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 in a cleaved form and may be complexed with PC2.

4 , rat beta-cells were not immunoreactive for PC2.

5 lysine and tyrosine on the negative side of PC2.

6 atch the most important variable for biology PC2.

7 ignals that are rescued by overexpression of PC2.

8 aved PC1 required an intact interaction with PC2.

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

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

11 ereby promoting the abnormal accumulation of PC2.

12 biquitination and proteasomal degradation of PC2.

13 peptides despite increased release of active PC2.

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

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

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

17 distinguishable from mice completely lacking PC2.

18 iscrimination of the counterfeit whiskies in PC2.

19 e surface expression and function of PC1 and PC2.

20 ion of CRH post-translationally by affecting 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 The human PKD2 locus encodes Polycystin-2 (PC2), a TRPP channel that localises to several distinct

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

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

26 entering the cilium in mutant cells, mutant PC2 accumulates at the ciliary base, forming a ring patt

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

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

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

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

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

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

35 a (OR = 1.43, 95% CI 1.01, 1.98) and between PC2 and overweight (OR = 1.51, 95% CI 1.28, 1.79).

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

37 However PC2 and PC3 explained a low fraction of the total varian

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

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

45 nguished different anatomical parts (PC1 and PC2) and cultivation systems (PC3) into well-defined gro

46 The polycystin-1 (PC1), polycystin-2 (PC2) and fibrocystin proteins, the respective products o

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

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

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

50 d tubulin, gamma-tubulin, polycystin [PC] 1, PC2, and KIF3A), fibroblasts (vimentin, alpha-smooth mus

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

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

57 ffer new insight into the normal function of PC2 as a ubiquitous stress-sensitive protein whose expre

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

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

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

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

62 interacts with the ion channel polycystin-2 (PC2) at the endoplasmic reticulum (ER) membrane, enhanci

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

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

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

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

67 Here, we dissect the ciliary role of PC2 by analysing mice carrying a non-ciliary localising,

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

90 The 2 first PC (PC1 and PC2) construct outcome variables on CSF biomarkers were

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

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

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

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

95 Although PC2 Cterm has been extensively studied for its relations

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

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

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

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

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

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

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

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

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

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

106 PC2-defective cholangiocytes show increased production o

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

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

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

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

111 s including human disease, and conclude that PC2-deficient cells have increased susceptibility to cel

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

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

114 3 reduces intracellular calcium content in a PC2-dependent manner, impairs lysosomal calcium refillin

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

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

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

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

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

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

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

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

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

124 2+)-bound states, consistent with a role for PC2-EF as a Ca(2+)-sensitive regulator.

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

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

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

128 PC2 explained 21.7% and captured horizontal maxillomandi

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

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

131 In this study, we measure how PC2 expression changes in different pathological states,

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

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

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

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

136 2 immunoreactivity, suggesting that aberrant PC2 expression may contribute to impaired proinsulin pro

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

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

139 suggests a two-step model of ciliary entry; PC2 first traffics to the cilium base before TOP domain

140 s were found when adjusting for both PC1 and PC2 for either subset of AIMs (r(2) > 0.900).

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

142 ther Leishmania spp., to take up diamino-PC (PC2) for red light inactivation.

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

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

145 Despite inhibition of PC2 function by temperature blockade, brefeldin A, chlor

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

147 sation in preventing PKD are limited because PC2 function is ablated throughout the cell in existing

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 the ER cation-permeant channel polycystin 2 (PC2) functions to reduce mitochondria-ER contacts.

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

155 ted PC2 protein expression without affecting PC2 gene expression.

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 s expression throughout the body, studies of PC2 have focused primarily on its role in the kidney, as

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

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

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

163 bodies revealed that there was no detectable PC2 immunoreactivity in human beta-cells and little PCSK

164 In all histological experiments, PC2 immunoreactivity in neighboring alpha-cells acted as

165 ith type 2 diabetes, beta-cells had elevated PC2 immunoreactivity, suggesting that aberrant PC2 expre

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

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

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

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

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

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

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

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

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

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

176 The best PC2 inhibitor effectively inhibited glucagon synthesis,

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

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

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

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

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

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

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

184 is also evidence that the C-terminal tail of PC2 is also cleaved in ELVs.

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

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

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

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

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

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

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

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

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

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

195 PC2 knockdown also led to increased ER-mediated mitochon

196 tethering between the ER and mitochondria in PC2 knockdown cells.

197 In cell culture models, PC2 knockdown led to a 50% increase in mitofusin 2 (MFN2

198 culture models and mice with kidney-specific PC2 knockout, knockdown of MFN2 rescued defective mitoch

199 y on its role in the kidney, as mutations in PC2 lead to the development of autosomal dominant polycy

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

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 Data underlining the importance of ciliary PC2 localisation in preventing PKD are limited because P

206 Our results suggest that PC2 localisation to the cilium is necessary to prevent P

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

208 s were examined with the intervention of URO/PC2-medated double-photodynamic inactivation to ascertai

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

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

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

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

213 -ciliary localising, yet channel-functional, PC2 mutation.

214 PC2 mutations are responsible for approximately 15% of a

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

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

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

218 Our data suggest that PC2 normally serves to limit key mitochondrial proteins

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

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

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

222 Polycystin 2 (PC2 or TRPP1, formerly TRPP2) is a calcium-permeant Tran

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

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

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

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

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

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

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

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

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

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

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

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

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

236 However, the endogenous role that PC2 plays in the regulation of general cellular homeosta

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

238 PC2 (positive loadings on Fusicatenibacter and Bifidobac

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

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

241 We found that PC2 proprotein convertase activity contributes to this p

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

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

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

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

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

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

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

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

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

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

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

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

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

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

256 ncoding polycystin-1 (PC1) and polycystin-2 (PC2), respectively.

257 roteins polycystin-1 (PC1) and polycystin-2 (PC2), respectively.

258 utation or deletion of the gene encoding for PC2 results in autosomal dominant polycystic kidney dise

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

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

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

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

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

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

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

266 rder neurons in the Drosophila brain, called pC2, that are tuned for multiple temporal aspects of one

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

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

269 /3 (PC1/3) and then prohormone convertase 2 (PC2), this finding has not been verified in human beta-c

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

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

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

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

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

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

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

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

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

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

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

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

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

285 expression leads to increased degradation of PC2 via autophagy.

286 When adjusted for fiber intake, PC2 was also associated with higher BMI z-scores (beta =

287 also associated with nasal obstruction, and PC2 was associated with breathing difficulties and lean

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

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

290 ta-cells process proinsulin by PC1/3 but not PC2, we suggest that there is a need to revise the long-

291 PC1 and PC2 were also associated with nasal obstruction, and PC2

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 Crown cells express PC1-L1 and PC2, which may form a heteromeric polycystin channel com

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

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

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

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