ライフサイエンスコーパス: PP2C

1 PP2C alpha and PP2C beta 2 co-purified with Mg(2+)-depen

2 PP2C exists in a complex with Dvl, beta-catenin, and Axi

3 PP2C phosphatases control biological processes including

4 PP2C utilizes Axin as a substrate both in vitro and in v

5 h interaction with a protein phosphatase 2C (PP2C) and a heterotrimeric GTP-binding protein (G protei

6 ed PXR scaffolds the protein phosphatase 2C (PP2C) and SGK2 to stimulate PP2C to dephosphorylate SGK2

7 dies have implicated protein phosphatase 2C (PP2C) as a novel negative regulator of stress response p

8 holipase D (PLD) and protein phosphatase 2C (PP2C) both play a role in mediating plant responses to a

9 t with inhibition of protein phosphatase 2C (PP2C) by chelation of intracellular Mg2+.

10 ) is a member of the protein phosphatase 2C (PP2C) family and controls cell cycle checkpoints in resp

11 ) is a member of the protein phosphatase 2C (PP2C) family and functions as a negative regulator of th

12 s two members of the protein phosphatase 2C (PP2C) family, Ptc2 and Ptc3, as well as the protein phos

13 rs of members of the PROTEIN PHOSPHATASE 2C (PP2C) family.

14 ent serine/threonine protein phosphatase 2C (PP2C) family.

15 d a serine/threonine protein phosphatase 2C (PP2C) from the human malaria parasite Plasmodium falcipa

16 Protein phosphatase 2C (PP2C) is a class of ubiquitous and evolutionarily conser

17 Protein phosphatase 2C (PP2C) is a Mn2+- or Mg2+-dependent protein Ser/Thr phosp

18 Protein phosphatase 2C (PP2C) is an archetype of the PPM Ser/Thr phosphatases, c

19 The protein phosphatase 2C (PP2C) mutant abi1-1 disrupted ABA activation of I(Ca) ch

20 se activities of the protein phosphatase 2C (PP2C) phosphatase family member, PPM1A.

21 e that POL encodes a protein phosphatase 2C (PP2C) with a predicted nuclear localization sequence, in

22 specific subclade of protein phosphatase 2C (PP2C), form functional holoreceptors.

23 crystal structure of protein phosphatase 2C (PP2C).

24 L] and an associated protein phosphatase 2C (PP2C).

25 paralogues encoding protein phosphatase 2C (PP2C, group A), which is known to be a negative regulato

26 ene, encoding a protein phosphatase type 2C (PP2C).

27 cus that encode protein phosphatase type 2C (PP2C).

28 he activity of protein phosphatases type 2C (PP2C).

29 ative regulation by protein phosphatases 2C (PP2Cs) of the protein kinase OPEN STOMATA 1 (OST1) and u

30 Clade A protein phosphatases type 2C (PP2Cs) are negative regulators of abscisic acid (ABA) si

31 genes encoding protein phosphatases type 2C (PP2Cs) involved in the regulation of ABA signalling.

32 ncoding Ser/Thr protein phosphatase type 2C (PP2Cs) known from genetic studies or predicted by hierar

33 ion of several clade A phosphatases type 2C (PP2Cs), since PYL8 interacted in vivo with at least five

34 ty and inhibit clade A phosphatases type-2C (PP2Cs) in an ABA-dependent manner.

35 ase M (PPM) family (protein phosphatases 2C [PP2Cs] subfamily), protein tyrosine (Tyr) phosphatases (

36 , we identified protein phosphatase 2Calpha (PP2C) as a Dvl-PDZ domain-interacting protein.

37 s thaliana) clade A protein phosphatase 2Cs (PP2Cs) have established abscisic acid (ABA) signaling ro

38 RCAR ABA receptors, PROTEIN PHOSPHATASE 2Cs (PP2Cs), and SNF1-RELATED PROTEIN KINASE 2s (SnRK2s) form

39 ink between a Pkn2-type protein kinase and a PP2C phosphatase.

40 GEF1 directly interacts with several clade A PP2C protein phosphatases, including ABI1.

41 n FtsZ; and a C-terminal domain comprising a PP2C protein phosphatase.

42 BtrU contains a PP2C-like serine phosphatase domain, BtrW contains a ser

43 Cloning of RDO5 showed that it encodes a PP2C phosphatase.

44 onsisting of several components, including a PP2C member, SnRK2-type kinase (OST1), and an ion channe

45 hemical analyses confirmed that BA-Stp1 is a PP2C phosphatase and dephosphorylates phosphoserine and

46 eptide, RRA(pT)VA, indicating that Pph1 is a PP2C phosphatase.

47 unds may form the basis for development of a PP2C inhibitor pharmacophore and may facilitate investig

48 ontrast, hypocotyl segments overexpressing a PP2C.D phosphatase are specifically impaired in auxin-me

49 ve to okadaic acid, consistent with PHLPP, a PP2C family member, controlling the hydrophobic site.

50 product, phosphatidic acid (PA), regulate a PP2C, ABI1, which is a negative regulator of ABA respons

51 RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating a signalling cascad

52 The presented findings point to a PP2C-RopGEF-ROP/RAC control loop model that is proposed

53 of a Schizosaccharomyces pombe strain with a PP2C (PTC1) deletion.

54 functional differentiation among the clade A PP2Cs and a point of cross talk between ABA-dependent an

55 iscovered that PYR/PYL receptors and clade A PP2Cs are crucial for the hydrotropic response that take

56 er potential, while mutants of other clade A PP2Cs had no or lesser effect on these drought resistanc

57 The group A PP2Cs ABI1, ABI2, and PP2CA down-regulated CPK6-mediated

58 The group-A PP2Cs, of which ABI1 is the prototypical member, are pro

59 ound receptors as well as a ternary PYL2-ABA-PP2C complex.

60 ced phosphatidic acid (PA) binds to the ABI1 PP2C to signal ABA-promoted stomatal closure, whereas PL

61 ed in metal binding and catalysis, abolished PP2C activity.

62 e propose that INS2 allosterically activates PP2C, fulfilling the role of a putative mediator mimetic

63 channels was reduced in the dominant active PP2C mutants abi1-1 and abi2-1.

64 1/pp2ca mutant plants, revealing that active PP2C protein phosphatases protect and stabilize RopGEF1

65 Diverse regulatory domains adapt PP2C phosphatases to specific functions, but how these d

66 In addition, PP2C expression relieves Axin-mediated repression of LEF

67 s that this switch is widely conserved among PP2C family members, serving as a platform to control ph

68 PP2C alpha and PP2C beta 2 co-purified with Mg(2+)-dependent Cdk2/Cdk6

69 ract, partially purified HeLa PP2C alpha and PP2C beta 2 isoforms, and the recombinant PP2Cs exhibite

70 oreover, purified recombinant PP2C alpha and PP2C beta 2 proteins efficiently dephosphorylated monome

71 he JNK MAP-kinase inhibitory phosphatase and PP2C in addition to string (Cdc25).

72 action kinetics between phosphomonoester and PP2C yielded exponential "bursts" of product formation,

73 lies of important signaling enzymes, PLD and PP2C.

74 PP1, PP2A, and PP2C but not PP2B were detected in lysates from Calu-3 c

75 threonine phosphatases (PP1, PP2A, PP2B, and PP2C) on AS160 dephosphorylation.

76 A receptor pyrabactin resistant 1 (PYR1) and PP2C phosphatases with two alternate signaling cores inc

77 RCARs and PP2C coreceptors are represented by small protein famili

78 PTPalpha, CD45, VHR, MKP3, Cdc25A, Stp1, and PP2C).

79 srupt the interaction between the SnRK2s and PP2Cs, thus preventing the PP2C-mediated dephosphorylati

80 hosphatases that are distinct from bacterial PP2C phosphatases such as RsbU, RsbX and SpoIIE.

81 lpha0) is unique to a subfamily of bacterial PP2C phosphatases that possess N-terminal sensing domain

82 Because PP2C is insensitive to these inhibitors, we tested the h

83 The dephosphorylation of Cdk2 and Cdk6 by PP2C isoforms was inhibited by the binding of cyclins.

84 y LKB1 and antagonizing dephosphorylation by PP2C.

85 First, release of inhibition by PP2C allows the SnRK2s to become partially active becaus

86 nd suggest a dynamic regulation of mGluR3 by PP2C.

87 receptors to preferentially inhibit certain PP2Cs.

88 f enzymatic (GGDEF, EAL, HD-GYP, CheB, CheC, PP2C, and HisK), RNA-binding (ANTAR and CsrA), protein-

89 enetic screen, we identified the chloroplast PP2C phosphatase, PHOTOSYSTEM II CORE PHOSPHATASE (PBCP)

90 To address the hypothesis that the ABI-clade PP2Cs regulate the bZIPs directly, in addition to their

91 Based on the results that a constitutive PP2C blocks but constitutive Ca2+-dependent protein kina

92 nd btrV encode proteins predicted to contain PP2C-like Ser phosphatase, HPK (His protein kinase)-like

93 BA receptor RCAR4/PYL10 showed ABA-dependent PP2C regulation.

94 activated mutants found in a very different PP2C protein.

95 he abi2-1 mutation, which lies in a distinct PP2C gene, also disrupted ABA activation of I(Ca).

96 gests a mechanism for the action of dominant PP2C mutants that could serve as valuable tools to under

97 We can now advance the model that either PP2C phosphatase, when triggered by its particular class

98 to D mutations near the DGH motif eliminated PP2C activity but displayed opposite effects on ABA sign

99 = 28 308) with strong homology to eukaryotic PP2C phosphatases and that it belongs to a new group of

100 t the alpha0 helix characterizes an extended PP2C domain in many bacterial signalling proteins, and s

101 Recombinant P. falciparum PP2C expressed in Escherichia coli was active in dephosp

102 e PYL8 interacted in vivo with at least five PP2Cs, namely HYPERSENSITIVE TO ABA1 (HAB1), HAB2, ABA-I

103 lation elongation component as substrate for PP2C suggests an important regulatory function for this

104 xy-terminal domain that encodes a functional PP2C.

105 Furthermore, PP2C-like enzymes are the predominant phosphatases towar

106 HAI PP2C mutants had enhanced proline and osmoregulatory sol

107 HAI PP2C single mutants were unaffected in ABA sensitivity,

108 Overall, the HAI PP2Cs had greatest effect on ABA-independent low water p

109 Conversely, the HAI PP2Cs had relatively less impact on several ABA sensitiv

110 The HAI PP2Cs interacted most strongly with PYL5 and PYL7 to -10

111 henotypic roles of the remaining three "HAI" PP2Cs, Highly ABA-Induced1 (HAI1), AKT1-Interacting PP2C

112 regulatory function, and the C terminus has PP2C-like phosphatase catalytic activity.

113 n HeLa cell extract, partially purified HeLa PP2C alpha and PP2C beta 2 isoforms, and the recombinant

114 The crystal structure of human PP2C reveals a novel protein fold with a catalytic domai

115 tent with the crystal structure of the human PP2C, the mutation of two conserved motifs in ABI1, pred

116 tructure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors.

117 sting stress signaling components, including PP2C phosphatases and SnRK kinases, were adapted for nov

118 ided by the demonstration that SAURs inhibit PP2C.D phosphatases to activate plasma membrane (PM) H(+

119 ABA receptors interacted with and inhibited PP2C phosphatase activity against the SnRK2-type kinase,

120 t the equivalent region of mGluR2, inhibited PP2C assayed by using [32P]casein as a substrate.

121 e in PM H(+)-ATPase activation by inhibiting PP2C.D family protein phosphatases.

122 re ABA receptors that function by inhibiting PP2Cs to activate SnRK2s, resulting in phosphorylation o

123 ay that controls ABA signaling by inhibiting PP2Cs.

124 to PYR1, which in turn binds to and inhibits PP2Cs.

125 Mn2+-dependent and okadaic acid-insensitive PP2C activity in vitro.

126 hpP, a S. pneumoniae Ser-Thr eukaryotic-like PP2C phosphatase as an interacting partner of RitR.

127 us high ABA levels, the RCARs regulated most PP2Cs and activated the ABA response to a similar extent

128 The Arabidopsis genome encodes nine PP2C coreceptors and 14 different RCARs, which can be di

129 rmine that it is due to PP2C beta 2, a novel PP2C beta isoform, and to PP2C alpha.

130 The metal-dependent activity of PP2C (as reflected in kcat and kcat/Km), indicated that

131 ive LEF-1 reporter gene assay, expression of PP2C activates transcription and also elicits a synergis

132 Second, high expression of PP2C leads to sustained activating tyrosine phosphorylat

133 First, high expression of PP2C produces phenotypes that are inconsistent with nega

134 Fourth, high expression of PP2C suppresses Atf1-dependent transcription of a stress

135 of Spc1, is unaffected by high expression of PP2C.

136 Inhibition of PP2C activity enables activation of SNF1-RELATED KINASE

137 acophore and may facilitate investigation of PP2C control and cellular function.

138 Modification of PP2C expression resulting in ABA insensitivity or hypers

139 In contrast, the D163A mutant of PP2C was not activated by INS2.

140 ct as positive transcriptional regulators of PP2C genes, and thereby as negative regulators of abscis

141 as evolutionary and structural relatives of PP2C phosphatases.

142 framework that links ABA-mediated release of PP2C inhibition to activation of SnRK2 kinases.

143 ctivation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C

144 revealed that there are three subfamilies of PP2C phosphatases in all 12 species of Drosophila.

145 e been proposed as the in vivo substrates of PP2C, the prototypical member of the PPM family.

146 t by okadaic acid, and is similar to that of PP2C phosphatase.

147 hile the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimic

148 Arabidopsis genome contains an abundance of PP2Cs (69) and a dearth of PTPs (one).

149 indicating that ABA-dependent inhibition of PP2Cs by PYR/PYLs is required for the proper perception

150 PYR/RCAR-dependent inhibition of PP2Cs was clearly required for rapid stomatal regulation

151 indicating that the substrate specificity of PP2Cs toward CDKs is evolutionarily conserved.

152 ization predicted a unique favorable site on PP2C for INS2 in a surface cleft adjacent to the catalyt

153 including within the gene encoding the only PP2C Ser/Thr phosphatase in Streptococcus pneumoniae, in

154 onserved residues that participate in ABA or PP2C contacts.

155 osphorylation sites was unaltered by PP2B or PP2C inhibitors.

156 the two or three metal ions present in other PP2C enzymes.

157 ss of substrates to the active site in other PP2C phosphatases is diminished in SpoIIE, and this obse

158 tabetaalpha arrangement reminiscent of other PP2C-type phosphatases.

159 e POL catalytic domain is conserved in other PP2Cs, the POL protein represents a unique subclass of p

160 hare conserved functional regions with other PP2Cs from a diverse array of species.

161 , CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha).

162 dephosphorylation by the protein phosphatase PP2C present in the retina.

163 r PYR1 with the type 2C protein phosphatase (PP2C) ABI1, the serine/threonine protein kinase SnRK2.6/

164 the downstream type 2C protein phosphatase (PP2C) effectors.

165 gene encodes a type 2C protein phosphatase (PP2C) that is induced by ionizing radiation in a p53-dep

166 ity of the ABI1 type 2C protein phosphatase (PP2C).

167 The Ptc1-type 2C Ser/Thr phosphatase (PP2C) inactivates Hog1 by dephosphorylating phospho-Thr,

168 nd the serine/threonine protein phosphatases PP2C and lambda.

169 d inhibition of type 2 protein phosphatases (PP2C) by PYRABACTIN RESISTANCE/REGULATORY COMPONENTS OF

170 es one of four type 2C protein phosphatases (PP2C) in the fission yeast Schizosaccharomyces pombe.

171 s that inhibit type 2C protein phosphatases (PP2C) when in their agonist-stabilized conformation.

172 ional type 2C serine/threonine phosphatases (PP2C), Ptc1 and Ptc3.

173 We show that type 2C protein phosphatases (PP2Cs) are responsible for this dephosphorylation of Cdc

174 Type 2C protein phosphatases (PP2Cs) are vitally involved in abscisic acid (ABA) signa

175 at two clade A type 2C protein phosphatases (PP2Cs), established repressors of the abscisic acid (ABA

176 a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA recep

177 complexes with type 2C protein phosphatases (PP2Cs).

178 rotein represents a unique subclass of plant PP2Cs.

179 In plants, PP2C activity would control the stomatal aperture by reg

180 r/Thr protein phosphatases (PP1, PP2A, PP2B, PP2C alpha, and lambda PP).

181 e protein phosphatase metallo-dependent (PPM/PP2C) family and is independent of beta-arrestin 2.

182 These observations identify the PPM/PP2C family as a mediator of G protein-coupled receptor

183 ster of 7 closely related members of the PPM/PP2C family is present, and (iv) some P. falciparum prot

184 onine phosphorylation and fig is a predicted PP2C phosphatase specific for serine/threonine residues.

185 fig codes for a predicted PP2C phosphatase.

186 ere identified and characterized as putative PP2C group A members.

187 o identify variants that increase basal PYR1-PP2C interactions, which uncovered activating mutations

188 Here, we analyzed all RCAR-PP2C combinations for their capacity to regulate ABA sig

189 vel the interaction network of possible RCAR-PP2C pairings and their different potentials to serve a

190 Of 126 possible RCAR-PP2C pairings, 113 were found to be functional.

191 of ABA-induced versus constitutive PYR/RCAR-PP2C interactions.

192 This emerging PYR/RCAR-PP2C-SnRK2 model of ABA signal transduction is reviewed

193 We also consider how the PYR/RCAR-PP2C-SnRK2 pathway interfaces with ABA-dependent gene ex

194 The specificity of the RCAR-PP2C interaction and the constraints contributing to spe

195 d identifies structural constraints of RCAR7-PP2C interaction.

196 ase catalytic cleft, thus mimicking receptor-PP2C interactions.

197 ctural feature absent in pyrabactin-receptor/PP2C complexes.

198 ctin forms a hydrogen bond with the receptor/PP2C "lock" hydrogen bond network, a structural feature

199 the core components PYL/RCAR ABA receptors, PP2C-type protein phosphatases, and protein kinases.

200 Moreover, purified recombinant PP2C alpha and PP2C beta 2 proteins efficiently dephosph

201 nd PP2C beta 2 isoforms, and the recombinant PP2Cs exhibited a comparable substrate preference for a

202 Several PP2C phosphatases belonging to clade A are involved in a

203 Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity

204 distinct from the active site in all solved PP2C structures.

205 n identification of novel activities of some PP2Cs.

206 that could activate them and found that some PP2Cs can also interact directly with CPK11.

207 phosphatase 2C (PP2C) and SGK2 to stimulate PP2C to dephosphorylate SGK2 at threonine 193.

208 PAS, a central coiled-coil and a C-terminal PP2C phosphatase.

209 A second class, in the RssB C-terminal PP2C-like domain, led to activation of RssB function.

210 ational analysis of two Arabidopsis thaliana PP2Cs, encoded by ABI1 and AtPP2C, involved in the plant

211 expression analyses further demonstrate that PP2C inhibition by ABA results in SnRK1 activation, prom

212 We find that PP2C, but not PP1, PP2A, or PP2B, dephosphorylates the m

213 Moreover, it was hypothesized that PP2C dephosphorylates one or more components of protein

214 t disprove this hypothesis and indicate that PP2C instead negatively regulates a downstream element o

215 These results indicate that PP2C is a positive regulator of Wnt signal transduction

216 ing to several protein kinases revealed that PP2C displays a strong preference for diphosphorylated p

217 These studies strongly suggest that PP2C acts downstream of Spc1 kinase in the stress-activa

218 These observations strongly suggest that PP2C enzymes play an important role in the attenuation o

219 ue in cystic fibrosis; our data suggest that PP2C may be an important phosphatase to target.

220 These results suggest that PP2C may be the okadaic acid-insensitive phosphatase tha

221 The PP2C AHG1 was regulated only by RCAR1/PYL9, RCAR2/PYL7,

222 The PP2C phosphatase Wip1 dephosphorylates p38 and blocks UV

223 ant for Wip1 inhibitor selectivity among the PP2C family.

224 neurons and demonstrates a new role for the PP2C/PPM phosphatases as regulators of neuronal developm

225 Hence, the PP2C hub allows the coordinated activation of ABA and en

226 A conserved tryptophan in the PP2C inserts directly between the gate and latch, which

227 r to dock into and competitively inhibit the PP2C active site.

228 tes after DNA damage and classified into the PP2C family.

229 imited sequence similarity to members of the PP2C class of protein serine/threonine phosphatases.

230 fied a Drosophila Ser/Thr phosphatase of the PP2C family, named Alphabet (Alph), which acts as a nega

231 PP2CA, one of the PP2C phosphatase family members acts in an opposing mann

232 presenting active and inactive states of the PP2C phosphatase SpoIIE from Bacillus subtilis.

233 en the SnRK2s and PP2Cs, thus preventing the PP2C-mediated dephosphorylation of the SnRK2s and result

234 Mutational analysis demonstrates that the PP2C domain is the Spn effector domain and is essential

235 Here, we found that the PP2C phosphatase, Ptc4, plays an important role in inact

236 We found that the PP2C-like activity in HeLa cell extract, partially purif

237 es a protein phosphatase that belongs to the PP2C family and is able to functionally complement a yea

238 Thr phosphatase (Stp1), which belongs to the PP2C family of phosphatases.

239 lay from the PYL/RCAR-type receptors, to the PP2C-SnRK2 phosphatase-kinase pairs, to the ion channel

240 /PYL family of ABA receptors, with which the PP2C proteins interact.

241 s additional SAUR proteins interact with the PP2C-D subfamily of type 2C protein phosphatases.

242 ltiple members of the ABF/AREB clade and the PP2Cs by yeast two-hybrid, in vitro phosphatase, and bim

243 the ABA signalling mechanism defined by the PP2Cs and the PYR/PYL family of ABA receptors, with whic

244 t the SnRK2 kinases are kept inactive by the PP2Cs through physical interaction and dephosphorylation

245 Furthermore, the PP2Cs HAI1 to HAI3 were regulated by all RCARs, and the

246 R7 regulated the phosphatase activity of the PP2Cs ABI1, ABI2, and PP2CA in vitro at nanomolar ABA le

247 In this study, we characterize this PP2C-like activity in HeLa cell extract and determine th

248 a previously uncharacterized member of this PP2C family in Arabidopsis (Arabidopsis thaliana), At5g5

249 L ABA receptors, and close relatives of this PP2C, such as PP2CA/ABA-HYPERSENSITIVE GERMINATION3 (AHG

250 To study the function of this PP2C, we have tested the ability of different constructs

251 five dual-specificity phosphatases and three PP2Cs.

252 ity is attenuated by either serine/threonine PP2C or tyrosine phosphatases.

253 2C beta 2, a novel PP2C beta isoform, and to PP2C alpha.

254 cell extract and determine that it is due to PP2C beta 2, a novel PP2C beta isoform, and to PP2C alph

255 ating that SAUR proteins also inhibit tomato PP2C.D family phosphatases and that AtSAUR19 overexpress

256 We show here that two PP2C serine phosphatases - RsbP, which is required for r

257 PPM1D (Wip1), a type PP2C phosphatase, is expressed at low levels in most nor

258 Wild-type PP2C activity assayed with a phosphopeptide substrate wa

259 mutants are unlikely to impede the wild-type PP2C and cause hyperphosphorylation of substrates.

260 The D163A mutant and wild-type PP2C in the absence of INS2 had the same Mn(2+)-dependen

261 ers, particularly for the largely unexplored PP2C set, will be a rich source of material for plant bi

262 of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity, suggestive of conver

263 n disrupts PYL association with ABA and with PP2C phosphatase effectors, leading to inactivation of S

264 the mGluR family only mGluR3 interacted with PP2C.

265 ail at Ser-845 inhibits the interaction with PP2C.

266 -triggered interaction of ABA receptors with PP2C-type phosphatases to send a fluorescence resonance

267 , was found to be able to complement a yeast PP2C-deficient mutant (pct1Delta).

268 d is able to functionally complement a yeast PP2C-deficient mutant TM126 (ptc1Delta).

269 Two yeast PP2Cs, Ptc2p and Ptc3p, display Cdc28p phosphatase activ