ライフサイエンスコーパス: PC2

1 genes, encoding polycystins 1 and 2 (PC1 and PC2).

2 y of prohormone convertases 1 and 2 (PC1 and PC2).

3 lysine and tyrosine on the negative side of PC2.

4 atch the most important variable for biology PC2.

5 ignals that are rescued by overexpression of PC2.

6 e surface expression and function of PC1 and PC2.

7 aved PC1 required an intact interaction with PC2.

8 II)-PC2, Cys-As-(GS)2, and GS-As(III)-desgly-PC2.

9 or (PC1-PC2) to 0.56 (95% CI: 0.48-0.63) for PC2.

10 ereby promoting the abnormal accumulation of PC2.

11 biquitination and proteasomal degradation of PC2.

12 peptides despite increased release of active PC2.

13 d the prohormone convertases (PCs) PC1/3 and PC2.

14 d from PC12 cells stably expressing PC1/3 or PC2.

15 ve form of Ubc9 (SUMO approximately Ubc9) by Pc2.

16 ires interaction of both CtBP1 and Akt1 with Pc2.

17 ion of CRH post-translationally by affecting PC2.

18 F38), a section with the highest homology to PC2.

19 iscrimination of the counterfeit whiskies in PC2.

20 in a cleaved form and may be complexed with PC2.

21 effect of decreased levels of polycystin 2 (PC2), a calcium channel that interacts with the ryanodin

22 Polycystin-2 (PC2), a ciliary calcium channel that is mutated in human

23 phosphorylates, and reduces the activity of PC2, a Ca(2+)-permeable nonselective cation channel and,

24 mote both Arkadia's colocalization with CBX4/Pc2, a component of Polycomb bodies, and the activation

25 study, a yeast two-hybrid screen identified PC2, a component of the Mediator complex, as a PLAGL2-bi

26 Caenorhabditis elegans and mammals, PC1 and PC2 act in the same genetic pathway, act in a sensory ca

27 Our findings link the DNA damage-induced Pc2 activation to the p53 transcriptional co-activation

28 ate peptide production through regulation of PC2 activity remains unclear.

29 lucagon cleavage has a greater dependence on PC2 activity than other precursors and moreover that 7B2

30 were able to stimulate both 87 kDa PC1/3 and PC2 activity, behavior related to the presence of aryl g

31 al element of Ca(2+)-sensitive regulation of PC2 activity.

32 age at the GPS/GAIN site and determined that PC2 acts as an essential chaperone for PC1 maturation an

33 roduction of active prohormone convertase 2 (PC2), an enzyme involved in the synthesis of peptide hor

34 Co-expression of Pc2 and Akt1 results in both phosphorylation and ubiquit

35 , understanding the functional regulation of PC2 and its interaction with other proteins under both p

36 f variance (ANOVA) was performed for PC1 and PC2 and means were statistically evaluated.

37 licing of a common precursor, proglucagon by PC2 and PC1, respectively.

38 d-type controls or other PC KO mice, such as PC2 and PC7 null mice.

39 Collectively, these findings identify PC2 and PDE4C as unique components of an AKAP complex in

40 The genetic correlation of PC1-PC2 and SNR was -0.67 showing that the 2 traits share va

41 that one compound was found to both inhibit PC2 and stimulate PC1/3.

42 We found that HDAC6 binds to PC2 and that expression of full-length PC1 accelerates t

43 apical and ciliary PC1 localization requires PC2 and that this delivery is sensitive to PC2 truncatio

44 We speculate that PC2 and the Ca(2+)-dependent transient receptor potentia

45 The molecular mechanism linking mutations in PC2 and the pathogenesis of ADPKD is not well understood

46 e data support tetrameric models of both the PC2 and TRPC1 channels, where the overall conductance of

47 ored structural and functional properties of PC2 and whether the conductance substates represent mono

48 localization of the ADPKD proteins (PC1 and PC2), and reduced mature PC1 was seen in GANAB(+/-) cell

49 centrations found to be inhibitory to PC1/3, PC2, and CPE are well within the physiological range fou

50 elaborated primary cilia and expressed PC1, PC2, and FPC at similar levels, and PKD and control iPS

51 PC1 has been shown to form a complex with PC2, and the severity of PKD1-mediated disease is associ

52 Mutations in PC2 are associated with polycystic liver diseases.

53 The prohormone convertases PC1/3 and PC2 are eukaryotic serine proteases involved in the prot

54 These properties of PC2 are lost in autosomal dominant polycystic kidney dis

55 Polycystin (PC)1 and PC2 are membrane proteins implicated in autosomal domina

56 Here, we show that both CtBP1 and Pc2 are phosphorylated by the kinase Akt1, which is acti

57 ling the subcellular localization of PC1 and PC2 are poorly understood.

58 PC1 and PC2 are secreted on urinary exosome-like vesicles (ELVs)

59 Together, the data identify PC2 as a novel PLAGL2-binding protein and important medi

60 We identified an E3 ligase, Pc2, as a SUMO-binding protein with two functionally dis

61 isms that control the trafficking of PC1 and PC2, as well as their broader physiological roles, are p

62 d from these cells expressed lower levels of PC2 at the cilium.

63 hat the interaction of Nek1 and TAZ maintain PC2 at the level needed for proper ciliogenesis.

64 Polycystin-2 (PC2) belongs to the transient receptor potential (TRP) f

65 ween the first two principle components (PC1-PC2) best represented ARHI.

66 s of PLAGL2, the region that is required for PC2 binding and contains the PLAGL2 activation domain.

67 cal, and cellular assays, we determined that PC2 binds two isoforms of the retromer-associated protei

68 an be corrected by reexpression of wild-type PC2 but not by a mutant lacking calcium channel activity

69 compound predicted to bind to PC2 in the PC1:PC2 C-terminal tail region with helix:helix interaction.

70 PC1 and PC2 can interact through their C-terminal tails, but rem

71 Mutations in polycystin 1 and 2 (PC1 and PC2) cause the common genetic kidney disorder autosomal

72 Pc2 (Cbx4) is a member of the chromobox family of polyco

73 nd sumoylation is regulated by the E3 ligase Pc2/CBX4.

74 is responsible for the cooperative nature of PC2 channel activation and inhibition.

75 es the concentration of calcium required for PC2 channel activity and cellular function.

76 sm of regulation of the Ca(2+) dependence of PC2 channel activity by PC2-EF.

77 of PC2 on PC1 localization is independent of PC2 channel activity, as tested using channel-inhibiting

78 The PC2 Cterm is also involved in the PC2 channel assembly and hetero-oligomerization with oth

79 l of human PC2 (HPC2 Cterm) is important for PC2 channel assembly and regulation.

80 nding the Ca(2+)-dependent regulation of the PC2 channel by its cytosolic C-terminal domain.

81 work we assessed the regulation by Ca(2+) of PC2 channel function from a preparation of apical membra

82 To confirm the oligomeric contributions to PC2 channel function, heteromeric PC2/TRPC1 channel comp

83 motif is truly a calcium sensor controlling PC2 channel function, we altered the number of calcium b

84 nding EF-hand domain, the molecular basis of PC2 channel gating by Ca(2+) remains unknown.

85 The relevant PKA site for PC2 channel regulation centers on a single residue serin

86 al for the calcium-dependent activity of the PC2 channel.

87 Our results support a model where PC2 channels are gated by discrete conformational change

88 Mutant PC2 channels unable to bind Ca(2+) via the EF-hand are i

89 ted Basmati from the other two cultivars and PC2 completely separated Jasmine from Jasmati cultivars.

90 h PC1 accelerates the transport of the HDAC6-PC2 complex toward aggresomes, whereas expression of the

91 These data indicate that specific ABP-PC2 complexes would confer distinct Ca(2+)-sensitive pro

92 Cystic cholangiocytes were isolated from PC2 conditional-KO (knockout) mice (Pkd2(flox/-) :pCxCre

93 ylation/demethylation of Polycomb 2 protein (Pc2) controls relocation of growth-control genes between

94 involved in the endosomal sorting of PC1 and PC2 could lead to new therapeutic approaches in ADPKD.

95 definition of the domain topology within the PC2 Cterm and the functional role of each domain.

96 The PC2 Cterm can form an oligomer, mediated by the coiled-c

97 Although PC2 Cterm has been extensively studied for its relations

98 Different functional domains of the PC2 Cterm have been studied using structural approaches.

99 The PC2 Cterm is also involved in the PC2 channel assembly a

100 t the molecular properties of the domains of PC2 Cterm to distinct aspects of PC2 functions and regul

101 ium binding to the C-terminal domain of PC2 (PC2 Cterm).

102 Within the PC2 Cterm, there is a calcium-binding EF-hand domain, cr

103 Low pH inhibited the PC2 currents in PC2 homomeric complexes, but failed to a

104 C2 homomeric complexes, but failed to affect PC2 currents in PC2/TRPC1 heteromeric complexes.

105 hree newly identified complexes: Cys-As(III)-PC2, Cys-As-(GS)2, and GS-As(III)-desgly-PC2.

106 In polycystin-2 (PC2)-defective mice, cyclic adenosine monophosphate (cAM

107 In PC2-defective cells, sorafenib inhibits B-Raf but parado

108 In PC2-defective cells, the interaction of STIM-1 with Orai

109 esults showed that, compared to WT cells, in PC2-defective cholangiocytes (Pkd2KO), cytoplasmic and E

110 PC2-defective cholangiocytes show increased production o

111 roduction and inappropriate ERK signaling in PC2-defective cholangiocytes.

112 In PC2-defective mice, cyclic 3',5'-adenosine monophosphate

113 idney cancers, inhibits liver cyst growth in PC2-defective mice, we treated PC2 (i.e., Pkd2(flox/-) :

114 PLD, because of PC2 deficiency, represents the first example of human di

115 In these conditions, PC2 degradation was instead inhibited by interfering wit

116 uitin-like proteins that promote proteosomal PC2 degradation, was increased.

117 to selectively regulate synthesis of certain PC2-dependent peptides.

118 sting that NEK8 may play a role in mediating PC2-dependent signaling.

119 itro and in vivo and increased Wnt-activated PC2-dependent whole-cell currents.

120 els between antioxidant capacity and PC1 and PC2 displayed strong linear correlations for NF fraction

121 the proteasome or the autophagy pathway, and PC2 down-regulation is associated with activation of ERK

122 We investigated the mechanisms connecting PC2 dysfunction to altered Ca(2+) and cAMP production an

123 amage stimulates hnRNP K sumoylation through Pc2 E3 activity, and this modification is required for p

124 ease in the radius of gyration (R(g)) of the PC2 EF-hand by small angle x-ray scattering and signific

125 We propose that the PC2 EF-hand is a Ca(2+) sensor required for channel gati

126 2+)-bound states, consistent with a role for PC2-EF as a Ca(2+)-sensitive regulator.

127 We found that PC2-EF binds Ca(2+) at a single site and undergoes Ca(2+

128 Human PC2-EF contains a divergent non-Ca(2+)-binding helix-loo

129 We propose that Ca(2+)-sensing by PC2-EF is responsible for the cooperative nature of PC2

130 three functional regions: an EF-hand domain (PC2-EF, 720-797), a flexible linker (798-827), and an ol

131 Ca(2+) dependence of PC2 channel activity by PC2-EF.

132 e NMR structure and dynamics of Ca(2+)-bound PC2-EF.

133 to determine whether the polycystins PC1 and PC2 (encoded by Pkd1 and Pkd2) and the transcriptional c

134 PC2 explained 21.7% and captured horizontal maxillomandi

135 the proteasome inhibitor bortezomib restored PC2 expression and significantly reduced the ductular re

136 d VEGF secretion; treatments able to restore PC2 expression and to reduce ductular reaction and fibro

137 sion in vivo and in vitro by down-regulating PC2 expression in a dose-dependent manner.

138 ia a C-terminal coiled-coil domain regulates PC2 expression in vivo and in vitro by down-regulating P

139 In response to biliary damage, PC2 expression is modulated posttranslationally by the p

140 In sum, our work shows that PC2 expression is required for the movement of PC1 to th

141 terminal truncation mutant increased ciliary PC2 expression levels in mouse kidney cells.

142 coiled-coil domain, failed to down-regulate PC2 expression, suggesting that PC1-PC2 interaction is n

143 Here, we demonstrated that PC1 and PC2 first interact in the ER before PC1 cleavage at the

144 at targets the ciliary protein polycystin 2 (PC2) for degradation, but whether Nek and TAZ contribute

145 genes, polycystin-1 (PC1) and polycystin-2 (PC2), form a plasma membrane receptor-ion channel comple

146 We recently demonstrated that PC2 from human syncytiotrophoblast (PC2hst) but not the

147 accessible through the channel that controls PC2 function in human syncytiotrophoblast of term placen

148 or responsible for the calcium dependence of PC2 function.

149 domains of PC2 Cterm to distinct aspects of PC2 functions and regulation.

150 PC2 functions as a Ca(2+)-activated Ca(2+) channel of th

151 Normally, PC2 functions as a calcium-permeable channel whose activ

152 hat it is crucial for many of the documented Pc2 functions, which converge on determining its E3 liga

153 e (PC) family comprises nine members: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9

154 ted PC2 protein expression without affecting PC2 gene expression.

155 oendocrine-specific Prohormone Convertase 2 (PC2) gene, and showed that amon is required during embry

156 stimulus-secretion pathway including PC1/3, PC2, GLUT-1, glucokinase, and K-ATP channel complex (Sur

157 Although the C-terminal cytoplasmic tail of PC2 has been shown to contain a Ca(2+)-binding EF-hand d

158 spiropyran-decorated covalent organic cage (PC2) has been designed, employing dynamic imine chemistr

159 om a canonical EF-hand found in invertebrate PC2 homologs.

160 Low pH inhibited the PC2 currents in PC2 homomeric complexes, but failed to affect PC2 curren

161 and protruding height when compared with the PC2 homomers.

162 The C-terminal cytoplasmic tail of human PC2 (HPC2 Cterm) is important for PC2 channel assembly a

163 dent calcium channel, and mutations to human PC2 (hPC2) are associated with polycystic kidney disease

164 yst growth in PC2-defective mice, we treated PC2 (i.e., Pkd2(flox/-) :pCxCreER(TM) [Pkd2cKO]) mice wi

165 (SNX3), including a novel isoform that binds PC2 in a direct manner.

166 inhibitor MG-132 restored the expression of PC2 in cells treated with cytokines but not in cells tre

167 osed cAMP stimulated hyperphosphorylation of PC2 in the absence of functional PC1 could contribute to

168 ls with reduced levels of functional PC1 and PC2 in the kidney exhibited severe, rapidly progressive

169 e identified a compound predicted to bind to PC2 in the PC1:PC2 C-terminal tail region with helix:hel

170 the surface expression of endogenous PC1 and PC2 in vitro and in vivo and increased Wnt-activated PC2

171 Loss of polycystin-2 (PC2) in mice (Pkd2(-/-)) results in total body edema, fo

172 fects in polycystin-1 (PC1) or polycystin-2 (PC2), in which tubular epithelia form fluid-filled cysts

173 Our results suggest that PC2 increases both PC1 GPS cleavage and PC1's appearance

174 Deletion of PC2 increases cAMP levels, which can be corrected by ree

175 PC1&PC2 independently predicted 90-day mortality (ORs 2.6, 9

176 In support of kinetic data suggesting that PC2 inhibition probably occurs via an allosteric mechani

177 The best PC2 inhibitor effectively inhibited glucagon synthesis,

178 ising PC1/3 competitive inhibitors and three PC2 inhibitors that exhibited various inhibition mechani

179 In contrast in a pc2 insertion mutant, which has strongly reduced plastoc

180 rmed as polycystin-1 (PC1) and polycystin-2 (PC2), interact via their C-termini to form a receptor-io

181 regulate PC2 expression, suggesting that PC1-PC2 interaction is necessary for PC2 regulation.

182 king and expression require GPS cleavage and PC2 interaction, respectively, and provide a framework f

183 Previously we demonstrated that PC2 interacts with the inositol 1,4,5-trisphosphate rece

184 PC2 is a member of the trp family of cation channels and

185 PC2 is a non-selective cation channel, with multiple sub

186 nction demonstrate that Ca(2+) regulation of PC2 is actually mediated by direct interaction(s) with s

187 nificance of the SIM2-dependent functions of Pc2 is demonstrated in the control of the precise expres

188 Polycystin-2 (PC2) is a Ca(2+)-permeable transient receptor potential

189 Polycystin 2 (PC2) is a calcium-dependent calcium channel, and mutatio

190 Polycystin-2 (PC2) is a TRP-type, Ca(2+)-permeable non-selective catio

191 mains with gelsolin, significantly increased PC2(iv) channel function both in the presence and absenc

192 The distinct effect(s) of the ABPs on PC2(iv) channel function demonstrate that Ca(2+) regulat

193 insensitive actin-binding proteins (ABPs) on PC2(iv) channel function in a lipid bilayer system.

194 tin-bundling protein alpha-actinin increased PC2(iv) channel function in the presence of cis Ca(2+),

195 ha-actinin had a strong inhibitory effect on PC2(iv) channel function in the presence, but no effect

196 Gelsolin stimulated PC2(iv) channel function in the presence, but not the ab

197 st) but not the in vitro translated protein (PC2(iv)), functionally responds to changes in intracellu

198 , chromatin immunoprecipitation analysis and PC2 knockdown studies confirmed that endogenous PC2 prot

199 Mutations in polycystin-2 (PC2) lead to autosomal dominant polycystic kidney diseas

200 The molecular mechanisms by which loss of PC2 leads to these phenotypes remain unknown.

201 We hypothesized that PC2 levels are modulated during biliary damage/repair, r

202 We propose that PC2 levels in the heart may directly contribute to cardi

203 Our results showed that decreased PC2 levels shifted the betaAR pathway balance and change

204 Furthermore, elevated Sirt1 increased PC2 levels, which in turn increased the production of ac

205 Although PC2 may contribute to Ca(2+) transport in human term pla

206 ata indicate that the cAMP pathway regulates PC2-mediated cation transport in the hST.

207 tively inhibited glucagon synthesis, a known PC2-mediated process, in a pancreatic cell line; no cyto

208 We hypothesize that heterozygous PC2 mice (Pkd2(+/-)) undergo cardiac remodeling as a res

209 This work suggests that Pc2 might coordinate multiple enzymatic activities to re

210 Here we describe that PC1 and PC2 must interact and form a complex to reach the trans-

211 PC2 mutations are responsible for approximately 15% of a

212 (Ca(2+)) signaling is a known consequence of PC2 mutations.

213 activity, as tested using channel-inhibiting PC2 mutations.

214 However, similar to cells lacking PC2, NEK8-depleted inner medullary collecting duct cells

215 Nek8-deficient embryos and cells did express PC2 normally, which localized properly to the cilia.

216 The effect of PC2 on PC1 localization is independent of PC2 channel ac

217 r-reporter studies reveal that the effect of PC2 on PLAGL2 target promoter activity was conferred via

218 In 3D systems, knockdown of either PC2 or InsP3R leads to cyst formation, but knockdown of

219 Polycystin-2 (PC2 or TRPPC2), a member of the transient receptor poten

220 either the mechanical properties of the LC (PC2) or of the neural tissue (PC4), rotation of the peri

221 We hypothesize that Ca(2+) signaling through PC2, or other intracellular Ca(2+) channels such as the

222 gene was found to be associated with hearing PC2 (P = 3.7x10(-8)) and further supported by whole-geno

223 calcium binding to the C-terminal domain of PC2 (PC2 Cterm).

224 ytiotrophoblast (hST), containing endogenous PC2 (PC2hst), and in vitro translated channel protein (P

225 ingly, the reconstituted in vitro translated PC2 (PC2iv) was completely insensitive to Ca(2+) regulat

226 f plants exposed to Cd(2+) showed a similar (PC2, PC4) or lower (PC3) concentration in snrk2.4 mutant

227 E4, and PC5/6, with similar potency, whereas PC2, PC7, and trypsin-like serine proteases are poorly a

228 However, the role of PC2 phosphorylation in channel function is still poorly

229 In the presence of Pc2, phosphorylation of CtBP1 is increased, and this req

230 (pkd1), primarily a signaling molecule, and PC2 (pkd2), a Ca(2+) channel.

231 ng polycystin-1 (PC1, PKD1) or polycystin-2 (PC2, PKD2) cause ADPKD, and PKD1 mutations are associate

232 These data suggest that PC2 plays a key role in SOCE activation and inhibits the

233 The PC3 versus PC2 plot has showed significant differences between nonm

234 In Pkd2-/- mice, complete loss of PC2 prevented PC1 maturation.

235 Pc2 promotes CtBP1 phosphorylation by recruiting Akt1 an

236 ditionally, binding of NEAT2 to unmethylated Pc2 promotes E2F1 SUMOylation, leading to activation of

237 knockdown studies confirmed that endogenous PC2 protein associated with the NCF2 promoter in MM1 cel

238 e results suggest that PC1 regulates ciliary PC2 protein expression levels and support the use of PKD

239 PKD iPS-derived hepatoblasts rescued ciliary PC2 protein expression levels, and overexpression of PC1

240 or type 2 phosphorylation and down-regulated PC2 protein expression without affecting PC2 gene expres

241 PC2 protein expression, but not its gene expression, was

242 n the assembly and hetero-interaction of the PC2 protein.

243 Notably, NEK8 and polycystin-2 (PC2) proteins interact, and we found that Nek8(-/-) and

244 In Pkd2 heterozygotes, the 50% PC2 reduction resulted in a nonequimolar reduction (20%-

245 Our results indicate that PC2 regulates PC1 maturation; therefore, mature PC1 leve

246 The molecular mechanisms associated with PC2 regulation by Ca(2+) remain ill-defined.

247 elationship with ADPKD and its importance in PC2 regulation, there are misunderstandings with respect

248 ng that PC1-PC2 interaction is necessary for PC2 regulation.

249 encode polycystin-1 (PC1) and polycystin-2 (PC2), respectively, cause autosomal dominant PKD (ADPKD)

250 ncoding polycystin-1 (PC1) and polycystin-2 (PC2), respectively, lead to autosomal dominant polycysti

251 h encode polycystin-1 (PC1) or polycystin-2 (PC2), respectively.

252 s this localization effect is independent of PC2's channel activity or PC1 binding ability but involv

253 analysis that included both populations, the PC2 score, reflecting exposure to DiNP, was negatively a

254 thway and kinase mediated phosphorylation of PC2 seem to be relevant to PC2 trafficking and its inter

255 analysis of spontaneous channel currents of PC2 showed that four intrinsic, non-stochastic subconduc

256 , the respective phosphirene (Ar[(t)Bu]N)3VN-PC2(SiMe3)2 (7) or phosphirane (Ar[(t)Bu]N)3VN-P(C8H16)

257 ), was greatly diminished in the presence of PC2 siRNA.

258 We also employed the sea urchin PC2 (SUPC2) as a model for biophysical and structural ch

259 ill assist in understanding how mutations in PC2 that confer altered Ca(2+) signaling lead to ADPKD c

260 thway suggesting that when PC1 is expressed, PC2 that is not bound to PC1 is directed to aggresomes a

261 mutation in the gene encoding polycystin-2 (PC2) that prevented this protein from properly trafficki

262 Polycystin-1 (PC1) and -2 (PC2), the two ADPKD gene products, are large transmembra

263 In contrast to the human PC2, the SUPC2 Ccore contains two cooperative Ca(2+)-bin

264 covery cohort, and the ratio of PC1/TMEM2 or PC2/TMEM2 could be used to distinguish individuals with

265 st measuring the urine exosomal PC1/TMEM2 or PC2/TMEM2 ratio may have utility in diagnosis and monito

266 idney disease, emphasizing the importance of PC2 to kidney cell function.

267 s and moreover that 7B2-dependent routing of PC2 to secretory granules is cell line-specific.

268 ce of binding of methylated and unmethylated Pc2 to the ncRNAs TUG1 and MALAT1/NEAT2, located in PcGs

269 anged from 0.70 (95% CI: 0.63-0.76) for (PC1-PC2) to 0.56 (95% CI: 0.48-0.63) for PC2.

270 hosphorylation of PC2 seem to be relevant to PC2 trafficking and its interaction with polycystin-1.

271 PC2 ('transience'), accounting for 27% of variance, desc

272 The topological features of the homomeric PC2-, TRPC1- and heteromeric PC2/TRPC1 channel complexes

273 butions to PC2 channel function, heteromeric PC2/TRPC1 channel complexes were also functionally asses

274 f the homomeric PC2-, TRPC1- and heteromeric PC2/TRPC1 channel complexes, assessed by atomic force mi

275 e contribution of individual monomers to the PC2/TRPC1 hetero-complexes was easily distinguishable.

276 plexes, but failed to affect PC2 currents in PC2/TRPC1 heteromeric complexes.

277 Polycystin-2 (PC2, TRPP2) is a Ca(2+)-permeable, nonselective cation c

278 Polycystin-2 (PC2, TRPP2), a member of the transient receptor potentia

279 Polycystin-2 (PC2, TRPP2), the gene product of PKD2, whose mutations c

280 Mutations in polycystins (PC1 or PC2/TRPP2) cause progressive polycystic liver disease (P

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

282 s PC2 and that this delivery is sensitive to PC2 truncation.

283 ed two principal components (PC1-tryptophan, PC2-tyrosine) that captured significant variance in the

284 ere that full-length PC1 that interacts with PC2 via a C-terminal coiled-coil domain regulates PC2 ex

285 Data also suggest that Sirt1 may alter PC2 via a post-translational mechanism.

286 expression leads to increased degradation of PC2 via autophagy.

287 PC2 was associated with SNPs upstream of SNAI3 (P = 0.00

288 The chaperone function of PC2 was dependent on the presence of the distal coiled-c

289 QPCR results indicated that PC1 and PC2 were expressed 4.1- and 5.7-fold higher in retina co

290 PC1 and PC2 were localized primarily in neuronal cells, whereas

291 PC1 and PC2 were primarily expressed in neurons, whereas PACE4 a

292 duals with PKD1 mutations, levels of PC1 and PC2 were reduced to 54% (P<0.02) and 53% (P<0.001), resp

293 a reciprocal functional link between PC1 and PC2 which is critically dependent on their interaction.

294 ncoding polycystin-1 (PC1) and polycystin-2 (PC2), which form an ion channel complex that may mediate

295 PKA directly phosphorylated PC2, which increased the mean open time but not the sing

296 H through an increase in the biosynthesis of PC2, which is essential in the maturation of CRH from it

297 e first phosphorylated residue (Ser(829)) in PC2, whose dephosphorylation is mediated by PC1 binding

298 hat catecholamines inhibited CPE, PC1/3, and PC2, with dopamine quinone the most potent inhibitor (IC

299 the secretion and increased the activity of PC2 within alpha-TC6 cells; the increased intracellular

300 reased intracellular concentration of active PC2 within these cells may therefore account for the enh