ライフサイエンスコーパス: ASK1

1 ASK1 directly phosphorylates Daxx at Ser(176) and Ser(18

2 ASK1 forms a high molecular mass complex whose activity

3 ASK1 is a central mediator of oxidant injury, but while

4 ASK1 is essential for the assembly and function of the I

5 ASK1 knockdown in C17.2 neural stem cells diminished hig

6 ASK1 participated in the IRE1alpha signalosome, and remo

7 ASK1 phosphorylation of Daxx, an ASK1 activator protein,

8 ASK1 transgenic mice exhibited no induction of cardiac h

9 ASK1 variants may increase susceptibility to type 2 diab

10 ASK1-interacting protein-1 (AIP1), a recently identified

11 ASK1-TBD is a monomeric and rigid domain that forms a st

12 lating apoptosis signal-regulating kinase 1 (ASK1) activity and subsequent ASK1-dependent apoptosis.

13 luding apoptosis signal-regulating kinase 1 (ASK1) and cyclic AMP (cAMP) response element-binding pro

14 O, via Apoptosis Signal-regulating Kinase 1 (ASK1) and Jun-N-terminal Kinase (JNK).

15 hrough apoptosis signal-regulating kinase 1 (ASK1) and MAKK4 (SEK1) upstream from JNK was caffeine se

16 d with apoptosis signal-regulating kinase 1 (ASK1) and thereby inhibited the MPP(+)-induced stimulati

17 tified apoptosis signal-regulating kinase 1 (ASK1) as a critical downstream target of HSP27 conferrin

18 w that apoptosis signal-regulating kinase 1 (ASK1) contributes to apoptosis of plasma cells because A

19 ion of apoptosis signal-regulating kinase 1 (ASK1) in hepatocytes is a key process in the progression

20 ion of apoptosis signal-regulating kinase 1 (ASK1) induced by inhibition of mTOR signaling leads to s

21 teine, apoptosis signal-regulating kinase 1 (ASK1) inhibitor thioredoxin, and c-Jun NH2-terminal kina

22 Apoptosis signal-regulating kinase 1 (ASK1) is a key regulatory kinase in the proapoptotic res

23 Apoptosis signal-regulating kinase 1 (ASK1) is a Mitogen-Activated Protein Kinase Kinase Kinas

24 Apoptosis signal-regulating kinase 1 (ASK1) is a serine/threonine kinase that responds to a pl

25 Apoptosis signal-regulating kinase 1 (ASK1) is activated by various stresses.

26 e that apoptosis signal regulating kinase 1 (ASK1) may influence in vivo insulin action in Pima India

27 d that apoptosis signal-regulating kinase 1 (ASK1) regulates the late phase of APAP-induced JNK activ

28 in for apoptosis signal-regulating kinase 1 (ASK1) which activates c-Jun NH2-terminal kinase (JNK) an

29 nus of apoptosis signal-regulating kinase 1 (ASK1), a kinase believed to be involved in the pathogene

30 Apoptosis signaling kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase,

31 Apoptosis signal-regulating kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase,

32 PAK1), apoptosis signal-regulating kinase 1 (ASK1), and polo-like kinase 3 (PLK3).

33 K) and apoptosis signal-regulating kinase 1 (ASK1), unveiling a critical node at the junction of surv

34 own as apoptosis signal-regulating kinase 1 (ASK1).

35 Apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5), a member of the mitogen-act

36 by an apoptosis signal-regulating kinase 1 (ASK1; MAPKKK) inhibitor and by a p38 inhibitor, indicati

37 while apoptosis signal regulating kinase-1 (ASK1) dissociated from the complex.

38 h at the level of apoptotic signal kinase-1 (ASK1) within the IRE1 pathway but without directly inhib

39 CaMKII, TIR-1/SARM adaptor protein and NSY-1/ASK1 MAPKKK, is localized to postsynaptic sites in the A

40 timulation promotes the formation of a Raf-1/ASK1 complex at the mitochondria, inhibits ASK1 kinase a

41 n domain (SS338/9AA) not only prevents Raf-1/ASK1 complex formation but abolishes bFGF-mediated EC pr

42 ne the linkage disequilibrium pattern across ASK1 in Pima Indians.

43 and that accumulated Daxx further activates ASK1.

44 esults indicate that Daxx not only activates ASK1 but also is a downstream target of ASK1 and that ac

45 endoplasmic reticulum (ER) stress activates ASK1-JNK signaling cascade, we investigated the role of

46 independent apoptosis pathway by activating ASK1, JNK, and caspase-3.

47 ed with dominant negative constructs against ASK1, and pharmacologic inhibition of JNK with SP600125

48 is essential for TNF-induced TRAF2-RIP1-AIP1-ASK1 complex formation and for the activation of ASK1-JN

49 Formation of the G alpha13-ASK1 complex was enhanced by JNK-interacting leucine zip

50 Although ASK1 overexpression did not alter the cardiac hypertroph

51 ASK1 phosphorylation of Daxx, an ASK1 activator protein, increases Daxx accumulation in c

52 ccumulation and enhanced inflammation, in an ASK1-dependent manner.

53 on of S58 releases ASK1 from 14-3-3zeta, and ASK1 then activates stress-activated protein kinases, le

54 pression resulted in PI3K-Akt activation and ASK1-JNK inactivation leading to accelerated PCa growth

55 proteins stimulate ASK1 kinase activity and ASK1-dependent apoptosis.

56 comitantly down-regulated both G alpha13 and ASK1.

57 zed in 536 nondiabetic Native Americans, and ASK1 expression was examined in skeletal muscle of 153 n

58 ma enhanced the association between JAK2 and ASK1, and the ASK1-JAK2 complex was labile and was stabi

59 ed key arrestin-binding elements in JNK3 and ASK1 and investigated the molecular interactions of arre

60 rate arrestins interact with JNK3, MKK4, and ASK1, but only arrestin3 facilitates JNK3 activation.

61 eviously shown to bind JNK3alpha2, MKK4, and ASK1.

62 that this peptide also binds MKK4, MKK7, and ASK1, which are upstream JNK3-activating kinases.

63 Our results also suggest that PRX2 and ASK1 may be potential targets for neuroprotective interv

64 proteins upon OTA treatment in scrambled and ASK1 knockdown cells, respectively.

65 on of the MAP2K MEK6 by two MAP3Ks, TAO2 and ASK1, and the subsequent phosphorylation of p38alpha by

66 pendent manner to block DAXX trafficking and ASK1-JNK activation.

67 rization of the TRX1-binding domain of ASK1 (ASK1-TBD) and its complex with reduced TRX1.

68 inding to ASK1, while phospho-S83 attenuates ASK1 substrate MKK6 binding.

69 ributes to apoptosis of plasma cells because ASK1 activity was induced during differentiation of shor

70 CR identified a positive correlation between ASK1 expression in skeletal muscle biopsies and in vivo

71 The link between ASK1 activation and endoplasmic reticulum (ER) stress, t

72 und that the KNC mutant, which tightly binds ASK1, MKK4, and JNK3 without facilitating JNK3 phosphory

73 for the first time ARC-DAXX binding to block ASK1-JNK activation as an ARC-specific endogenous mechan

74 PTP/MPP(+)-induced neurotoxicity by blocking ASK1-mediated signaling.

75 Because both ASK1 and ANP are associated with pathologic cardiac hype

76 ival in normal and malignant plasma cells by ASK1.

77 ocessivity in the phosphorylation of MEK6 by ASK1, and suggested that the order of phosphorylation is

78 n of p21(Cip1), predominantly carried out by ASK1, is associated with binding to ASK1 and inactivatio

79 rt-lived plasma cells, and, when produced by ASK1-deficient mice, these cells survived better than th

80 am regulatory kinase of the MKK/JNK cascade, ASK1, Hsp27 effectively inhibited ASK1 activity via a ph

81 ith the components of the two MAPK cascades, ASK1-MKK4-JNK3 and c-Raf-1-MEK1-ERK2.

82 When expressed in HEK293T cells, ASK1 was reproducibly purified within a high-molecular m

83 py shows that, when expressed in Hela cells, ASK1 and NPPA exhibit distinct, but overlapping, stainin

84 In malignant plasma cells, ASK1 transcription was directly suppressed by B lymphocy

85 t accumulation and interaction with cellular ASK1.

86 nctionally, TAT.ARC treatment inhibited DAXX-ASK1-JNK signaling in the ischemic brain.

87 Thus, the Daxx-ASK1 positive feedback loop amplifying JNK/p38 signaling

88 t wounded rat ATII cells exhibited decreased ASK1 phosphorylation at Serine-966, decreased serine pho

89 ression in HK-2 cells successfully decreased ASK1, which was confirmed by Western blot analysis.

90 directly interacts with and deubiquitinates ASK1 in hepatocytes.

91 Knocking down ASK1 inhibits ionomycin-induced p38 phosphorylation and

92 was neuroprotective and inhibited downstream ASK1 signaling pathways.

93 odulating the redox status of the endogenous ASK1 inhibitor thioredoxin (Trx).

94 an suppress the PI3K-Akt pathway and enhance ASK1 activation leading to cell apoptosis, whereas loss

95 4-3-3 release from ASK1, leading to enhanced ASK1-JNK signaling.

96 thioredoxin binding protein, which enhanced ASK1 activation by disrupting the thioredoxin-ASK1 compl

97 x accumulation in cells and further enhances ASK1 activity through a positive feedback mechanism.

98 xx deficient in polyubiquitin still exhibits ASK1-dependent accumulation and interaction with cellula

99 ckstrin homology domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding

100 que molecular complex comprising CXCR4, FAK, ASK1, and PP5 in ATII cells during wound healing.

101 ducing Trx2 binding to ASK1 and allowing for ASK1 phosphorylation/activation, resulting in induction

102 in and an intact TPR region are required for ASK1 activity.

103 However, the phosphatase(s) responsible for ASK1 dephosphorylation at pSer967 has not been identifie

104 e findings demonstrate an essential role for ASK1 in cell death induced by ER stress.

105 ative stress, suggesting a possible role for ASK1 in diabetic nephropathy.

106 K2 S964A-induced dissociation of 14-3-3 from ASK1 correlated with enhanced phosphorylation of ASK1 at

107 ge, thereby preventing its dissociation from ASK1.

108 Murine embryonic fibroblasts from ASK1 knock-out mice, alveolar epithelial cells transfect

109 on was increased in ATII cells isolated from ASK1 knockout mice.

110 pSer967 and subsequently 14-3-3 release from ASK1, leading to enhanced ASK1-JNK signaling.

111 ally inactive mutant, dissociated SOCS1 from ASK1.

112 In conclusion, this study identifies ASK1 as a new therapeutic target in diabetic nephropathy

113 lvement of ASK1 in diverse diseases, the IKK/ASK1 interface offers a promising target for therapeutic

114 lls generated by immunization accumulated in ASK1-deficient mice, suggesting ASK1 also plays a negati

115 ddition to the critical role of C2 domain in ASK1 activity, are important for modulating PI3K-Akt act

116 mediated by a MAP kinase cascade, including ASK1 and c-Jun N-terminal kinase.

117 itutively activated G alpha13Q226L increased ASK1 expression.

118 gest that oxidative stress rapidly increases ASK1 catalytic efficiency for MKK6 phosphorylation by in

119 Indeed, ASK1 transgenic mice showed a greater than 2-fold increa

120 P1) transduces tumor necrosis factor-induced ASK1-JNK signaling.

121 IFN-gamma-induced ASK1 Tyr(P)-718 was enhanced in mouse EC deficient in SH

122 PRX2 inhibited 6-OHDA-induced ASK1 activation by modulating the redox status of the en

123 d the regulation of oxidative stress-induced ASK1-catalyzed phosphorylation of MKK6.

124 active mutant of SHP2 inhibited, TNF-induced ASK1 dephosphorylation.

125 AIP1 at Ser604, are critical for TNF-induced ASK1 dephosphorylation.

126 s-induced, but not oxidative stress-induced, ASK1-JNK activation and cell apoptosis.

127 K cascade, ASK1, Hsp27 effectively inhibited ASK1 activity via a physical association through its N-t

128 1 phosphorylation of ASK1 on Ser83 inhibited ASK1-mediated c-Jun N-terminal kinase phosphorylation as

129 1/ASK1 complex at the mitochondria, inhibits ASK1 kinase activity, and protects ECs from genotoxic st

130 provide evidence to show that RSK2 inhibits ASK1 by phosphorylating S83, T1109, and T1326 through a

131 ineage kinase 3 (MLK3) mediates the initial, ASK1-independent phase of APAP-induced JNK activation an

132 Moreover, depletion of intracellular ASK1 reduces the level of AGP-induced oxidative stress a

133 -stress-induced cell death via the IRE1alpha-ASK1-JNK pathway.

134 egulatory region actively primes MKK6, a key ASK1 substrate, for phosphorylation.

135 d activation of the oxidant-sensitive kinase ASK1 and its downstream kinase JNK.

136 ssion of apoptosis signal-regulating kinase (ASK1)-dependent activation of the c-Jun N-terminal kinas

137 inactivation of apoptosis-stimulated kinase (ASK1)-JNK pathways is often detected.

138 e regulation of the stress-activated kinase, ASK1.

139 ct cells upon expression of upstream kinases ASK1, MKK4, or MKK7.

140 Apoptosis signal-regulating kinases (ASK1-3) are apical kinases of the p38 and JNK MAP kinase

141 nsgene driven by the ARABIDOPSIS SKP1-LIKE1 (ASK1) promoter and the other CYCA1;2/TAM-GFP driven by t

142 lele for rs1570056 was associated with lower ASK1 expression (P = 0.003, r = -0.22).

143 nhibits the MAP kinase kinase kinase Map3k5 (ASK1) is upstream of JNK1 activation.

144 In contrast, proteins modulating ASK1 activity and degradation were found to interact wit

145 Genetic variants in or near ASK1 were analyzed to assess the role of this gene in in

146 reviously we have shown that tyrosine 718 of ASK1 when phosphorylated is critical for SOCS1 binding a

147 ds enhanced phosphorylation of serine 967 of ASK1, promoting ASK1 binding to 14-3-3, an event associa

148 ll death through IRE1-mediated activation of ASK1 and possibly downstream caspases.

149 In turn, activation of ASK1 is associated with a number of human pathological c

150 eine also inhibits AGP-induced activation of ASK1, as well as apoptosis.

151 results in an increase in the activation of ASK1, JNK, and caspase 3 along with exacerbation of 4-HN

152 deficient Jurkat cells via the activation of ASK1, JNK, and caspase 3, and the apoptosis can be inhib

153 xx and inhibits Daxx-dependent activation of ASK1, prevents Daxx phosphorylation and stabilization.

154 2A-AIP1 complex in TNF-induced activation of ASK1-JNK apoptotic signaling.

155 and AIP1 cooperatively induce activation of ASK1-JNK signaling and EC apoptosis, as demonstrated by

156 tion of ASK1 at Tyr(P)-718 and activation of ASK1-JNK signaling, as well as EC apoptosis, are signifi

157 complex formation and for the activation of ASK1-JNK/p38 apoptotic signaling.

158 with TRAF2-ASK1 that leads to activation of ASK1-JNK/p38 signaling in endothelial cells (EC).

159 y in renal epithelial cells by activation of ASK1.

160 ctor-alpha (TNF-alpha)-induced activation of ASK1.

161 The activity of ASK1 is triggered by various stress stimuli and is invol

162 t directly inhibiting the kinase activity of ASK1 or >400 other kinases tested.

163 ronounced when a dominant-negative allele of ASK1 with deficient kinase activity was coexpressed with

164 aft animal model; furthermore, alteration of ASK1 activity affected MM cell survival.

165 n of ASK2 dramatically reduced the amount of ASK1 complexed with 14-3-3.

166 r-718, leading to an enhanced association of ASK1 with SOCS1 and subsequent ASK1 degradation.

167 Importantly, the strength of the binding of ASK1 or JNK3, as revealed by the efficiency of co-immuno

168 a dominant role of ASK2 in 14-3-3 control of ASK1 function.

169 ron-gamma (IFN-gamma) induced degradation of ASK1 in normal but not in SOCS1-KO endothelial cells (EC

170 S1 binding and SOCS1-mediated degradation of ASK1.

171 The evidence for TNF-signaling dependence of ASK1-mediated apoptosis suggests possible mechanisms for

172 ein family, facilitates dephosphorylation of ASK1 at pSer967 and subsequently 14-3-3 release from ASK

173 necrosis factor-induced dephosphorylation of ASK1 at Tyr(P)-718 and activation of ASK1-JNK signaling,

174 for phosphorylation and dephosphorylation of ASK1 at Tyr-718 are unknown.

175 talytic subunit induced dephosphorylation of ASK1 pSer967 and activation of c-Jun N-terminal kinase (

176 RNA blunted TNF-induced dephosphorylation of ASK1 pSer967 and activation of JNK without effects on NF

177 is factor (TNF)-induced dephosphorylation of ASK1 pSer967 in ECs was blocked by PP2A inhibitor okadai

178 K and CXCR4 were increased upon depletion of ASK1 using shRNA in MLE-12 cells, but unaffected when PP

179 aracterization of the TRX1-binding domain of ASK1 (ASK1-TBD) and its complex with reduced TRX1.

180 -3-3zeta interacts with the kinase domain of ASK1 in close proximity to its active site, thus indicat

181 s N-terminal domain and the kinase domain of ASK1.

182 The expression of ASK1 and Blimp-1 showed an inverse correlation between n

183 ells), and induction of Bax in the hearts of ASK1 transgenic mice following 1 and 8 weeks of pressure

184 ted with binding to ASK1 and inactivation of ASK1 kinase function.

185 Incubation of ASK1-depleted HK-2 cells with the two FLCs prevented the

186 o prevented by pharmacological inhibition of ASK1 (apoptosis signal-regulating kinase 1) or of c-Jun

187 Finally, the inhibition of ASK1 by Akt was responsible for the protection from apop

188 The role of 14-3-3 in the inhibition of ASK1 has yet to be elucidated.

189 sly unexplored association and inhibition of ASK1 kinase signaling.

190 ll as the interaction with and inhibition of ASK1 signaling.

191 this study, we performed RNA interference of ASK1 in HEK293 cells and employed an iTRAQ-based quantit

192 Because of the intimate involvement of ASK1 in diverse diseases, the IKK/ASK1 interface offers

193 Moreover, knockdown of ASK1 or inhibition of the ASK1/MKK4 cascade effectively

194 at the catalytic efficiency (k(cat)/K(m)) of ASK1 was 4000-fold greater in cells treated with H(2)O(2

195 ally investigate the regulatory mechanism of ASK1 in OTA-induced renal cytotoxicity.

196 lthough a 14-3-3-binding defective mutant of ASK1 (S967A) has no effect on the ASK2/14-3-3 interactio

197 iac-specific and inducible overexpression of ASK1 in the heart to assess its gain-of-function effect.

198 correlated with enhanced phosphorylation of ASK1 at T838 and increased c-Jun N-terminal kinase phosp

199 ime-dependent increase in phosphorylation of ASK1 at T845, indicating activation of this enzyme, was

200 FN-gamma-induced tyrosine phosphorylation of ASK1 at Tyr-718 was blocked by a JAK2-specific inhibitor

201 Direct phosphorylation of ASK1 by IKK also defines a novel IKK phosphorylation mot

202 her demonstrate that PIM1 phosphorylation of ASK1 decreases its kinase activity induced by oxidative

203 PIM1 phosphorylation of ASK1 on Ser83 inhibited ASK1-mediated c-Jun N-terminal k

204 that regulate inhibitory phosphorylation of ASK1.

205 sphorylation, the two biological readouts of ASK1 activation.

206 eased phosphorylation of endogenous Ser83 of ASK1 and was associated with a decrease in cell viabilit

207 l a compact and slightly asymmetric shape of ASK1-TBD and suggest reduced TRX1 interacts with this do

208 We demonstrated that NPPA is a substrate of ASK1 in an in vitro kinase assay.

209 iated phosphorylation for its suppression of ASK1 cell death signaling and neuroprotection against is

210 3-3, an event associated with suppression of ASK1 function.

211 Suppression of ASK1 is crucial for cell survival because its enforced e

212 (TNFAIP3) as a key endogenous suppressor of ASK1 activation, and we found that TNFAIP3 directly inte

213 ctionally important endogenous suppressor of ASK1 hyperactivation in the pathogenesis of NASH and ide

214 ates ASK1 but also is a downstream target of ASK1 and that accumulated Daxx further activates ASK1.

215 ulator of S58 phosphorylation and thereby of ASK1-mediated cell death.

216 -regulation of Thioredoxin (Trx)-1 to permit ASK1 activation and apoptosis.

217 t JAK1, directly bound to and phosphorylated ASK1 at Tyr-718, leading to an enhanced association of A

218 and decreased association of phosphorylated ASK1 with FAK.

219 ormed a complex with tyrosine-phosphorylated ASK1, suggesting that ASK1 is a direct SHP2 substrate.

220 IKK forms a complex with and phosphorylates ASK1 at a sensor site, Ser967, leading to the recruitmen

221 Here we show that PIM1 phosphorylates ASK1 specifically on serine residue 83 (Ser83) both in v

222 the ability of arrestin proteins to promote ASK1-dependent JNK3 phosphorylation.

223 which the central regulatory region promotes ASK1 activity via its pleckstrin homology domain but als

224 phorylation of serine 967 of ASK1, promoting ASK1 binding to 14-3-3, an event associated with suppres

225 uppressor of kinetochore protein 1) protein, ASK1 and ASK2, are required for Agrobacterium-mediated p

226 independent of the Arabidopsis SKP1 protein, ASK1.

227 Groups of diabetic Nos3(-/-) mice received ASK1 inhibitor (GS-444217 delivered in chow) as an early

228 Small interfering RNA designed to reduce ASK1 expression in HK-2 cells successfully decreased ASK

229 y decreasing insulin sensitivity via reduced ASK1 expression.

230 Reducing ASK1 protein expression using small interfering RNA also

231 at JAK2-SOCS1 and SHP2 reciprocally regulate ASK1 phosphorylation and stability in response to cytoki

232 ings identify a novel pathway that regulates ASK1 activation and oxidant stress-induced cell death.

233 Phosphorylation of S58 releases ASK1 from 14-3-3zeta, and ASK1 then activates stress-act

234 d in the IRE1alpha signalosome, and removing ASK1 abrogated the proapoptotic kinase activity of IRE1a

235 this study, we examined whether a selective ASK1 inhibitor can prevent the induction and progression

236 occur through PAR1, reactive oxygen species, ASK1, and JNK signaling in HGFs.

237 ngagement with Sdc1 is blocked by SSTNIGF1R, ASK1 becomes activated, and initiates JNK- and caspase-3

238 as involving sequential TRAF3 stabilisation, ASK1 phosphorylation, MKK4 (but not MKK7) activation and

239 eterotrimeric G12 and G13 proteins stimulate ASK1 kinase activity and ASK1-dependent apoptosis.

240 In response to oxidative stress, ASK1 activates the cell death-associated p38 MAPK pathwa

241 ssociation of ASK1 with SOCS1 and subsequent ASK1 degradation.

242 ting kinase 1 (ASK1) activity and subsequent ASK1-dependent apoptosis.

243 ed MAX2 interacts with the core SCF subunits ASK1 and AtCUL1 in planta.

244 cumulated in ASK1-deficient mice, suggesting ASK1 also plays a negative role in survival of long-live

245 al-triggered ASK1 activation, and suppresses ASK1-mediated functions.

246 the IGF1 receptor (IGF1R) by Sdc1 suppresses ASK1-dependent apoptosis in multiple myeloma cells.

247 We concluded that ASK1 plays an essential role in promoting OTA-induced re

248 , which further supports our hypothesis that ASK1 plays a causal role in diabetes-induced ER stress a

249 These results indicate that ASK1 does not directly regulate the cardiac hypertrophic

250 ay classification and analysis revealed that ASK1 participated in OTA-induced inhibition of mRNA spli

251 However, the role that ASK1 plays in regulating the cardiac hypertrophic respon

252 Mechanistically, we show that ASK1 is bound to active IGF1R and inhibited by Tyr and S

253 Here, we show that ASK1-dependent phosphorylation of Daxx induces Lys(63) (

254 Our results showed that ASK1 knockdown alleviated OTA-induced ROS generation and

255 We have previously shown that ASK1-interacting protein 1 (AIP1) transduces tumor necro

256 Previously, we have shown that ASK1-interacting protein 1 (AIP1, also known as DAB2IP),

257 yrosine-phosphorylated ASK1, suggesting that ASK1 is a direct SHP2 substrate.

258 NPPA in the culture medium, suggesting that ASK1 negatively impacts NPPA processing and/or secretion

259 Reactive oxygen species then activated the ASK1-JNK/p38 pathways.

260 Here, we report that IFN-gamma activates the ASK1-MKK3/MKK6-p38 mitogen-activated protein kinase (MAP

261 e association between JAK2 and ASK1, and the ASK1-JAK2 complex was labile and was stabilized by the p

262 mplex ( approximately 1500 kDa) known as the ASK1 signalosome.

263 ructural analysis of the complex between the ASK1 kinase domain phosphorylated at Ser-966 (pASK1-CD)

264 iption-independent action in controlling the ASK1-JNK axis, coupling IKK to ROS and ER stress respons

265 On the other hand, the ASK1-p38 pathway induced expression of the monocyte chem

266 ere, we report a biochemical analysis of the ASK1 kinase domain in conjunction with its N-terminal th

267 osphorylated Ser-966 motif downstream of the ASK1 kinase domain.

268 ibited the MPP(+)-induced stimulation of the ASK1-mediated signaling cascade.

269 over, knockdown of ASK1 or inhibition of the ASK1/MKK4 cascade effectively inhibited cell death follo

270 3 and receptor-bound arrestin-3 scaffold the ASK1-MKK4-JNK3 module, promoting JNK3 phosphorylation, w

271 Furthermore, it occurs through the ASK1 pathway and is JNK- and p38-dependent.

272 nals couple ASK2 S964 phosphorylation to the ASK1 signalosome through dual engagement of 14-3-3.

273 degradation were found to interact with the ASK1 signalosome once MKK6 activation was completed.

274 tently, endogenous MKK6 was found within the ASK1 signalosome in intact cells and in addition copurif

275 increasing MKK6 binding affinity within the ASK1 signalosome prior to induction of inactivation and

276 SK1 activation by disrupting the thioredoxin-ASK1 complexes.

277 vate the intrinsic apoptotic pathway through ASK1, JNK, and p53.

278 ces the accumulation of Daxx protein through ASK1 activation by preventing its proteasome-dependent d

279 endent manners, in part by signaling through ASK1 and CREB, and contributes to cancer cell invasion a

280 rexpression or ING3 knockdown in addition to ASK1 knockdown further rescued the increased sensitivity

281 dizes Trx2, thereby reducing Trx2 binding to ASK1 and allowing for ASK1 phosphorylation/activation, r

282 d out by ASK1, is associated with binding to ASK1 and inactivation of ASK1 kinase function.

283 phospho-T1109/T1326 inhibits ATP binding to ASK1, while phospho-S83 attenuates ASK1 substrate MKK6 b

284 in vitro and in vivo and that PIM1 binds to ASK1 in cells by co-immunoprecipitation.

285 Whereas AIP1, via its C2 domain, binds to ASK1, PP2A binds to the GAP domain of AIP1.

286 pecific antibody, with a similar kinetics to ASK1-JNK/p38 activation.

287 critical role of AIP1 in recruiting PP2A to ASK1.

288 F), allowing it to form a complex with TRAF2-ASK1 that leads to activation of ASK1-JNK/p38 signaling

289 mally induces association of AIP1 with TRAF2-ASK1.

290 14-3-3, counteracts stress signal-triggered ASK1 activation, and suppresses ASK1-mediated functions.

291 vel redox-sensitive mitochondrial TXNIP-Trx2-ASK1 signaling cascade.

292 Additionally, coexpressing wild-type ASK1 with NPPA in Hela cells led to reduced levels of NP

293 However, the mechanism underlying ASK1 activation is still unclear, and thus the endogenou

294 We sought to investigate whether ASK1 is involved in the unfolded protein response (UPR)

295 SHP2 associated with ASK1 in response to tumor necrosis factor in EC.

296 hanistically, cardiomyopathy associated with ASK1 overexpression after 8 weeks of pressure overload w

297 intact cells and in addition copurified with ASK1 following treatment for 3 min.

298 In screening for proteins that interact with ASK1 in the context of NASH, we identified the deubiquit

299 r Daxx accumulation or Daxx interaction with ASK1 because mutant Daxx deficient in polyubiquitin stil

300 e, which forms a positive feedback loop with ASK1 through Txnip.

301 ermore, TNF-induced association of PP2A with ASK1 was diminished in AIP1-knockdown ECs, suggesting a

302 nduces a complex formation of AIP1-PP2A with ASK1.