the gene product mutated in nephronophthisis type II, functions as a molecular switch between Wnt signaling pathways
    • Simons M, Gloy J, Ganner A et al. Inversin, the gene product mutated in nephronophthisis type II, functions as a molecular switch between Wnt signaling pathways. Nat Genet 2005; 37: 537-543.
    • (2005) Nat Genet , vol.37 , pp. 537-543
    • Simons, M.1    Gloy, J.2    Ganner, A.3
  • 168
    • 34948834648 scopus 로고    scopus 로고
    • Polycystin-1 induces cell migration by regulating phosphatidylinositol 3-kinase-dependent cytoskeletal rearrangements and GSK3beta-dependent cell cell mechanical adhesion
    • Boca M, D'Amato L, Distefano G et al. Polycystin-1 induces cell migration by regulating phosphatidylinositol 3-kinase-dependent cytoskeletal rearrangements and GSK3beta-dependent cell cell mechanical adhesion. Mol Biol Cell 2007; 18: 4050-4061.
    • (2007) Mol Biol Cell , vol.18 , pp. 4050-4061
    • Boca, M.1    D'Amato, L.2    Distefano, G.3
  • 169
    • 77956555166 scopus 로고    scopus 로고
    • Aberrant regulation of planar cell polarity in polycystic kidney disease
    • Luyten A, Su X, Gondela S et al. Aberrant regulation of planar cell polarity in polycystic kidney disease. J Am Soc Nephrol 2010; 21: 1521-1532.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 1521-1532
    • Luyten, A.1    Su, X.2    Gondela, S.3
  • 170
    • 77949361893 scopus 로고    scopus 로고
    • Loss of oriented cell division does not initiate cyst formation
    • Nishio S, Tian X, Gallagher AR et al. Loss of oriented cell division does not initiate cyst formation. J Am Soc Nephrol 2010; 21: 295-302.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 295-302
    • Nishio, S.1    Tian, X.2    Gallagher, A.R.3
  • 171
    • 84877018892 scopus 로고    scopus 로고
    • The Meckel syndrome protein meckelin (TMEM67) is a key regulator of cilia function but is not required for tissue planar polarity
    • Leightner AC, Hommerding CJ, Peng Y et al. The Meckel syndrome protein meckelin (TMEM67) is a key regulator of cilia function but is not required for tissue planar polarity. Hum Mol Genet 2013; 22: 2024-2040.
    • (2013) Hum Mol Genet , vol.22 , pp. 2024-2040
    • Leightner, A.C.1    Hommerding, C.J.2    Peng, Y.3
  • 172
    • 67649878597 scopus 로고    scopus 로고
    • Wnt9b signaling regulates planar cell polarity and kidney tubule morphogenesis
    • Karner CM, Chirumamilla R, Aoki S et al. Wnt9b signaling regulates planar cell polarity and kidney tubule morphogenesis. Nat Genet 2009; 41: 793-799.
    • (2009) Nat Genet , vol.41 , pp. 793-799
    • Karner, C.M.1    Chirumamilla, R.2    Aoki, S.3
  • 173
    • 84886654516 scopus 로고    scopus 로고
    • Polycystin-1 binds Par3/aPKC and controls convergent extension during renal tubular morphogenesis
    • Castelli M, Boca M, Chiaravalli M et al. Polycystin-1 binds Par3/aPKC and controls convergent extension during renal tubular morphogenesis. Nat Commun 2013; 4: 2658.
    • (2013) Nat Commun , vol.4 , pp. 2658
    • Castelli, M.1    Boca, M.2    Chiaravalli, M.3
  • 174
    • 41349107244 scopus 로고    scopus 로고
    • THM1 negatively modulates mouse sonic hedgehog signal transduction and affects retrograde intraflagellar transport in cilia
    • Tran PV, Haycraft CJ, Besschetnova TY et al. THM1 negatively modulates mouse sonic hedgehog signal transduction and affects retrograde intraflagellar transport in cilia. Nat Genet 2008; 40: 403-410.
    • (2008) Nat Genet , vol.40 , pp. 403-410
    • Tran, P.V.1    Haycraft, C.J.2    Besschetnova, T.Y.3
  • 175
    • 84921802641 scopus 로고    scopus 로고
    • Downregulating hedgehog signaling reduces renal cystogenic potential of mouse models
    • Tran PV, Talbott GC, Turbe-Doan A et al. Downregulating hedgehog signaling reduces renal cystogenic potential of mouse models. J Am Soc Nephrol 2014; 25: 2201-2212.
    • (2014) J Am Soc Nephrol , vol.25 , pp. 2201-2212
    • Tran, P.V.1    Talbott, G.C.2    Turbe-Doan, A.3
  • 176
    • 33745268851 scopus 로고    scopus 로고
    • Mutations in GLIS3 are responsible for a rare syndrome with neonatal diabetes mellitus and congenital hypothyroidism
    • Senee V, Chelala C, Duchatelet S et al. Mutations in GLIS3 are responsible for a rare syndrome with neonatal diabetes mellitus and congenital hypothyroidism. Nat Genet 2006; 38: 682-687.
    • (2006) Nat Genet , vol.38 , pp. 682-687
    • Senee, V.1    Chelala, C.2    Duchatelet, S.3
  • 177
    • 66349117479 scopus 로고    scopus 로고
    • Glis3 is associated with primary cilia and Wwtr1/TAZ and implicated in polycystic kidney disease
    • Kang HS, Beak JY, Kim YS et al. Glis3 is associated with primary cilia and Wwtr1/TAZ and implicated in polycystic kidney disease. Mol Cell Biol 2009; 29: 2556-2569.
    • (2009) Mol Cell Biol , vol.29 , pp. 2556-2569
    • Kang, H.S.1    Beak, J.Y.2    Kim, Y.S.3
  • 178
    • 33748085676 scopus 로고    scopus 로고
    • Haploinsufficiency of Pkd2 is associated with increased tubular cell proliferation and interstitial fibrosis in two murine Pkd2 models
    • Chang MY, Parker E, Ibrahim S et al. Haploinsufficiency of Pkd2 is associated with increased tubular cell proliferation and interstitial fibrosis in two murine Pkd2 models. Nephrol Dial Transplant 2006; 21: 2078-2084.
    • (2006) Nephrol Dial Transplant , vol.21 , pp. 2078-2084
    • Chang, M.Y.1    Parker, E.2    Ibrahim, S.3
  • 179
    • 28544433252 scopus 로고    scopus 로고
    • Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2
    • Li X, Luo Y, Starremans PG et al. Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2. Nat Cell Biol 2005; 7: 1202-1212.
    • (2005) Nat Cell Biol , vol.7 , pp. 1202-1212
    • Li, X.1    Luo, Y.2    Starremans, P.G.3
  • 180
    • 50849100989 scopus 로고    scopus 로고
    • Loss of polycystin-1 causes centrosome amplification and genomic instability
    • Battini L, Macip S, Fedorova E et al. Loss of polycystin-1 causes centrosome amplification and genomic instability. Hum Mol Genet 2008; 17: 2819-2833.
    • (2008) Hum Mol Genet , vol.17 , pp. 2819-2833
    • Battini, L.1    Macip, S.2    Fedorova, E.3
  • 181
    • 84883455352 scopus 로고    scopus 로고
    • Loss of cilia suppresses cyst growth in genetic models of autosomal dominant polycystic kidney disease
    • Ma M, Tian X, Igarashi P et al. Loss of cilia suppresses cyst growth in genetic models of autosomal dominant polycystic kidney disease. Nat Genet 2013; 45: 1004-1012.
    • (2013) Nat Genet , vol.45 , pp. 1004-1012
    • Ma, M.1    Tian, X.2    Igarashi, P.3
  • 182
    • 70350346866 scopus 로고    scopus 로고
    • Polycystin-1 and-2 dosage regulates pressure sensing
    • Sharif-Naeini R, Folgering JH, Bichet D et al. Polycystin-1 and-2 dosage regulates pressure sensing. Cell 2009; 139: 587-596.
    • (2009) Cell , vol.139 , pp. 587-596
    • Sharif-Naeini, R.1    Folgering, J.H.2    Bichet, D.3
  • 183
    • 84861166382 scopus 로고    scopus 로고
    • Mechanoprotection by polycystins against apoptosis is mediated through the opening of stretch-activated K(2P) channels
    • Peyronnet R, Sharif-Naeini R, Folgering JH et al. Mechanoprotection by polycystins against apoptosis is mediated through the opening of stretch-activated K(2P) channels. Cell Rep 2012; 1: 241-250.
    • (2012) Cell Rep , vol.1 , pp. 241-250
    • Peyronnet, R.1    Sharif-Naeini, R.2    Folgering, J.H.3
  • 184
    • 84926482985 scopus 로고    scopus 로고
    • Inactivation of integrin-beta1 prevents the development of polycystic kidney disease after the loss of polycystin-1
    • Lee K, Boctor S, Barisoni LM et al. Inactivation of integrin-beta1 prevents the development of polycystic kidney disease after the loss of polycystin-1. J Am Soc Nephrol 2014; 26: 888-895.
    • (2014) J Am Soc Nephrol , vol.26 , pp. 888-895
    • Lee, K.1    Boctor, S.2    Barisoni, L.M.3
  • 185
    • 18744363653 scopus 로고    scopus 로고
    • Mispolarization of desmosomal proteins and altered intercellular adhesion in autosomal dominant polycystic kidney disease
    • Silberberg M, Charron AJ, Bacallao R et al. Mispolarization of desmosomal proteins and altered intercellular adhesion in autosomal dominant polycystic kidney disease. Am J Physiol Renal Physiol 2005; 288: F1153-F1163.
    • (2005) Am J Physiol Renal Physiol , vol.288 , pp. F1153-F1163
    • Silberberg, M.1    Charron, A.J.2    Bacallao, R.3
  • 186
    • 38349078529 scopus 로고    scopus 로고
    • Pkd1 and Nek8 mutations affect cell-cell adhesion and cilia in cysts formed in kidney organ cultures
    • Natoli TA, Gareski TC, Dackowski WR et al. Pkd1 and Nek8 mutations affect cell-cell adhesion and cilia in cysts formed in kidney organ cultures. Am J Physiol Renal Physiol 2008; 294: F73-F83.
    • (2008) Am J Physiol Renal Physiol , vol.294 , pp. F73-F83
    • Natoli, T.A.1    Gareski, T.C.2    Dackowski, W.R.3
  • 187
    • 0034600035 scopus 로고    scopus 로고
    • Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells
    • Charron AJ, Nakamura S, Bacallao R et al. Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells. J Cell Biol 2000; 149: 111-124.
    • (2000) J Cell Biol , vol.149 , pp. 111-124
    • Charron, A.J.1    Nakamura, S.2    Bacallao, R.3
  • 188
    • 79955634491 scopus 로고    scopus 로고
    • The exocyst protein Sec10 interacts with polycystin-2 and knockdown causes PKD-phenotypes
    • Fogelgren B, Lin SY, Zuo X et al. The exocyst protein Sec10 interacts with polycystin-2 and knockdown causes PKD-phenotypes. PLoS Genet 2011; 7: e1001361.
    • (2011) PLoS Genet , vol.7 , pp. e1001361
    • Fogelgren, B.1    Lin, S.Y.2    Zuo, X.3
  • 189
    • 33750694608 scopus 로고    scopus 로고
    • Stable knockdown of polycystin-1 confers integrin-alpha2beta1-mediated anoikis resistance
    • Battini L, Fedorova E, Macip S et al. Stable knockdown of polycystin-1 confers integrin-alpha2beta1-mediated anoikis resistance. J Am Soc Nephrol 2006; 17: 3049-3058.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 3049-3058
    • Battini, L.1    Fedorova, E.2    Macip, S.3
  • 190
    • 33749257880 scopus 로고    scopus 로고
    • Functional characterization of PKDREJ, a male germ cell-restricted polycystin
    • Sutton KA, Jungnickel MK, Ward CJ et al. Functional characterization of PKDREJ, a male germ cell-restricted polycystin. J Cell Physiol 2006; 209: 493-500.
    • (2006) J Cell Physiol , vol.209 , pp. 493-500
    • Sutton, K.A.1    Jungnickel, M.K.2    Ward, C.J.3
  • 191
    • 33747621396 scopus 로고    scopus 로고
    • Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor
    • USA
    • Ishimaru Y, Inada H, Kubota M et al. Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor. Proc Natl Acad Sci USA 2006; 103: 12569-12574.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 12569-12574
    • Ishimaru, Y.1    Inada, H.2    Kubota, M.3
  • 192
    • 70350787052 scopus 로고    scopus 로고
    • Upregulation of PKD1L2 provokes a complex neuromuscular disease in the mouse
    • Mackenzie FE, Romero R, Williams D et al. Upregulation of PKD1L2 provokes a complex neuromuscular disease in the mouse. Hum Mol Genet 2009; 18: 3553-3566.
    • (2009) Hum Mol Genet , vol.18 , pp. 3553-3566
    • Mackenzie, F.E.1    Romero, R.2    Williams, D.3
  • 193
    • 48849084706 scopus 로고    scopus 로고
    • Expression of Pkd2l2 in testis is implicated in spermatogenesis
    • Chen Y, Zhang Z, Lv XY et al. Expression of Pkd2l2 in testis is implicated in spermatogenesis. Biol Pharm Bull 2008; 31: 1496-1500.
    • (2008) Biol Pharm Bull , vol.31 , pp. 1496-1500
    • Chen, Y.1    Zhang, Z.2    Lv, X.Y.3
  • 194
    • 0034700483 scopus 로고    scopus 로고
    • Co-assembly of polycystin-1 and-2 produces unique cation-permeable currents
    • Hanaoka K, Qian F, Boletta A et al. Co-assembly of polycystin-1 and-2 produces unique cation-permeable currents. Nature 2000; 408: 990-994.
    • (2000) Nature , vol.408 , pp. 990-994
    • Hanaoka, K.1    Qian, F.2    Boletta, A.3
  • 195
    • 84923872599 scopus 로고    scopus 로고
    • Aberrant glycosylation and localization of polycystin-1 cause polycystic kidney in an AQP11 knockout model
    • Inoue Y, Sohara E, Kobayashi K et al. Aberrant glycosylation and localization of polycystin-1 cause polycystic kidney in an AQP11 knockout model. J Am Soc Nephrol 2014; 25: 2789-2799.
    • (2014) J Am Soc Nephrol , vol.25 , pp. 2789-2799
    • Inoue, Y.1    Sohara, E.2    Kobayashi, K.3
  • 196
    • 0037385521 scopus 로고    scopus 로고
    • Positional cloning of jcpk/bpk locus of the mouse
    • Cogswell C, Price SJ, Hou X et al. Positional cloning of jcpk/bpk locus of the mouse. Mamm Genome 2003; 14: 242-249.
    • (2003) Mamm Genome , vol.14 , pp. 242-249
    • Cogswell, C.1    Price, S.J.2    Hou, X.3
  • 197
    • 77958565531 scopus 로고    scopus 로고
    • Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/SH3 domain interaction and regulates the apoptotic response in mammals
    • Wodarczyk C, Distefano G, Rowe I et al. Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/SH3 domain interaction and regulates the apoptotic response in mammals. PLoS One 2010; 5: e12719.
    • (2010) PLoS One , vol.5 , pp. e12719
    • Wodarczyk, C.1    Distefano, G.2    Rowe, I.3
  • 198
    • 84964315230 scopus 로고    scopus 로고
    • Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of polycystic kidney disease 1 protein
    • Su X, Driscoll K, Yao G et al. Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of polycystic kidney disease 1 protein. Hum Mol Genet 2014; 23: 5441-5451.
    • (2014) Hum Mol Genet , vol.23 , pp. 5441-5451
    • Su, X.1    Driscoll, K.2    Yao, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.