ライフサイエンスコーパス: polycystin

1 ADPKD progression following inactivation of polycystins.

2 egorize the effects of missense mutations in polycystins.

3 n detected between the ARPKD FPC protein and polycystins.

4 or that represses cystogenesis distinct from polycystins.

5 der that is caused by mutations at two loci, polycystin 1 (PKD1) and polycystin 2 (PKD2).

6 Mutations in polycystin 1 and 2 (PC1 and PC2) cause the common geneti

7 ations in the PKD1 or PKD2 genes that encode Polycystin 1 and 2 (PC1/2), transmembrane proteins that

8 c kidney disease (PKD), genetic mutations in polycystin 1 and 2 lead to defective intracellular traff

9 Polycystin 1 and polycystin 2 are large transmembrane pr

10 Mutations in polycystin 1 and polycystin 2 are responsible for autoso

11 ons in the PKD1 and PKD2 genes, encoding the polycystin 1 and polycystin 2 Ca(2+) ion channels, respe

12 se is inversely correlated with the level of polycystin 1 function.

13 The inactivation of the ciliary proteins polycystin 1 or polycystin 2 leads to autosomal dominant

14 s) and the polycystic kidney disease-causing polycystin 1/2 complex.

15 utations in the PKD1 or PKD2 genes, encoding polycystins 1 and 2 (PC1 and PC2).

16 is caused by mutations in the genes encoding polycystin-1 (PC-1) and polycystin-2 (PC-2).

17 TORC1 negatively regulates the biogenesis of polycystin-1 (PC-1) and trafficking of the PC-1/2 comple

18 Polycystin-1 (PC-1) is a G protein-coupled receptor-like

19 Polycystin-1 (PC1) and -2 (PC2), the two ADPKD gene prod

20 aled that the protein and mRNA expression of polycystin-1 (PC1) and polycystin-2 (PC2) were increased

21 The ADPKD proteins encoded by these genes, polycystin-1 (PC1) and polycystin-2 (PC2), form a plasma

22 The ADPKD proteins, termed as polycystin-1 (PC1) and polycystin-2 (PC2), interact via

23 tations of the PKD1 and PKD2 genes, encoding polycystin-1 (PC1) and polycystin-2 (PC2), respectively,

24 gous mutations in PKD1 or PKD2, which encode polycystin-1 (PC1) and polycystin-2 (PC2), respectively,

25 aused by mutations in PKD1 and PKD2 encoding polycystin-1 (PC1) and polycystin-2 (PC2), respectively.

26 encode the multipass transmembrane proteins polycystin-1 (PC1) and polycystin-2 (PC2), respectively.

27 is caused by mutations in the genes encoding polycystin-1 (PC1) and polycystin-2 (PC2), which form an

28 d by mutations in PKD1 or PKD2 which encodes polycystin-1 (PC1) and polycystin-2, respectively.

29 The polycystin-1 (PC1) and pVHL proteins may therefore parti

30 t two-hybrid screens using the C-terminus of polycystin-1 (PC1) as bait.

31 Polycystin-1 (Pc1) cleavage at the G protein-coupled rec

32 Mutations in polycystin-1 (PC1) give rise to autosomal dominant polyc

33 ll subunits of the BBSome, the ADPKD protein polycystin-1 (PC1) interacts with BBS1, BBS4, BBS5 and B

34 Polycystin-1 (PC1) is a large membrane protein that is e

35 Polycystin-1 (PC1) is a transmembrane protein originally

36 Mutation of polycystin-1 (PC1) is the major cause of autosomal domin

37 Mutations in polycystin-1 (PC1) lead to autosomal-dominant polycystic

38 Dysregulation of polycystin-1 (PC1) leads to autosomal dominant polycysti

39 Polycystin-1 (PC1) mutations result in proliferative ren

40 ning disorder, commonly caused by defects in polycystin-1 (PC1) or polycystin-2 (PC2), in which tubul

41 ve copy of either PKD1 or PKD2, which encode polycystin-1 (PC1) or polycystin-2 (PC2), respectively.

42 acid sequence, KVHPSST, in the C-terminus of polycystin-1 (PC1) that serves as a ciliary-targeting si

43 Mutations in the gene coding for polycystin-1 (PC1) underlie the majority of cases but th

44 The protein product of PKD1 (polycystin-1 (PC1)) is a large transmembrane protein wit

45 Defective ciliary localization of polycystin-1 (PC1), a large integral membrane protein en

46 Mutations in Pkd1, encoding polycystin-1 (PC1), cause autosomal-dominant polycystic

47 Mutations in PKD1, which encodes polycystin-1 (PC1), contribute to >85% of cases of autos

48 Polycystin-1 (PC1), encoded by the PKD1 gene that is mut

49 The polycystin-1 (PC1), polycystin-2 (PC2) and fibrocystin p

50 in liver and kidney as the result of reduced polycystin-1 (PC1).

51 s with mutations in the gene (PKD1) encoding polycystin-1 (PC1).

52 mostly caused by mutations in PKD1, encoding polycystin-1 (PC1).

53 ysregulation of the PKD1 gene, which encodes polycystin-1 (PC1).

54 the PKD1 gene product, the membrane protein polycystin-1 (PC1).

55 Mutations in the genes encoding polycystin-1 (PC1, PKD1) or polycystin-2 (PC2, PKD2) cau

56 ease, a genetic disease caused by defects in polycystin-1 (Pkd1) or polycystin-2 (Pkd2).

57 We demonstrate for the first time that polycystin-1 (required for cilia function) and polaris (

58 Reduced expression of polycystin-1 also serves to sensitize the kidney to cyst

59 Smooth muscle cell polycystin-1 and -2 (TRPP1 and -2) proteins modulate the

60 dentification of mutations in genes encoding polycystin-1 and -2 in polycystic kidney diseases.

61 Studies of the ADPKD proteins, polycystin-1 and -2, and the development and characteriz

62 ncident collecting duct-specific knockout of polycystin-1 and AC6 (also homozygous for the floxed ADC

63 roteomic analysis confirmed that cleavage of polycystin-1 and fibrocystin occurs in vivo, in manners

64 ng down 2 primary cilia structural proteins, polycystin-1 and intraflagellar protein-88.

65 bolish calcium and nitric oxide signaling in polycystin-1 and polaris mutant endothelial cells.

66 cystin research, with a focus on the role of polycystin-1 and polycystin-2 in primary cilia and the c

67 y-membrane translocation of the PKD proteins polycystin-1 and polycystin-2 is compromised in DZIP1L-m

68 ycystic kidney disease (ADPKD) gene products polycystin-1 and polycystin-2 localize to both cilia and

69 Polycystic kidney disease proteins, polycystin-1 and polycystin-2, localize to primary cilia

70 y caused by the genes PKD1 or PKD2 (encoding polycystin-1 and polycystin-2, respectively) and ARPKD c

71 KD2, which encode the transmembrane proteins polycystin-1 and polycystin-2, respectively, cause autos

72 Studies suggest that polycystin-1 and polycystin-2, which are encoded by PKD1

73 the polycystic kidney disease gene products, polycystin-1 and polycystin-2.

74 s with a novel ciliary targeting sequence of polycystin-1 and regulates polycystin-1 trafficking.

75 consistent with cleavage at the GPS site in polycystin-1 and the proprotein convertase site in fibro

76 Mutations in polycystin-1 and transient receptor potential polycystin

77 ene product demonstrated distinct effects on polycystin-1 biogenesis.

78 Collecting duct-specific knockout of polycystin-1 caused massive renal cyst formation, kidney

79 These studies suggest that nephron polycystin-1 deficiency does not itself contribute to AD

80 een cystic dilation and levels of functional polycystin-1 following mutation of Prkcsh or Sec63.

81 define genetic and biochemical modulators of polycystin-1 function and provide a more complete defini

82 inhibition increases steady-state levels of polycystin-1 in cells lacking glucosidase IIbeta and tha

83 s on the proper localization and function of polycystin-1 in cilia.

84 demonstrate, for the first time, a role for polycystin-1 in kidney injury and repair and indicate th

85 ibe a potential physiologic role for nephron polycystin-1 in the absence of cysts, tubule dilation, o

86 We investigated whether polycystin-1 is a bone mechanosensor.

87 These data indicate that polycystin-1 is essential for the anabolic response to s

88 We find that polycystin-1 is the rate-limiting component of this comp

89 t Tulp3 loss did not inhibit cystogenesis in polycystin-1 knockouts, unlike ciliary disruption.

90 cystic kidney disease (ADPKD) gene products, polycystin-1 or -2, are reduced.

91 e-dimensional structure after loss of either polycystin-1 or -2.

92 intermediate between that caused by loss of polycystin-1 or cilia.

93 el in its homomeric complex and in the TRPP2/polycystin-1 receptor/ion channel complex.

94 Polycystin-1 represses NHA2 expression via Ca(2+) /NFAT

95 eting sequence of polycystin-1 and regulates polycystin-1 trafficking.

96 PKD1 (polycystin-1), the disease-causing gene for ADPKD, is wi

97 , demarcated by the presence of aquaporin-2, polycystin-1, and podocin.

98 D, which displays a hypomorphic phenotype of polycystin-1, demonstrated increased cyst progression an

99 Vs) and isolated a subpopulation abundant in polycystin-1, fibrocystin (in their cleaved forms), and

100 In the Medicago lineage, nodule-specific Polycystin-1, Lipoxygenase, Alpha Toxin (PLAT) domain pr

101 nsertions in a M. truncatula nodule-specific polycystin-1, lipoxygenase, alpha-toxin (PLAT) domain-en

102 e investigated the role of the intracellular polycystin-1, lipoxygenase, and alpha-toxin (PLAT) signa

103 gene encodes a large transmembrane protein (polycystin-1, or PC-1) that is reported to function as a

104 tosomal recessive polycystic kidney disease (polycystin-1, polycystin-2, and fibrocystin) localize to

105 inergic Ca(2+) signaling may be regulated by polycystin-1, since ORPK cells only expressed the C-term

106 s in defective maturation and trafficking of polycystin-1, the central determinant of cyst pathogenes

107 In polycystin-1-deficient mice, MIF was required for recrui

108 regulated in cyst-lining epithelial cells in polycystin-1-deficient murine kidneys and accumulated in

109 ation of the Ire1alpha-Xbp1 pathway or cause polycystin-1-dependent PKD.

110 PKD1L1 encodes a polycystin-1-like protein and its loss of function is kn

111 egments in embryonic mouse kidney results in polycystin-1-mediated polycystic kidney disease (PKD).

112 It is unknown whether the Pkd1 gene product polycystin-1-the predominant causal factor in ADPKD-itse

113 to PC2 trafficking and its interaction with polycystin-1.

114 stresses through proteolytic modification of polycystin-1.

115 yst development, either in genetic models of polycystin-1/2 reduction or in response to ischemia/repe

116 um binding from the membrane-targeting PLAT (polycystin-1/lipoxygenase/alpha-toxin) domain to the act

117 a role by which GPSM1 increased heteromeric polycystin-1/polycystin-2 ion channel activity via Gbeta

118 Polycystin 2 (PC2 or TRPP1, formerly TRPP2) is a calcium

119 ase complex that targets the ciliary protein polycystin 2 (PC2) for degradation, but whether Nek and

120 e showed that the ER cation-permeant channel polycystin 2 (PC2) functions to reduce mitochondria-ER c

121 Polycystin 2 (PC2) is a calcium-dependent calcium channe

122 nvestigate the effect of decreased levels of polycystin 2 (PC2), a calcium channel that interacts wit

123 c1 functions by modulating the expression of polycystin 2 (Pkd2), a member of the transient receptor

124 Polycystin 2 (Pkd2), which belongs to the transient rece

125 tations at two loci, polycystin 1 (PKD1) and polycystin 2 (PKD2).

126 olycystin-1 and transient receptor potential polycystin 2 (TRPP2) account for almost all clinically i

127 t may be a result of aberrant trafficking of polycystin 2 and other ciliary proteins.

128 iliary function through its association with polycystin 2 and provides evidence of a further link bet

129 tin 2, dual morpholino-mediated knockdown of polycystin 2 and RP2 results in enhanced situs inversus,

130 Polycystin 1 and polycystin 2 are large transmembrane proteins, which, wh

131 Mutations in polycystin 1 and polycystin 2 are responsible for autosomal dominant poly

132 nd PKD2 genes, encoding the polycystin 1 and polycystin 2 Ca(2+) ion channels, respectively, result i

133 Our results suggest that polycystin 2 deficiency causes increased collagen II syn

134 In zebrafish, polycystin 2 knockdown induces kidney cysts, hydrocephal

135 tion of the ciliary proteins polycystin 1 or polycystin 2 leads to autosomal dominant polycystic kidn

136 ented the dorsal axis curvature formation in polycystin 2 morphants and curly up polycystin 2 mutants

137 al axis curvature and kidney cystogenesis in polycystin 2 morphants.

138 ation in polycystin 2 morphants and curly up polycystin 2 mutants.

139 s canonical binding site (EF-hand domain) of polycystin 2, a Ca(2+)-dependent channel with relevance

140 bserved physical interaction between RP2 and polycystin 2, dual morpholino-mediated knockdown of poly

141 ased notochord sheath collagen deposition in polycystin 2-deficient embryos is directly linked to axi

142 rectly and coordinate the ciliary removal of polycystin 2.

143 l dominant polycystic kidney disease protein polycystin 2.

144 n the genes encoding polycystin-1 (PC-1) and polycystin-2 (PC-2).

145 Polycystin-2 (PC2 or TRPPC2), a member of the transient

146 The polycystin-1 (PC1), polycystin-2 (PC2) and fibrocystin proteins, the respect

147 n 33 (TMEM33) interacts with the ion channel polycystin-2 (PC2) at the endoplasmic reticulum (ER) mem

148 Polycystin-2 (PC2) belongs to the transient receptor pot

149 Loss of polycystin-2 (PC2) in mice (Pkd2(-/-)) results in total

150 Polycystin-2 (PC2) is a Ca(2+)-permeable transient recep

151 Polycystin-2 (PC2) is a TRP-type, Ca(2+)-permeable non-s

152 Mutations in polycystin-2 (PC2) lead to autosomal dominant polycystic

153 Notably, NEK8 and polycystin-2 (PC2) proteins interact, and we found that

154 ied a missense mutation in the gene encoding polycystin-2 (PC2) that prevented this protein from prop

155 nd mRNA expression of polycystin-1 (PC1) and polycystin-2 (PC2) were increased in jck mouse kidneys.

156 Polycystin-2 (PC2), a ciliary calcium channel that is mu

157 The human PKD2 locus encodes Polycystin-2 (PC2), a TRPP channel that localises to sev

158 coded by these genes, polycystin-1 (PC1) and polycystin-2 (PC2), form a plasma membrane receptor-ion

159 y caused by defects in polycystin-1 (PC1) or polycystin-2 (PC2), in which tubular epithelia form flui

160 D proteins, termed as polycystin-1 (PC1) and polycystin-2 (PC2), interact via their C-termini to form

161 or PKD2, which encode polycystin-1 (PC1) and polycystin-2 (PC2), respectively, cause autosomal domina

162 PKD2 genes, encoding polycystin-1 (PC1) and polycystin-2 (PC2), respectively, lead to autosomal domi

163 or PKD2, which encode polycystin-1 (PC1) or polycystin-2 (PC2), respectively.

164 KD1 and PKD2 encoding polycystin-1 (PC1) and polycystin-2 (PC2), respectively.

165 ransmembrane proteins polycystin-1 (PC1) and polycystin-2 (PC2), respectively.

166 in the genes encoding polycystin-1 (PC1) and polycystin-2 (PC2), which form an ion channel complex th

167 In polycystin-2 (PC2)-defective mice, cyclic adenosine mono

168 e genes encoding polycystin-1 (PC1, PKD1) or polycystin-2 (PC2, PKD2) cause ADPKD, and PKD1 mutations

169 Polycystin-2 (PC2, TRPP2) is a Ca(2+)-permeable, nonsele

170 Polycystin-2 (PC2, TRPP2), a member of the transient rec

171 Polycystin-2 (PC2, TRPP2), the gene product of PKD2, who

172 The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca(2+)-permeable channel, is

173 us work has indicated that sensory cilia and polycystin-2 (Pkd2), a cation channel, are required for

174 nterferes with expression of the TRP channel polycystin-2 (PKD2).

175 caused by defects in polycystin-1 (Pkd1) or polycystin-2 (Pkd2).

176 biochemically and genetically interacts with polycystin-2 (the protein product of the polycystic kidn

177 pting the recycling endosome reduces ciliary polycystin-2 and causes its accumulation in the recyclin

178 Our analysis showed that fibrocystin and polycystin-2 are dependent on IFT20, GMAP210, and the ex

179 he activation of which may reduce functional polycystin-2 below a critical threshold, precipitating t

180 the structural and mechanistic regulation of polycystin-2 by its TOP domain-a site with unknown funct

181 f PKD2 variants associated with ADPKD, where polycystin-2 channel dysregulation in the primary cilia

182 changes in the activation of the associated polycystin-2 channel or other intracellular events media

183 The biophysical properties of single polycystin-2 channels were investigated using a planar l

184 Biophysical properties of lacrimal gland polycystin-2 channels were similar to those described fo

185 is of immunogold labeling revealed strongest polycystin-2 expression on the membranes of the endoplas

186 with a focus on the role of polycystin-1 and polycystin-2 in primary cilia and the cell cycle.

187 ls generated from ADPKD patients do not show polycystin-2 in the cilia and are unable to sense fluid

188 We propose a new role for polycystin-2 in transmitting extracellular shear stress

189 ich GPSM1 increased heteromeric polycystin-1/polycystin-2 ion channel activity via Gbetagamma subunit

190 netic variants in PKD2 which encodes for the polycystin-2 ion channel are responsible for many clinic

191 ocation of the PKD proteins polycystin-1 and polycystin-2 is compromised in DZIP1L-mutant cells.

192 Polycystin-2 is found in organelle membranes, including

193 Here, we show that polycystin-2 is localized to the cilia of mouse and huma

194 The PKD2 encoding for polycystin-2 is mutated in approximately 15% of ADPKD pa

195 Polycystin-2 is therefore likely to play multiple roles

196 sease (ADPKD) gene products polycystin-1 and polycystin-2 localize to both cilia and EVs, act in the

197 Furthermore, exocyst Sec8 and polycystin-2 no longer localize to primary cilia or the

198 solated artery, we further show that ciliary polycystin-2 responds specifically to shear stress and n

199 ted N-terminal ciliary-targeting sequence in polycystin-2 similarly binds Arf4.

200 Thus, aberrant expression or localization of polycystin-2 to cilia could promote high blood pressure

201 normal expression level and localization of polycystin-2 to cilia is required for the endothelial ci

202 ciliary localization of the membrane protein Polycystin-2, a protein playing an important role in the

203 ive polycystic kidney disease (polycystin-1, polycystin-2, and fibrocystin) localize to various subce

204 the transport of ciliary components such as polycystin-2, and partial loss of this enzyme is suffici

205 ects the ciliary trafficking of fibrocystin, polycystin-2, and smoothened.

206 that PDE1A activity is altered downstream of polycystin-2, and suggest that PDE1A is a viable drug ta

207 kDa, pericentriolar material protein 1, and polycystin-2, as well as the Golgi distribution of its b

208 n of the cilium and the ciliary transport of polycystin-2, as well as to alter proliferation signals

209 In addition, we found that polycystin-2, but not smoothened or fibrocystin, require

210 ic kidney disease proteins, polycystin-1 and polycystin-2, localize to primary cilia.

211 l channel-forming isoforms of TRPP channels (polycystin-2, polycystin-L, and polycystin-2L2) were exp

212 enes PKD1 or PKD2 (encoding polycystin-1 and polycystin-2, respectively) and ARPKD caused by PKHD1 (e

213 the transmembrane proteins polycystin-1 and polycystin-2, respectively, cause autosomal dominant pol

214 or PKD2 which encodes polycystin-1 (PC1) and polycystin-2, respectively.

215 ARL13B is required for the ciliary entry of polycystin-2, the protein mutated in autosomal dominant

216 PKD2 (polycystin-2, TRPP1) channels are expressed in a wide va

217 PKD2 (polycystin-2, TRPP1), a TRP polycystin channel, is expre

218 Studies suggest that polycystin-1 and polycystin-2, which are encoded by PKD1 and PKD2, respec

219 whose mutation impairs ciliary motility, and polycystin-2, whose ablation is associated with hydrocep

220 d pro-angiogenic effects of IGF1 and VEGF in polycystin-2-defective mice.

221 Conditional polycystin-2-knockout (Pkd2KO) mice were used for in viv

222 dney disease gene products, polycystin-1 and polycystin-2.

223 1, fibrocystin (in their cleaved forms), and polycystin-2.

224 egulates the calcium-permeant cation channel polycystin-2.

225 PP channels (polycystin-2, polycystin-L, and polycystin-2L2) were expressed in adult mouse lacrimal g

226 as to alter proliferation signals linked to polycystin activity.

227 vel disease-associated protein families: The polycystins (ADPKD); fibrocystins (ARPKD); and meckelin.

228 a cystogenic activator that is inhibited by polycystins and an independent but relatively minor cyst

229 al a pathway connecting TNF-alpha signaling, polycystins and cystogenesis, the activation of which ma

230 with the signal transduction pathways of the polycystins and may control the targeting of these cilia

231 Thus, we show that polycystins and TAZ integrate at the molecular level to

232 ressed cyst growth following inactivation of polycystins and that the severity of cystic disease was

233 Here, we show that ciliary function (polycystins) and structure (polaris) are required for pr

234 The cellular mechanisms of polycystin- and cilia-dependent cyst progression in ADPK

235 This molecule stimulated polycystin- and TAZ-dependent osteoblastogenesis and inh

236 Polycystins appear to play key roles during development,

237 Mutations in polycystins are a cause of polycystic liver disease.

238 Polycystins are a family of eight-transmembrane proteins

239 Polycystins are expressed in the primary cilium, and dis

240 The polycystins are thought to form a receptor-calcium chann

241 esults from a reduction of ciliary levels of polycystins, Arl13b, and Arl13b-dependent lipidated carg

242 Mutations in the polycystins cause autosomal dominant polycystic kidney d

243 PC1-L1 and PC2, which may form a heteromeric polycystin channel complex on primary cilia.

244 PKD2 (polycystin-2, TRPP1), a TRP polycystin channel, is expressed in endothelial cells (E

245 Besides polycystin channels voltage gated channels like HCN4 and

246 Using both reconstituted and ciliary polycystin channels, we further show that a soluble frag

247 EV biology and the relationship between the polycystins, cilia, and EVs is lacking.

248 ome-like vesicles (ELVs) where they form the polycystin complex (PCC).

249 of genetic mechanisms, the structure of the polycystin complex and the roles of G-protein signalling

250 egments, in the assembly and function of the polycystin complex are largely unknown.

251 onal understanding of the putative PC-1/PC-2 polycystin complex is lacking due to technical hurdles i

252 lar localization and channel activity of the polycystin complex through its interaction with the O2-s

253 geting mechanism, whereby Rabep1 couples the polycystin complex to a GGA1/Arl3-based ciliary traffick

254 erstood how fluid flow activates the ciliary polycystin complex.

255 Polycystin complexes, or TRPP-PKD complexes, made of tra

256 bly, surface expression, and function of the polycystin complexes.

257 ar loops in the assembly and function of the polycystin complexes.

258 Recent findings suggest that polycystins could function in the maintenance of extrace

259 Brefeldin A treatment after the onset of polycystin deficiency phenotypes reversed the curved axi

260 ators of cardiac hypertrophy, are targets of polycystin-dependent fluid stress sensing in renal epith

261 sh the existence of a new pathway defined by polycystin-dependent inhibition and cilia-dependent acti

262 lease channels, transient receptor potential polycystin family (TRPP) channels.

263 Polycystins function as calcium ion channels, but their

264 tein Tulp3 determines ciliary trafficking of polycystins in kidney collecting duct cells without affe

265 The functional role of the polycystins in mechanosensation remains largely unknown.

266 Kidney cysts occur following inactivation of polycystins in otherwise intact cilia or following compl

267 These data suggest a novel role for the polycystins in sensing and responding to cellular O2 lev

268 Polycystin knockouts have severe cystogenesis compared t

269 disease 2-like 1 (Pkd2l1 or Pkdl), encoding polycystin-L (PCL), a non-selective cation channel, incr

270 ing isoforms of TRPP channels (polycystin-2, polycystin-L, and polycystin-2L2) were expressed in adul

271 LOXHD1 consists entirely of PLAT (polycystin/lipoxygenase/alpha-toxin) domains and is expr

272 Polycystins localize to the primary cilium, an organelle

273 shed and release ECVs containing GFP-tagged polycystins LOV-1 and PKD-2.

274 sponse from mating-deficient pkd-2 and lov-1 polycystin mutant males.

275 Polycystin (PC)1 and PC2 are membrane proteins implicate

276 The PKD1 or PKD2 genes encode polycystins (PC) 1 and 2, which are associated with poly

277 or cilia (acetylated tubulin, gamma-tubulin, polycystin [PC] 1, PC2, and KIF3A), fibroblasts (vimenti

278 logical experiments to determine whether the polycystins PC1 and PC2 (encoded by Pkd1 and Pkd2) and t

279 Mutations in polycystins (PC1 or PC2/TRPP2) cause progressive polycys

280 tations in Pkd1/Pkd2 and Pkhd1, which encode polycystins (PCs) and fibrocystin/polyductin (FPC).

281 The mammalian polycystins (PCs) localize to cilia, as well as to urina

282 localization of the kinesin-3 KLP-6 and the polycystin PKD-2 in male-specific sensory neurons in C.

283 In contrast to the hypothesis that polycystin (PKD) channels initiate changes in ciliary ca

284 However, how mutated polycystins predispose patients with ADPKD to cardiac pa

285 The polycystin proteins (PC and PKD), identified in linkage

286 The function of polycystin proteins and the pathogenesis of autosomal do

287 ngth of time between the initial loss of the polycystin proteins and the subsequent involution of cil

288 Mutations in the polycystin proteins, PC-1 and PC-2, result in autosomal

289 on, maturation, or localization of the ADPKD polycystin proteins, with no interaction detected betwee

290 This review discusses recent topics in polycystin research, with a focus on the role of polycys

291 d new pathways controlling EV biogenesis and polycystin signaling and also identified EV cargo, which

292 tivated protein kinase (MAPK) pmk-1 acted in polycystin-signaling pathways controlling male mating be

293 e we demonstrate that TRPP2, a member of the polycystin subfamily of TRP channels encoded by the PKD2

294 ipocyte differentiation, indicating that the polycystins/TAZ complex may be a potential therapeutic t

295 The molecular pathways linking polycystins to cyst development in ADPKD are still uncle

296 Failure of mutant polycystins to localize to cilia abolishes flow-stimulat

297 made of transient receptor potential channel polycystin (TRPP) and polycystic kidney disease (PKD) pr

298 LOV-1 and PKD-2 transient receptor potential polycystin (TRPP) complex localizes to ciliated endings

299 se (ADPKD), a disease caused by mutations in polycystins, which are proteins that regulate signaling,

300 ses by combining conditional inactivation of polycystins with concomitant ablation of cilia in develo

301 These data indicate that FPC and the polycystins work independently, with separate disease-ca