ライフサイエンスコーパス: polycystin

1 egorize the effects of missense mutations in polycystins.

2 Polycystin 1 (PC1), the product of the PKD1 gene, has be

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

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

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

6 Polycystin 1 and polycystin 2 are large transmembrane pr

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

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

9 Coexpression of a cytoplasmic fragment of polycystin 1 blocks the PC2-TAZ interaction and prevents

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

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

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

13 hydrate or when ciliary-associated proteins polycystin-1 (a mechanoreceptor), polycystin-2 (a Ca2+ c

14 eceptor potential polycystin (TRPP) channels polycystin-1 (PC-1) and polycystin-2 (PC-2) act as a mec

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

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

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

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

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

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

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

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

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

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

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

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

27 ory cilia of Caenorhabditis elegans neurons, polycystin-1 (PC1) and transient receptor polycystin-2 c

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

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

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

31 Polycystin-1 (PC1) has an essential function in renal tu

32 The mechanisms of action of polycystin-1 (PC1) have been difficult to dissect becaus

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

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

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

38 Polycystin-1 (PC1) may play an important role in skeleto

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 tion of either PC2 or its regulatory protein polycystin-1 (PC1) results in autosomal dominant polycys

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

44 Mutations in polycystin-1 (PC1) underlie most cases of ADPKD, but the

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

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

47 eoblast/osteocyte expression and function of polycystin-1 (PC1), a transmembrane protein that is a co

48 suggests that fibrocystin/polyductin (FPC), polycystin-1 (PC1), and polycystin-2 (PC2) are all local

49 sease (ADPKD), which results from defects in polycystin-1 (PC1), but the function of PC1 remains poor

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

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

52 Polycystin-1 (PC1), the PKD1 gene product, plays a criti

53 Polycystin-1 (PC1), the product of the PKD1 gene mutated

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

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

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

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

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

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

60 n craniofacial sutures of mice deficient for polycystin-1 (Pkd1).

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

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

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

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

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

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

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

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

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

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

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

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

73 ns in either PKD1 or PKD2, genes that encode polycystin-1 and polycystin-2, respectively.

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

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

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

81 Pkdrej, a member of the polycystin-1 gene family, is expressed only in the male

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 We investigated whether polycystin-1 is a bone mechanosensor.

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

87 Our data suggest that polycystin-1 is required for proliferation of subpopulat

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

89 Polycystin-1 localized in the basal body of Tg737(orpk/o

90 ization and function of the mechanosensitive polycystin-1 molecule.

91 PKD1 or with abnormal ciliary expression of polycystin-1 or -2 were not responsive to fluid shear st

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

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

94 ll) or Tg737(orpk/orpk) mutation encoded for polycystin-1 or polaris, respectively, are unable to tra

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

96 Mutations in PKD1 (the gene encoding polycystin-1) are the principal cause of this disease.

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

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

99 8 interacted with polycystin-2, but not with polycystin-1, and that the jck mutation did not affect t

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

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

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 cyte cilia are sensory organelles containing polycystin-1, polycystin-2, and adenylyl cyclase isoform

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

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

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

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

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

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

111 stresses through proteolytic modification of polycystin-1.

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

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

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

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

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

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

118 The calcium-permeable cation channel protein polycystin 2 (PC2) is overexpressed in kidneys of TAZ-/-

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

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

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

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

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

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

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

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

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

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

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

130 lization of the transient receptor potential polycystin 2 channel (TRPP2/PKD-2) is evolutionarily con

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

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

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

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

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

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

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

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

139 l dominant polycystic kidney disease protein polycystin 2.

140 a(2+)-activated non-specific cation channel, Polycystin 2.

141 rectly and coordinate the ciliary removal of polycystin 2.

142 d proteins polycystin-1 (a mechanoreceptor), polycystin-2 (a Ca2+ channel), and the Ca2+-inhibitable

143 stin (TRPP) channels polycystin-1 (PC-1) and polycystin-2 (PC-2) act as a mechanosensitive channel, w

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 in/polyductin (FPC), polycystin-1 (PC1), and polycystin-2 (PC2) are all localized at the plasma membr

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

148 Mutations in polycystin-2 (PC2) cause autosomal dominant polycystic k

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

150 at PC1 co-localizes with the calcium channel polycystin-2 (PC2) in primary cilia of MC3T3-E1 osteobla

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

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

153 In polycystic kidney disease (PKD), polycystin-2 (PC2) is frequently mutated or truncated in

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

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

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

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

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

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

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

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

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

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

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

165 sensation opens the calcium (Ca(2+)) channel polycystin-2 (PC2), resulting in a calcium flux-mediated

166 and co-localizes with the Pkd2 gene product polycystin-2 (PC2), suggesting that these two proteins m

167 Polycystin-2 (PC2), the gene product of one of two genes

168 Polycystin-2 (PC2), the PKD2 protein, is a non-selective

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

170 smembrane protein that is a component of the polycystin-2 (PC2)-ciliary mechano-sensor complex in ren

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

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

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

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

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

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

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

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

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

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

181 Polycystin-2 also was expressed in muscle cells and in a

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

183 Immunostaining with anti-zebrafish Polycystin-2 antibody revealed protein expression in mot

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

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

186 s, polycystin-1 (PC1) and transient receptor polycystin-2 channel (TRPP2 or PC2), function together a

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

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

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

190 In addition, cells not expressing polycystin-2 exhibit significantly more branching morpho

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

192 Polycystin-2 functions as a cation-permeable transient r

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

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

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

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

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

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

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

200 Polycystin-2 is therefore likely to play multiple roles

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

202 n-2-expressing counterparts, suggesting that polycystin-2 may also play an important role in the regu

203 binding sites in the cytoplasmic tail caused Polycystin-2 mislocalization to the apical cell surface.

204 Disruption of Polycystin-2 mRNA expression resulted in pronephric kidn

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

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

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

208 ock cilia assembly but reduces the amount of polycystin-2 that is localized to the cilia.

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

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

211 ans with ADPKD, disrupts the localization of polycystin-2 to the plasma membrane and primary cilia th

212 s, whereas in the caudal pronephric segment, Polycystin-2 was concentrated in subapical cytoplasmic v

213 t specific; in the proximal nephron segment, Polycystin-2 was localized to basolateral cell membranes

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

215 sensory organelles containing polycystin-1, polycystin-2, and adenylyl cyclase isoform 6 through whi

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

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

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

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

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

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

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

223 ments demonstrated that Nek8 interacted with polycystin-2, but not with polycystin-1, and that the jc

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

225 or PKD2, genes that encode polycystin-1 and polycystin-2, respectively.

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

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

228 ther exploration of the in vivo functions of Polycystin-2, this study examined its expression and fun

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

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

231 e induces cellular calcium release through a polycystin-2-dependent pathway, arrests Pkd1(-/-) cell g

232 owth factor-stimulated conditions than their polycystin-2-expressing counterparts, suggesting that po

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

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

235 1, fibrocystin (in their cleaved forms), and polycystin-2.

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

237 y transduction, the mechanisms that regulate polycystin activity and localization, or ciliary membran

238 as to alter proliferation signals linked to polycystin activity.

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

240 ia are accompanied by enhanced expression of polycystins along the cilia.

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

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

243 les display normal ciliary expression of the polycystins and respond to fluid-flow shear stress with

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

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

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

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

248 Polycystins appear to play key roles during development,

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

250 Polycystins are a family of eight-transmembrane proteins

251 Cellular pathways that involve the polycystins are being mapped and involve the primary cil

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

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

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

255 The overall function of the primary cilium-polycystin complex may be to sense and transduce environ

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

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

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

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

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

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

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

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

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

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

266 low shear stress can be used as a readout of polycystin function and that loss of mechanosensation in

267 Polycystins function as calcium ion channels, but their

268 otein families, the most prominent being the polycystin gene family, whose products are found on the

269 IMA-related (never in mitosis A) kinase, and polycystins in jck cilia is shown for the first time.

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

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

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

273 Despite the importance of the polycystins in sensory transduction, the mechanisms that

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

291 These findings suggest that FPC and polycystins share, at least in part, a common mechanotra

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

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

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

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

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

297 dney cells, the transient receptor potential polycystin (TRPP) channels polycystin-1 (PC-1) and polyc

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