ライフサイエンスコーパス: PP2A

1 PP2A complexes are modulated by proteins such as cancero

2 PP2A complexes with B56 subunits are targeted by Shugosh

3 PP2A comprises three distinct subunits and forms through

4 PP2A directly dephosphorylates MYC, resulting in its deg

5 PP2A holoenzymes comprise catalytic C-, scaffolding A-,

6 PP2A is an essential protein phosphatase that regulates

7 PP2A regulates Na(v)1.5 activity in mouse cardiomyocytes

8 PP2A substrate specificity, localization, and regulation

9 PP2A's tumor-suppressive functions have been intensely s

10 PP2A-B55 activity is then sharply downregulated at the o

11 regulatory subunit of protein phosphatase 2 (PP2A), determines sensitivity to CHK1 inhibition.

12 bor mutations in the protein phosphatase 2A (PP2A) Aalpha scaffold subunit encoded by PPP2R1A In this

13 atic mutation of the protein phosphatase 2A (PP2A) Aalpha-subunit gene PPP2R1A is highly prevalent in

14 e found that a lower protein phosphatase 2A (PP2A) activity, a phosphatase responsible for Syn I (S9)

15 Protein phosphatase 2A (PP2A) critically regulates cell signaling and is a human

16 Protein phosphatase 2A (PP2A) enzymes can suppress tumors, but they are often in

17 The serine/threonine Protein Phosphatase 2A (PP2A) functions as a tumor suppressor by negatively regu

18 r and its associated protein phosphatase 2A (PP2A) in macrophage activation.

19 ribution of CD25 and protein phosphatase 2A (PP2A) in promoting IL-2R signaling in Tregs.

20 Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), cat

21 Protein phosphatase 2A (PP2A) is a key signaling component that controls stress

22 Protein phosphatase 2A (PP2A) is a large enzyme family responsible for most cell

23 Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase that regulates a

24 The tumor suppressor protein phosphatase 2A (PP2A) is a serine/threonine phosphatase whose activity i

25 rates by the ser/thr protein phosphatase 2A (PP2A) is poorly understood, limiting our understanding o

26 (SET)/inhibitor 2 of protein phosphatase 2A (PP2A) oncoprotein binds and inhibits PP2A, composed of v

27 herapy" by depleting protein phosphatase 2A (PP2A) or its inhibition using a small molecule inhibitor

28 tochondria-localized protein phosphatase 2A (PP2A) regulatory subunit, as a neuron-specific Drp1 acti

29 e with activation of protein phosphatase 2A (PP2A), a tumor suppressor phosphatase, and determined th

30 ning Aldob, Akt, and protein phosphatase 2A (PP2A), leading to inhibition of cell viability, cell cyc

31 hosphatases, such as protein phosphatase 2A (PP2A), that normally counteract kinases, contributes to

32 for association with protein phosphatase 2A (PP2A).

33 hosphorylated by the protein phosphatase 2A (PP2A); our data show that when methionine is abundant, t

34 egulators, including protein phosphatase 2A (PP2A-B55/SUR-6), biophysical regulators, including dynei

35 transcription factor TCP8-like (TCP8) and a PP2A regulatory subunit TAP46-like (TAP46) were indeed p

36 sDNA breaks, homologous recombination, and a PP2A-dependent replication stress response.

37 osis can occur independently of p53 but in a PP2A-dependent manner.

38 analysis identified protein phosphatase 2 A (PP2A) as one of the top ATG-interacting proteins in rena

39 ential host enzyme, protein phosphatase 2 A (PP2A), is repurposed as an integral component of the int

40 the PP2A holoenzyme, composed of PP2A-Abeta, PP2A-B56gamma, and PP2ACalpha subunits, is selectively a

41 manner; low concentrations of Cdk1 activate PP2A-B55 and high concentrations inactivate it.

42 APs, a separate class of compounds, activate PP2A holoenzymes containing a different regulatory subun

43 ed intracellular Ca(2+) levels and activated PP2A, which down-regulated IGF signaling and promoted th

44 protein phosphatase 2 phosphatase activator (PP2A) and protein phosphatase 1 (PP1).

45 Furthermore, inhibition of Alk5, PP2A or Notch signaling rescues MG proliferation in Tgfb

46 a demonstrate that the P179R mutation alters PP2A-Aalpha protein conformation, impairing holoenzyme f

47 ctive binding partners, Sgo1 helps to anchor PP2A-B56 at both locations: it collaborates with BubR1 t

48 by RSK3 (p90 ribosomal S6 kinase type 3) and PP2A (protein phosphatase 2A) at signalosomes organized

49 gesting that Sgo1 can integrate Aurora B and PP2A activities to modulate Aurora B substrate phosphory

50 bal substrate identification of PP2A-B56 and PP2A-B55 holoenzymes.

51 By acting together, CDK1-CCNB1 and PP2A-B55 thus create a spindle checkpoint-permissive sta

52 a layer to the interaction between CDK1 and PP2A in regulating mitotic entry.

53 balance of cyclin-dependent kinase Cdk1 and PP2A:B55 activity.

54 the state of mitochondrial connectivity and PP2A/Bbeta2-mediated dephosphorylation of Drp1 play a cr

55 e antiviral APOBEC3 enzymes (APOBEC3C-H) and PP2A phosphatase regulators (PPP2R5A to PPP2R5E).

56 cortex and greater coexpression of Syn I and PP2A A subunit, which was observed as perinuclear aggreg

57 signaling proteins, such as TAK1, IKKs, and PP2A, that impairs TRAF6-mediated activation of NF-kappa

58 centromeres inactivates Aurora B kinase, and PP2A phosphatase dephosphorylates the kinetochore protei

59 meostasis by balancing the opposing LKB1 and PP2A.

60 Mechanistically, PKCzeta, ERK1/2, mTOR, and PP2A are key regulators of the Myc response in this sett

61 r propose that crosstalk involving Notch and PP2A enables tuning and integration of Notch signaling w

62 cancers driven by RABL6A overexpression and PP2A inactivation.

63 he metazoan SAC, since the relevant PLK1 and PP2A-B56 binding motifs have coevolved in the same regio

64 ven when the levels or activities of PP1 and PP2A are strongly inhibited at kinetochores.

65 d by CDK1-cyclin B and counteracting PP1 and PP2A family phosphatases through modulation of both acti

66 onstrate the association of DAT with PP1 and PP2A in the mouse brain and heterologous cell systems.

67 the CDK1-counteracting phosphatases PP1 and PP2A-B55, allowing wide-spread dephosphorylation of subs

68 We show here that PP1 and PP2A-B56 phosphatases are primarily required to remove P

69 t involves two protein phosphatases, PP1 and PP2A-B56, that are thought to extinguish checkpoint sign

70 o express in vivo mAKAPbeta-derived RSK3 and PP2A anchoring disruptor peptides that block the associa

71 e functions have been intensely studied, and PP2A inactivation has been shown to be a prerequisite fo

72 UNC5B and PP2A are regarded as tumor suppressors, as they promote

73 rlying mechanism and identify the DRD5-ARRB2-PP2A axis as a potential target for future therapy of in

74 Furthermore, the DA-DRD5-ARRB2-PP2A signaling axis can prevent S. aureus-induced inflam

75 The B55alpha-PP2A complex localized to adhesions and directly dephosp

76 Mechanistically, we found that the B55alpha/PP2A complex restrains PHD-2 activity, promoting EC surv

77 data underline a unique role of the B55alpha/PP2A phosphatase complex in vessel remodeling and sugges

78 DT-061, specifically stabilizes the B56alpha-PP2A holoenzyme in a fully assembled, active state to de

79 S1 S281 dephosphorylation is delayed because PP2A-B55 is negatively regulated by CDK1-CCNB1 and only

80 However, most validated LxxIxE motifs bind PP2A:B56 with micromolar affinities, suggesting that add

81 Thus, blocking PP2A association with Integrator stimulates pause releas

82 We find that Integrator-bound PP2A dephosphorylates the RNA Pol II C-terminal domain a

83 sponses, and cellular processes regulated by PP2A modulation and may enable the development of combin

84 The canonical PP2A holoenzyme comprises a scaffolding subunit (PP2A Aa

85 rpin RNA-mediated targeting of the catalytic PP2A subunit (Ppp2ca) had no effect on dexamethasone res

86 sought to reduce the complexity of cellular PP2A holoenzymes.

87 One of the best-characterized PP2A substrates is MYC proto-oncogene basic helix-loop-h

88 e, we show that ST not only displaces common PP2A B subunits but also promotes A-C subunit interactio

89 Functional studies showed complete PP2A dysfunction in four individuals with seemingly mild

90 -ceramide, and mechanism of FTY720-dependent PP2A activation, remain unknown.

91 x, leading to resistance to FTY720-dependent PP2A activation.

92 A crystal structure of the tumor-derived PP2A mutant revealed marked changes in A-subunit conform

93 of serine/threonine phosphatases designated PP2A, is essential for the pathogenesis of many diseases

94 Together, this study describes how different PP2A-B56 complexes utilise isoform-specific interactions

95 ernative holoenzymes by binding of different PP2A regulatory subunits compared with wild-type Aalpha,

96 explore the therapeutic potential of direct PP2A activation in a diverse set of MYC-driven cancers,

97 as allosteric switches to activate distinct PP2A complexes with unique substrates.

98 sistent with global phosphoproteome effects, PP2A modulations broadly affect responses to more than 2

99 ting that additional motifs exist to enhance PP2A:B56 binding.

100 Enhanced PP2A activity by ATG reduces p65 NF-kappaB-mediated infl

101 substrate of PGLS, bound to Src and enhanced PP2A recruitment.

102 Enhancing PP2A activity represents a feasible therapeutic approach

103 generated a series of cell lines expressing PP2A-dependent phosphodegron variants of MYC and demonst

104 ST recruitment of STRIPAK facilitates PP2A-mediated dephosphorylation of MAP4K4 and induces ce

105 Recently, the first PP2A:B56 consensus binding motif, LxxIxE, was identified

106 For PP2A-B56, these patterns are further modulated by affini

107 A role for PP2A in CAR regulation has been less clear, although los

108 Here, we uncover a role for PP2A-B55/SUR-6 in regulating centrosome separation.

109 ding, a function distinct and exclusive from PP2A-B56 binding.

110 and reveals unexpected mechanisms governing PP2A dephosphorylation site specificity and tumor suppre

111 for assembly and activation of heterogeneous PP2A heterotrimers.

112 rically assembling a specific heterotrimeric PP2A holoenzyme consisting of PPP2R1A (scaffold), PPP2R5

113 Moreover, they highlight PP2A reactivation as a potential therapeutic strategy fo

114 viding a new framework for understanding how PP2A regulation drives cellular signaling.

115 We identified PP2A-modulated targets in diverse cellular pathways, inc

116 found that pathogenic PPP2CA variants impair PP2A-B56(delta) functionality, suggesting that PP2A-rela

117 These outcomes implicate PP2A functional inactivation as a critical component of

118 totic entry and exit but that the changes in PP2A-B55 activity are the ultimate trigger.

119 ns: Our study indicates that the decrease in PP2A activity that occurs in COPD contributes to elevate

120 e antibody was mediated by an enhancement in PP2A activity.

121 sults demonstrate that the R183W mutation in PP2A Aalpha scaffold abrogates the tumor suppressive act

122 n released SET from PP2ACalpha, resulting in PP2A activation, while monomeric SET remained associated

123 nding the phosphorylation site play roles in PP2A substrate specificity.

124 comprehensive drug-sensitivity screening in PP2A-modulated cells to evaluate the functional impact o

125 alpha/mTORC1 pathways derived from increased PP2A activity in protocol 2, whereas it additionally inh

126 We demonstrate that increased PP2A activity can interrupt ongoing DNA replication, res

127 division cycle 45 (CDC45) and that increased PP2A activity caused dissociation of CDC45 and polymeras

128 left ventricular function through increased PP2A activity and inhibition of AMPKalpha and its downst

129 iroketal fragment might be crucial to induce PP2A inhibition.

130 ding A-subunit of PP2A (PPP2R1A) (to inhibit PP2A) in HeLa cells.

131 ase 2A (PP2A) oncoprotein binds and inhibits PP2A, composed of various isoforms of scaffolding, regul

132 r findings provide fundamental insights into PP2A complex assembly and regulation, identify a unique

133 e netrin-UNC5B axis, such as those involving PP2A, assumes greater clinical significance.

134 Here, we show that SET, a known PP2A inhibitor, directly binds to a domain in Sgo1 in cl

135 At the molecular level, PP2A/B56alpha complex was found to localize and coimmuno

136 catalytic activity by kinetochore-localized PP2A-B56 is thus critical for controlled MPS1 activity a

137 Mechanistically, PP2A-B55/SUR-6 regulates nuclear size before mitotic ent

138 Mechanistically, PP2A-Cdc55 ceramide-activated phosphatase was found to a

139 hibition of protein phosphatase 2A-mediated (PP2A-mediated) dephosphorylation of Ser5 in the pyrin do

140 s-of-function genetic approaches to modulate PP2A activity, we found that PP2A regulates DNA replicat

141 Modulating PP2A expression or activity, with silencer siRNA or a ch

142 , assembling and anchoring a multifunctional PP2A complex with other targets.

143 show that PP2A complexity reduction, but not PP2A overexpression, reveals a role of this holoenzyme i

144 Notably, PP2A inhibition or reactivation affected largely distinc

145 The ability of PP2A to dephosphorylate hundreds of proteins is regulate

146 e positioned through the concerted action of PP2A-B55/SUR-6-regulated nuclear envelope-based dynein p

147 d abrogates the tumor suppressive actions of PP2A, thereby potentiating oncogenic signaling and reduc

148 osphatase, and determined that activation of PP2A and inhibition of mTOR synergistically increase apo

149 Knockout of FAM122A results in activation of PP2A-B55alpha, a phosphatase that dephosphorylates the W

150 on or a specific small-molecule activator of PP2A (SMAP) efficiently attenuates HCC tumorigenesis in

151 o Furthermore, a small-molecule activator of PP2A (SMAP) phenocopies restoration of wild-type PPP2R1A

152 ted that a novel small-molecule activator of PP2A, DT-061, selectively stabilizes a specific PP2A hol

153 first-in-class small-molecule activators of PP2A (SMAPs) in Burkitt lymphoma, KRAS-driven non-small

154 e iHAPs (improved heterocyclic activators of PP2A) that kill leukemia cells by allosterically assembl

155 erapeutics, but small-molecule activators of PP2A, the phosphatase that regulates MYC Ser62 phosphory

156 LKB1 activation, due to enhanced activity of PP2A, the upstream phosphatase of AMPK.

157 Protein expression analysis of PP2A family members revealed that the Aalpha deletion ma

158 Antagonism of PP2A by HIV-1 Vif is therefore independent of APOBEC3 fa

159 Binding of PP2A-B56 to ADAM17 protease decreases growth factor sign

160 uggest that the PP2A holoenzyme, composed of PP2A-Abeta, PP2A-B56gamma, and PP2ACalpha subunits, is s

161 Small T antigen (ST) or mutation/deletion of PP2A subunits alters the abundance and types of PP2A com

162 sequent decrease in the dephosphorylation of PP2A-B55 substrates promoted mitotic entry.

163 Enhancement of PP2A activity prevented chronic smoke-induced COPD in mi

164 redundancy and high endogenous expression of PP2A holoenzymes, traditional approaches of overexpressi

165 We extend the molecular functionality of PP2A-B'gamma to a protein kinase-phosphatase interaction

166 egies for global substrate identification of PP2A-B56 and PP2A-B55 holoenzymes.

167 d cells to evaluate the functional impact of PP2A across diverse cellular pathways targeted by these

168 g is the key target of CTD, independently of PP2A and PP1 activities.

169 gulation was conferred by Pak2 inhibition of PP2A (protein phosphatase 2A) activity.

170 ed by pressure overload, while inhibition of PP2A signaling prevents eccentric cardiac remodeling ind

171 Here, we report that Sds23, an inhibitor of PP2A family protein phosphatases, promotes the symmetric

172 range of human cancers, and partial loss of PP2A function contributes to cell transformation.

173 lation has been less clear, although loss of PP2A in yeast causes defects in cytokinesis.

174 enzyme and highlight inherent mechanisms of PP2A complex assembly.

175 als were administered chemical modulators of PP2A (protein phosphatase 2A) activity.

176 Only a limited number of PP2A-regulated phosphorylation sites are known.

177 h enhanced the inhibitory phosphorylation of PP2A by Src.

178 ruitment, essential for recruiting a pool of PP2A involved in chromosome congression during meiosis I

179 now demonstrate that the BUBR1-bound pool of PP2A-B56 regulates MPS1 T-loop autophosphorylation and h

180 olecule-mediated therapeutic reactivation of PP2A significantly inhibited tumorigenicity in vivo.

181 Akt (p-Akt) and promotes the recruitment of PP2A to dephosphorylate p-Akt, and this scaffolding effe

182 ld-type Aalpha, suggesting a rededication of PP2A functions.

183 Removal of PP2A-B55/SUR-6 and the nuclear lamina simultaneously fur

184 nal simulations predicted the requirement of PP2A-B55/SUR-6 regulation of nuclear size and nuclear-en

185 Therefore, the role of PP2A in C. elegans female meiosis is unknown.

186 on potentials revealed an unexpected role of PP2A in I(Na,L) regulation that was confirmed by direct

187 offer what we believe is a novel strategy of PP2A reactivation for treatment of PNETs as well as othe

188 ides insight into the druggable structure of PP2A, guiding future phosphatase therapeutics.

189 of a positively charged motif in a subset of PP2A:B56 interactors, including KIF4A, to facilitate B56

190 tivate PP2A) or the scaffolding A-subunit of PP2A (PPP2R1A) (to inhibit PP2A) in HeLa cells.

191 ers the activity of the catalytic subunit of PP2A, shifting the balance of Gcn4 toward a dephosphoryl

192 udies demonstrate that combined targeting of PP2A and mTOR suppresses proliferative signaling and ind

193 A subunits alters the abundance and types of PP2A complexes in cells, leading to transformation.

194 ly understood, limiting our understanding of PP2A-regulated signaling.

195 in vessel remodeling and suggest the use of PP2A-inhibitors as potent antiangiogenic drugs targeting

196 e most commonly mutated residue, Arg-183, on PP2A function have yet to be fully elucidated.

197 Cancer cells were dependent on PP2A disruption for sustained tumorigenic potential, and

198 the impact of the P179R missense mutation on PP2A function.

199 ation; dephosphorylation then commences once PP2A-B55 spikes in activity.

200 ) and the protein phosphatase 1 (PP1) and/or PP2A.

201 lated to ROS induction, copper chelation, or PP2A activation.

202 erexpressing, knocking down, or knocking out PP2A regulatory subunits have yielded only limited insig

203 nsistently, systemic administration of a pan-PP2A inhibitor disrupts vascular network formation and t

204 e most mitotic proteins, because of parallel PP2A:B55 phosphatase inactivation by Greatwall kinase.

205 ulatory subunits of key cellular phosphatase PP2A (PPP2R5A-E; Greenwood et al., 2016; Naamati et al.,

206 acts that the Cdk1-counteracting phosphatase PP2A-B55 functions as a bistable switch, even when the b

207 t CDK1-CCNB1 and a counteracting phosphatase PP2A-B55 regulate the engagement of human MPS1 with unat

208 lation of the Cdk1-counteracting phosphatase PP2A-B55.

209 ignaling and supports a role for phosphatase PP2A, but also suggests Sav1 has functions in addition t

210 loss of methylation of the major phosphatase PP2A in response to methionine starvation activates the

211 conserved heterotrimeric protein phosphatase PP2A controls the timing of events in mitosis, and upstr

212 ltransferase Ppm1 via its target phosphatase PP2A to selectively stabilize Gcn4.

213 on the catalytic subunit of the phosphatase PP2A, which disrupted its holoenzyme formation with the

214 tions involving serine-threonine phosphatase PP2A subunits occur in a range of human cancers, and par

215 Type 2A protein phosphatases (PP2As) are highly expressed in the brain and regulate ne

216 ed by the main cardiac protein phosphatases, PP2A and PP1.

217 ble signaling networks, such as the GNAS/PKA/PP2A axis in SCLC.

218 essed ARPP19 and ENSA turns them into potent PP2A-B55 inhibitors.

219 st that PKA-mediated phosphorylation and PP1/PP2A-dependent dephosphorylation of the alpha2 subunit p

220 tin at anaphase)-associated phosphatases PP1/PP2A.

221 analogues were synthesized, and preliminary PP2A enzyme assay inhibition studies were performed for

222 We propose PP2A-B'gamma age-dependently controls salicylic acid-rel

223 nnexin 43 (Cx43) and gated by cAMP-EPAC-RAP1-PP2A signaling.

224 tion of CIP2A, PME-1, and SET (to reactivate PP2A) or the scaffolding A-subunit of PP2A (PPP2R1A) (to

225 ibiting Akt activity or through reactivating PP2A may be a potential therapeutic approach for HCC tre

226 ry subunit B55alpha as the factor recruiting PP2A to PDE4D5.

227 BUB-1 recruits PP2A:B56 to the chromosomes via a newly identified LxxIx

228 ne 27-linked ubiquitination of BRAF recruits PP2A to antagonize the S365 phosphorylation and disrupts

229 es elucidates the role of a highly recurrent PP2A-Aalpha-subunit mutation PPP2R1A P179R as a biologic

230 se (PGLS), the second oxiPPP enzyme, reduced PP2A activity.

231 impairing holoenzyme formation and reducing PP2A phosphatase activity to promote endometrial cancer

232 m pathways including Greatwall-Ensa regulate PP2A activity.

233 In addition, Cdk1 regulates PP2A-B55 in a biphasic manner; low concentrations of Cdk

234 and show that the STRIPAK complex regulates PP2A specificity and activity.

235 e of this incoherent feedforward regulation, PP2A-B55 activity rises concurrently with Cdk1 activity

236 ditionally, we show that during replication, PP2A exists in complex with cell division cycle 45 (CDC4

237 This mechanical transition required PP2A phosphatase and correlated with inactivation of PLK

238 duced mitotic catastrophe that also requires PP2A.IMPORTANCE UNC5B, PP2A, and netrin-1 are deregulate

239 sm for the attenuation of the inhibitory SET-PP2A interaction.

240 oligomerization and the formation of the SET-PP2A inhibitory complex, leading to resistance to FTY720

241 ting in expression of predominantly a single PP2A heterotrimer composed of the A/B charge-swap pair a

242 A, DT-061, selectively stabilizes a specific PP2A holoenzyme responsible for dephosphorylating critic

243 lysis revealed increased binding of specific PP2A regulatory subunits to Abeta, and knockdown of thes

244 henothiazine derivatives reactivate specific PP2A isozymes with potential benefit in cancer and other

245 is associated with ST and is required for ST-PP2A-induced cell transformation.

246 development, and the PP2A regulatory subunit PP2A-B'gamma is required for negative regulation of path

247 holoenzyme comprises a scaffolding subunit (PP2A Aalpha/beta), which serves as the platform for bind

248 eads to the reactivation of tumor suppressor PP2A.

249 t binds recombinant GSH S-transferase-tagged PP2A-B55alpha.

250 its interaction with PP2A-B55alpha and that PP2A-B55alpha dephosphorylates phospho-Ser(315) Spreadin

251 hes to modulate PP2A activity, we found that PP2A regulates DNA replication.

252 hanced activation of pSTAT5, indicating that PP2A promotes IL-2R signaling through multiple mechanism

253 Starting from our previous observations that PP2A (protein phosphatase 2) regulates the HIF (hypoxia-

254 We report that PP2A is essential for meiotic spindle assembly and chrom

255 Using B'delta/PPP2R5D, we show that PP2A complexity reduction, but not PP2A overexpression,

256 tion of genomic alterations, suggesting that PP2A regulates ongoing replication as a mechanism for ma

257 2A-B56(delta) functionality, suggesting that PP2A-related neurodevelopmental disorders constitute fun

258 The PP2A complex activated by iHAP1 dephosphorylates the MYB

259 The PP2A complex STRIPAK(SLMAP) blocks MST1/2 activation.

260 Borealin and the PP2A phosphatase complex can bind simultaneously to the

261 fferent stages of plant development, and the PP2A regulatory subunit PP2A-B'gamma is required for neg

262 pistatic to PPP2R2A, a gene that encodes the PP2A B55alpha subunit, which we show interacts with IER5

263 mutations in PPP2R1A, the gene encoding the PP2A Aalpha scaffolding subunit, have been identified ac

264 nding to the gamma subunits and enhances the PP2A-mediated de-phosphorylation, but it impedes the LKB

265 ding B/R2, B'/R5, and B"/R3), which form the PP2A heterotrimeric holoenzyme by associating with a dim

266 Proteomics identified the PP2A regulatory subunit B55alpha as the factor recruitin

267 These results identify the PP2A regulatory network as a critical component in the s

268 veal that in response to ETC impairment, the PP2A complex generates a dephosphorylated, mitochondrial

269 that individuals harboring mutations in the PP2A Aalpha gene have a higher fraction of genomic alter

270 Mutants lacking the PP2A methyltransferase or the effector H3K36 demethylase

271 Overexpression of the PP2A catalytic subunit (PP2Ac) by lentiviral transductio

272 the dephosphorylation site preference of the PP2A catalytic subunit, resulting in unique patterns of

273 Members of the PP2A family of serine/threonine phosphatases are importa

274 The absence of Ppm1 or the loss of the PP2A methylation destabilizes Gcn4 even when methionine

275 iously that transgenic overexpression of the PP2A methylesterase, PME-1, or the PP2A methyltransferas

276 enetically reducing endogenous levels of the PP2A methylesterase, PME-1, prevents the cognitive and e

277 onversely, reducing endogenous levels of the PP2A methyltransferase, LCMT-1, increases sensitivity to

278 y, or pharmacologically by activation of the PP2A phosphatase, suppresses SCLC expansion in culture a

279 identifies RABL6A as a new inhibitor of the PP2A tumor suppressor and an essential activator of AKT

280 ew interacting and substrate proteins of the PP2A-B55alpha holoenzyme in bovine pulmonary endothelial

281 rylate FAM122A, leading to activation of the PP2A-B55alpha phosphatase and increased WEE1 expression.

282 on of the PP2A methylesterase, PME-1, or the PP2A methyltransferase, LCMT-1, altered the sensitivity

283 combined with global phosphoproteomics, the PP2A/B'delta reduction approach identified consensus dep

284 interaction also unexpectedly stabilized the PP2A-B55alpha complex.

285 Our data also suggest that the PP2A holoenzyme, composed of PP2A-Abeta, PP2A-B56gamma,

286 We show that the PP2A regulatory subunit B55alpha is at the crossroad bet

287 These results indicate that the PP2A-flotillin-1 interaction identified here affects maj

288 Binding to the PP2A catalytic subunit was significantly impaired, disru

289 Therefore, PP2A directs the methylation status of histones by regul

290 ar interactions between DT-061 and all three PP2A subunits that prevent dissociation of the active en

291 In presenescent leaf tissues, PP2A-B'gamma is also required to negatively control the

292 he that also requires PP2A.IMPORTANCE UNC5B, PP2A, and netrin-1 are deregulated in a variety of cance

293 Various PP2A-associated downstream effector proteins in the pres

294 o2 up-regulates Aurora B kinase activity via PP2A inhibition in prometaphase.

295 during metaphase hyperactivates Aurora B via PP2A inhibition, and thereby rescues the feedback loop.

296 imarily dephosphorylated threonines, whereas PP2A reactivation results in dephosphorylation of cluste

297 er, our results uncover a mechanism by which PP2A Aalpha regulates Abeta protein stability and activi

298 ere, we report molecular mechanisms by which PP2A-B'gamma regulates Botrytis cinerea resistance and l

299 1 significantly affects its interaction with PP2A-B55alpha and that PP2A-B55alpha dephosphorylates ph

300 is regulated by the interaction of PyST with PP2A.