ライフサイエンスコーパス: MyD88

1 s adaptor myeloid differentiation factor 88 (MyD88).

2 mutations altering the BCR subunit CD79B and MYD88.

3 ponse in mice lacking TIRAP, but not TLR2 or MyD88.

4 on of the IL-1R and IL-36R signaling adaptor Myd88.

5 ssors associated with acquisition of mutated MYD88.

6 LR signaling, and this interaction relies on MyD88.

7 receptor 2 (TLR-2) or depleting its mediator MyD88.

8 sponses observed were dependent, in part, on MyD88.

9 nd possibly other diseases driven by mutated MYD88.

10 K, is highly active in patients with mutated MYD88.

11 lise a critical interface between IRAK-4 and MyD88.

12 ll-like receptors (TLR9, TLR7) that activate MYD88.

13 nteraction of MAL with its downstream target MyD88.

14 with the human TLR adapter proteins MAL and MYD88.

15 ptor interacts with mTOR via the TLR adapter MyD88.

16 a high prevalence of activating mutations in MyD88 (91%) and CXCR4 (28%).

17 Commonly recurring mutations include MYD88 (95% to 97%), CXCR4 (30% to 40%), ARID1A (17%), an

18 n mice and humans, deficiencies of IRAK-4 or MyD88 abolish most TLR (except for TLR3 and some TLR4) a

19 MYD88 activity was directly regulated through lysine ace

20 ignals via a canonical pathway involving the MyD88 adapter and the interleukin-1 receptor-associated

21 pimod blocks cell-surface recruitment of the MyD88 adapter, one of the earliest events in TLR signali

22 secretion in glial cells depends on TLR2 and MyD88 adapter-like/TIRAP.

23 ignals via the appropriate receptors and the MyD88 adaptor protein.

24 MyD88 adaptor-like (MAL) is a critical protein in innate

25 TLR4 signaling relative to those mutated for MYD88 alone.

26 Here, we show that activation of MyD88 and Card9 signal pathways are required for resista

27 ts in human DLBCL samples revealed that both MYD88 and CD79B mutations are substantially enriched in

28 vide an explanation for the co-occurrence of MYD88 and CD79B mutations in lymphomas.

29 CCI induced up-regulation of MyD88 and chemokine C-C motif ligand 2 expression in DRG

30 MYD88 and CXCR4 mutation status may be helpful in treatm

31 ctive in patients with WM and is affected by MYD88 and CXCR4 mutation status.

32 MYD88 and CXCR4 mutations affect WM disease presentation

33 Transcription is affected by MYD88 and CXCR4 mutations and includes overexpression of

34 macroglobulinemia (WM) that are impacted by MYD88 and CXCR4(WHIM) mutations.

35 data as well as the impact of new mutations (MYD88 and CXCR4) on treatment decisions, indications for

36 Thus, MyD88 and downstream mitogen-activated protein kinase an

37 To investigate the roles of Myd88 and Fcer1g in non-B cells, we transferred anti-sel

38 MyD88 and FcR common gamma-chain (Fcer1g, FcRgamma) elic

39 ment was dependent on CD40L, indicating that Myd88 and FcRgamma, presumably on myeloid APCs, were req

40 Our data show that in pericytes, MyD88 and IRAK4 are key regulators of 2 major injury res

41 Unexpectedly, we found that MyD88 and its downstream effector kinase IRAK4 intrinsic

42 at is dependent on the TLR signaling adaptor MyD88 and its downstream kinase IL-1R-associated kinase

43 ates IL-1RI expression on AM surface through MyD88 and NF-kappaB dependent signaling.

44 ed ABC-associated mutations in genes such as MYD88 and PIM1.

45 Bladder expression of TLR4 and MyD88 and serum expression of HMGB1 were increased in ST

46 Furthermore, the TLR signaling adaptors MyD88 and Trif are required for cytokine responses and r

47 protein leads to the engagement of both the MyD88 and TRIF pathways and to the activation of PKC, MA

48 protein leads to the engagement of both the MyD88 and TRIF pathways and to the activation of PKC-bet

49 d (i) that Tat was able to activate both the MyD88 and TRIF pathways, (ii) the capacity of Tat to ind

50 Further, we showed that downstream of the MyD88 and TRIF pathways, the Tat protein activated the p

51 ere abrogated in mice that were deficient in MyD88 and Trif, molecules that are critical in innate im

52 TLR4 signalling through the MyD88 and TRIF-dependent pathways initiates translocatio

53 cytosis of TLR4 and NOX2, independently from MyD88 and TRIF.

54 Patients with mutated MYD88 and wild-type CXCR4 mutation status exhibit best r

55 suggest increased P. aeruginosa adhesion to MyD88(-/-) and blotted corneas is not due to reduction i

56 id differentiation primary response gene 88 (MyD88)- and Toll-interleukin 1 receptor (TIR) domain-con

57 upregulated expression of TLR4, its adaptor MyD88, and coreceptors CD14 and MD2.

58 urface glycosylation requires IL-1R, but not MyD88, and is not sufficient to prevent bacterial bindin

59 proliferation and survival, including IRF4, MYD88, and MYC.

60 ruitment of IL-1R-associated kinase (IRAK)1, MyD88, and protein kinase C (PKC)epsilon to the downstre

61 cpC mediated inhibition of signaling through MyD88, and subsequent amelioration of experimental autoi

62 Collectively, our data demonstrate that MyD88- and Card9-mediated IFN-gamma and nitric oxide pro

63 in the setting of septic insult by targeting MyD88- and Toll/IL-1R domain-containing adaptor inducing

64 LPS binding, thereby enhancing TLR4-adaptor MyD88- and TRIF-dependent signaling that resulted in an

65 broad TLR suppressive activity affects both MyD88- and TRIF-inducing IFN-beta-mediated signaling pat

66 osis-mediated induction of IL-27 in a TLR7-, MyD88-, and NOD2-dependent manner.

67 MyD88(-/-) andCard9(-/-) mice recruited reduced numbers

68 Activating mutations in MYD88 are present in approximately 95% of patients with

69 the Toll-like receptor (TLR) adaptor protein MYD88 as a key regulator of the antiproliferative effect

70 Using mutated MYD88 as a tumor marker, BTK(Cys481) mutations were subc

71 ferentiate into B cells was not dependent on MyD88, as myd88(-/-) LSK(-) cell expansion and different

72 Toll-like receptor (TLR) adaptors TIRAP and MyD88, as well as the ubiquitin-associated protein 1 (UB

73 interaction by rapamycin, truncation of the MyD88-binding domain of TACI, or B-cell-conditional mTOR

74 of MHC-II(high)and production of IL-12p40 in MyD88(-/-)bone marrow-derived dendritic cells (BMDCs) co

75 Genetic deletion of TLR7 or MyD88, but not TLR3, and inhibition of the MAPKs (JNK an

76 absence of the adjuvant effect in vaccinated MyD88(-/-)Cardif(-/-) mice, which are devoid of TLR (wit

77 ped a fusion protein by linking CD8alpha and MyD88 (CD8alpha:MyD88) to enhance CD8(+) T-cell response

78 VDAC protein levels when compared to WT and Myd88(-/-) cells.

79 We employed Myd88 conditional knockout (CKO) mice, in which Myd88 wa

80 highly prevalent somatic mutations including MYD88, CXCR4, and ARID1A in Waldenstrom macroglobulinemi

81 investigation include therapeutics targeting MYD88, CXCR4, and BCL2 signaling.

82 7, or TLR9 deficiency and cell type-specific MyD88 deficiency to study the functional correlation bet

83 e responses are similar to those of TLR4 and MyD88 deficient mice in these models and confirm that GS

84 TLR2-, TLR4-, MyD88-deficient and WT BALB/c mice were intratracheally

85 ddition, VH4-34-encoded IgGs from IRAK4- and MYD88-deficient patients often displayed an unmutated FW

86 Unlike most IRAK-4- or MyD88-deficient patients, he did not suffer from invasiv

87 actic treatments in healthy immunocompetent, MyD88-deficient, lymphocyte-deficient, and neutrophil-de

88 on in HEK-293 cells bearing TLR2 and TLR4 in MyD88 dependent manner.

89 vitro and in vivo production of IL-1beta is MyD88 dependent.

90 nuclear factor kappa B pathways in MDSCs was MyD88 dependent.

91 id differentiation primary response gene 88 (MyD88)-dependent fashion.

92 IL-1R/MYD88/NF-kappaB signaling pathway and MYD88-dependent abnormalities in expression of structura

93 emic inflammation triggered aversion through MyD88-dependent activation of the brain endothelium foll

94 This TAS response was MyD88-dependent and sufficient to directly suppress both

95 inistered 24 hours after radiation and shows MyD88-dependent function.

96 an intradermal S. aureus challenge promoted MyD88-dependent host defense initiated by IL-1beta rathe

97 promotes skin inflammation involving IL-36R/MyD88-dependent IL-17 T cell responses.

98 We now show a novel role for the MyD88-dependent interleukin-33 (IL-33) receptor, ST2, in

99 liver tissues in a toll-like receptor (TLR)/MyD88-dependent manner.

100 ese findings suggest that disruption of this MyD88-dependent pathway in pericytes might be a potentia

101 ligands trigger host Toll-like receptor and MyD88-dependent pathways, leading to IL-36gamma secretio

102 controlled by inputs from the TCR and a TLR2-MyD88-dependent PI3K signaling pathway.

103 shown that pericytes activate a TLR2/4- and MyD88-dependent proinflammatory program in response to t

104 Here, we explored contributions of MyD88-dependent receptors using vital mouse eyes and con

105 strates equipotent activity against multiple MyD88-dependent responses both in vitro and in vivo.

106 l kinase that phosphorylates MyD88, promoted MyD88-dependent signaling and mediates dermatosis in Ptp

107 vs and Tlr7 was independent of viral load or MyD88-dependent signaling but dependent on bacterial bur

108 of danger-associated molecular patterns and MyD88-dependent signaling.

109 us S. aureus exposure to mouse skin promoted MyD88-dependent skin inflammation initiated by IL-36, bu

110 fine the likely cellular candidates for this MyD88-dependent step.

111 MYD88-dependent TLR signaling controlled cytokine levels

112 it homologous to that which drives canonical MYD88-dependent TLR signaling in contemporary mammalian

113 SOCS1 as a key negative regulator to inhibit MyD88-dependent type I IFN signaling in pDCs.

114 The LPS-induced TNF-alpha increases were MyD88-dependent, and were attenuated in primary hepatocy

115 Therefore, TLR/MyD88-dependent, TRAF6-facilitated CREBH activation repr

116 inflammatory cytokine production was through MyD88-dependent, TRIF-independent, TLR4-induced events.

117 function against Pseudomonas aeruginosa was MyD88-dependent.

118 CD8alpha:MyD88-engineered T cells exhibited increased proliferati

119 xclusive as we show UBAP1 can associate with MyD88, enhancing its plasma membrane localization.

120 High expression of MYD88 exhibited increased sensitivity to HDAC inhibitors

121 ding to HCK, whereas transduction of mutated MYD88 expressing WM cells with a mutated HCK gatekeeper

122 CD8alpha:MyD88-expressing T cells improved antitumor responses in

123 protein 1 (HMGB1) increased bladder TLR4 and MyD88 expression and enhanced contractile response to el

124 on-induced cytidine deaminase, hematopoietic MyD88 expression, and an intact microbiome, against whic

125 s deficient for TLR3, -7, and 9, UNC93B1, or MyD88 failed to undergo L. major-induced autophagy.

126 nnate immune receptor that is dependent upon MyD88 for activity of its dominant signaling pathway.

127 like receptor genes as well as the HMGB1 and MyD88 gene transcripts.

128 sing conditions, sialitis did not develop in MyD88(-/-) GF mice.

129 Deletion of MyD88 impairs fusion of myoblasts without affecting thei

130 The combined adjuvant acts via MyD88 in both bone marrow-derived and non-bone marrow-de

131 lpha (IL-1alpha) signaling through IL-1R and MyD88 in both stromal and immune cells drive inflammatio

132 TcpC abrogates the function of MyD88 in macrophages, thus perturbing all the signaling

133 Specific ablation of MyD88 in pericytes or pharmacological inhibition of MyD8

134 Our findings suggest that MyD88 in primary sensory neurons plays an active role in

135 rons, to examine the unique role of neuronal MyD88 in regulating acute and chronic pain, and possible

136 ation, and the previously identified role of MyD88 in the disease.

137 Here we report a cell-autonomous role of MyD88 in the regulation of myoblast fusion.

138 oles of toll-like receptor (TLR) 2, TLR4 and MyD88, in exacerbation of allergen-induced lung eosinoph

139 al. suggested that LPS-driven activation of MyD88, in the absence of TRIF, impairs NF-kappaB translo

140 wnstream of TLR4, which can also activate an MyD88-independent pathway.

141 86126 failed to inhibit assays downstream of MyD88-independent receptors, including the TNF receptor

142 The MyD88-independent Toll/IL-1R domain-containing adapter i

143 id differentiation primary response gene 88 (MyD88), indicating that the adjuvants function in vivo v

144 id differentiation primary response gene 88 (MyD88) induced donor-specific kidney allograft tolerance

145 hanistically, F. nucleatum targeted TLR4 and MYD88 innate immune signaling and specific microRNAs to

146 ent of the death domain (DD) adaptor protein MyD88 into an oligomeric post receptor complex termed th

147 differentiation primary response protein 88 (MyD88)-IRAK-dependent signaling axis.

148 receptor domain containing adaptor protein)-MyD88-IRAK (interleukin-1 receptor-associated kinase)1/4

149 MyD88 is an adaptor protein involved in proinflammatory

150 The adaptor protein MYD88 is critical for relaying activation of Toll-like r

151 In B cells, Myd88 is required for anti-DNA and anti-RNA autoantibody

152 MyD88 is the main adaptor molecule for TLR and IL-1R fam

153 ese findings confirm that signalling through MyD88 is the primary driver for LPS-dependent NF-kappaB

154 id differentiation primary response gene 88 (MyD88) is an adaptor protein that mediates Toll-like rec

155 In addition, MyD88(-/-) joint inflammatory cytokine levels on day 3 a

156 Subsequently, swelling of MyD88(-/-) joints surpassed WT joint swelling, and resol

157 ced/eliminated in TLR4 deficient (Tlr4-d) or MyD88 knockout (MyD88(-/-)) mice.

158 spersal among wild-type and immune-deficient myd88 knockout zebrafish and observed that interhost dis

159 Immunodeficient MyD88-knockout mice infected with S. aureus experienced

160 the peritoneal space that was attenuated in MyD88-knockout or TLR7-knockout mice, respectively.

161 In vitro, MYD88 L265P mutation promoted p100 signaling through TAK

162 ith relapsed or refractory disease harboring MYD88 L265P mutation.

163 g checkpoint against B cell dysregulation by MYD88(L265P) and provide an explanation for the co-occur

164 s has the opposite effect on accumulation of MYD88(L265P) B cells in vitro and in vivo.

165 in clinical trials of TLR7/9 inhibitors for MYD88(L265P) B-cell malignancies.

166 ected, powerful inhibitory effect of TLR9 on MYD88(L265P) B-cell proliferation and differentiation th

167 Conversely, B cells expressing MYD88(L265P) decreased surface IgM coupled with accumula

168 IRAK4 inhibition in the treatment of mutant MYD88(L265P) diffuse large B-cell lymphoma (DLBCL).

169 pression of CD79B counteracted the effect of MYD88(L265P) In B cells chronically stimulated by self-a

170 The MYD88(L265P) mutation is found in 2% to 10% of chronic l

171 ically stimulated by self-antigen, CD79B and MYD88(L265P) mutations in combination, but not individua

172 ere we analyze the consequences of CD79B and MYD88(L265P) mutations individually and combined in norm

173 a, and one of the most frequent mutations in MYD88, L265P, conferred increased cell sensitivity to HD

174 n of SYK, ERK, and AKT and the other through MYD88 leading to activation of NF-kappaB.

175 into B cells was not dependent on MyD88, as myd88(-/-) LSK(-) cell expansion and differentiation rem

176 in mouse livers in a manner depending on the MyD88-mediated inflammatory pathway.

177 n was significantly reduced in TLR4(-/-) and Myd88(-/-) mice and following pretreatment with a NF-kap

178 At early time points, MyD88(-/-) mice display decreased joint inflammation, sw

179 Surprisingly, corneas from MyD88(-/-) mice displayed similar GalNAz labeling to wil

180 ke helicase signaling, whereas in vaccinated MyD88(-/-) mice the adjuvant effect was reduced.

181 Joint bacterial loads in MyD88(-/-) mice were significantly greater than those in

182 njunctiva in wild type, but not in Tlr4-d or MyD88(-/-) mice with topical challenge.

183 In macrophages from MyD88(-/-) mice, RBP4 fails to stimulate secretion of tu

184 In MyD88(-/-) mice, this pro-inflammatory mediator-inducing

185 ressed in gene-deficient mice, especially in MyD88(-/-) mice.

186 infected mice were significantly reduced in MyD88(-/-)mice compared to WT controls, suggesting that

187 TES were significantly increased in infected MyD88(-/-)mice compared to WT mice.

188 rial clearance in vivo R. australis-infected MyD88(-/-)mice showed significantly lower expression lev

189 study, we found that host susceptibility of MyD88(-/-)mice to infection with Rickettsia conorii or R

190 n TLR4 deficient (Tlr4-d) or MyD88 knockout (MyD88(-/-)) mice.

191 Our study shows that MyD88 modulates myoblast fusion and suggests that augmen

192 and has a hierarchical arrangement with 6-8 MyD88 molecules assembling with exactly 4 of IRAK-4 and

193 Finally, in silico experiments revealed that MYD88-mutant ABC-DLBCL cells in particular display an ac

194 ression profiles for patients with wild-type MYD88, mutated ARID1A, familial predisposition to WM, ch

195 novel target for therapeutic development in MYD88-mutated WM and ABC DLBCL, and possibly other disea

196 Toll-like receptor signaling as a result of MYD88 mutation and/or NFKBIZ amplification, frequent con

197 overlapping B-cell malignancies is aided by MYD88 mutation status.

198 CD79B and MYD88 mutations are frequently and simultaneously detect

199 pression of tumor suppressors upregulated by MYD88 mutations in a manner associated with the suppress

200 ding patients having PCNSL with CD79B and/or MYD88 mutations, and 86% of evaluable patients achieved

201 2 amplifications frequently co-occurred with MYD88 mutations, further validating our approach.

202 MYD88 mutations, particularly the p.L265P mutation, have

203 Among patients with MYD88 mutations, those with CXCR4 mutations show transcr

204 platelets from mice with genetic deletion of MyD88 (myeloid differentiation factor 88) or TLRs (Toll-

205 esion if it lacks the innate defense protein MyD88 (myeloid differentiation primary response gene 88)

206 marks, including the classical NF-kappaB and MYD88 (myeloid differentiation primary response gene 88)

207 Toll-6 promotes cell survival via MyD88-NF-kappaB and cell death via Wek-Sarm-JNK.

208 esent inactivated PRRSV antigen through TRIF/MyD88-NF-kappaB signaling pathway and be used as adjuvan

209 0) were significantly increased through TRIF/MyD88-NF-kappaB signaling pathway when porcine periphera

210 that TLR3 up-regulation is dependent on TLR4-MyD88-NF-kappaB signaling.

211 espiratory epithelial cells through a TLR2-, MyD88-, NF-kB-, and MAPK-dependent signaling pathway.

212 ction induces miR-301b expression via a TLR4/MyD88/NF-kappaB pathway.

213 d aberrant activation of the intrinsic IL-1R/MYD88/NF-kappaB signaling pathway and MYD88-dependent ab

214 The MyD88/NF-kappaB signaling pathway was found to be critic

215 mice are as susceptible as mice deficient in MyD88 or UNC93B1, a chaperone required for appropriate l

216 , but did not affect parasite replication in Myd88(-/-) or Unc93b1(-/-) macrophages.

217 anti-chromatin Ab, into mice lacking Fcer1g, Myd88, or both and studied the extrafollicular plasmabla

218 was abolished in cells deficient of TLR7 or MyD88, or by a TLR7 antagonist, but remained the same in

219 nucleic acid sensor TLR7, signaling adaptor MyD88, or transcription factor IRF7 was ablated or pDCs

220 ells, leads to the conditional expression of Myd88(p.L252P) (the orthologous position of the human MY

221 252P) (the orthologous position of the human MYD88(p.L265P) mutation) from the endogenous locus.

222 defining DLBCL molecular subtypes and posit MYD88/p100 signaling as a regulator for B-cell activatio

223 on macrophages, leading to activation of the MyD88 pathway and TNF-alpha production.

224 ndings establish the T-cell intrinsic IL-18R/MyD88 pathway as a crucial element for induction of cogn

225 L degradation, (iii) the crucial role of the MyD88 pathway in the production of Tat-induced TNF-alpha

226 not of IL-1R, phenocopied the absence of the MyD88 pathway, indicating that IL-18R is a critical MyD8

227 ncreased expression is dependent on an IL-1R-MyD88 pathway.

228 id differentiation primary response gene 88 (MyD88) pathway that activates nuclear factor-kappaB and

229 report that the Toll-like receptor 9 (TLR9)-MyD88 pattern-recognition receptor pathway is uniquely c

230 nds and suppresses SYK activation to inhibit MyD88 phosphorylation.

231 and SYK crosstalk as a critical regulator of MyD88 post-translational modifications and IL-1-driven i

232 id differentiation primary response gene-88 (MYD88)/proline-rich tyrosine kinase 2 (PYK2)/LYN complex

233 SYK as a critical kinase that phosphorylates MyD88, promoted MyD88-dependent signaling and mediates d

234 MyD88 protein levels are increased during in vitro myoge

235 these differential responses involve cognate MyD88 recognition.

236 Ablation of MyD88 reduces myofiber size during muscle regeneration,

237 MyD88 regulates non-canonical NF-kappaB and canonical Wn

238 Given these observations, CD8alpha:MyD88 represents a unique and versatile approach to help

239 n the lung of mice by enhancing NTHi-induced MyD88 short, a negative regulator of inflammation, via i

240 Patients with wild-type MYD88 show lower bone marrow disease burden and serum im

241 was mediated by toll-like receptor 4 (TLR-4)/MyD88 signal-transduction pathway up-regulation of MLCK

242 ntestinal permeability was mediated by TLR-4/MyD88 signal-transduction pathway up-regulation of MLCK.

243 unlike T1D, which is blocked in mice lacking MyD88 signaling adaptor under conventional, but not GF,

244 RABGEF1 in dampening keratinocyte-intrinsic MYD88 signaling and sustaining epidermal barrier functio

245 n pericytes or pharmacological inhibition of MyD88 signaling by an IRAK4 inhibitor in vivo protected

246 is, at least in part, via inhibition of TLR4/MyD88 signaling cascade as well as inactivation of NLRP3

247 In vitro, baicalein down-regulated the TLR4/MyD88 signaling cascades (NF-kappaB and MAPKs) in lipopo

248 esting that different IL-1 cytokines trigger MyD88 signaling depending on the anatomical depth of S.

249 Moreover, ablation of MYD88 signaling in RABGEF1-deficient keratinocytes or de

250 Thus, keratinocyte Myd88 signaling in response to S. aureus PSMalpha drives

251 Here, we demonstrated that T-cell intrinsic MyD88 signaling is required for proliferation, protectio

252 Collectively these data demonstrate MyD88 signaling mediates early inflammatory responses in

253 Taken together, our results suggest that MyD88 signaling mediates instructive signals in DCs and

254 Thus, RABGEF1-mediated regulation of IL-1R/MYD88 signaling might represent a potential therapeutic

255 pression was dependent on the microbiota and MyD88 signaling, appeared upon weaning, and was present

256 ns, and other targets in B-cell receptor and MYD88 signaling.

257 r other proteins to restrict the strength of MyD88 signaling.

258 and AP activation through specific TLR7 and MyD88 signaling.

259 lammation in the murine lung via a TLR2/TLR4/MyD88-signaling pathway.

260 R4 knockout mice and by knockdown (siRNA) of MyD88 siRNA in wild type glia.

261 PAF did not affect mRNA expression of MyD88, suggesting that PAF acts downstream the adaptor.

262 ssion and activation is triggered by mutated MYD88, supports the growth and survival of mutated MYD88

263 myeloid differentiation primary response 88 (MyD88), TANK binding kinase 1 (TBK1), or Toll-like recep

264 The upstream pathways of MyD88 that mediate this process, however, remain unclear

265 id differentiation primary response gene 88 (MyD88), the common adaptor for toll-like receptor (TLR)

266 In macrophages lacking MyD88, there is minimal NF-kappaB translocation to the n

267 TSG6 inhibited the association of TLR4 with MyD88, thereby suppressing NF-kappaB activation.

268 approaches, including mice deficient in the MyD88, TIRAP/MAL, or TRIF adaptor, biochemical analysis,

269 mplex, induction of downstream signaling via MyD88/TIRAP, phosphorylation of IRAK4, and subsequent ac

270 R2 signaling competence, leading to impaired MyD88-TLR2 assembly, reduced phosphorylation of IRAK-1,

271 do not have functional B or T cells, and in MyD88-/-, TLR2-/- and TLR4-/- mice that are defective in

272 We also confirmed that Myd88(-/-), Tlr3/7/9(-/-), and Unc93b1(-/-) cells were h

273 dy, we generated Mer(-/-) mice with a global MyD88, TLR7, or TLR9 deficiency and cell type-specific M

274 Released IL-1beta signals through pericyte MyD88 to amplify this response.

275 minal motif of TcpC, i.e. TIR-TcpC, we found MyD88 to be critical for the induction and progression o

276 -like receptors, the precise contribution of MyD88 to the development of autoimmunity, particularly r

277 R753Q TLR2 displayed reduced recruitment of MyD88 to TLR2, decreased NF-kappaB activation, and impai

278 tein by linking CD8alpha and MyD88 (CD8alpha:MyD88) to enhance CD8(+) T-cell responses to weakly immu

279 id differentiation primary response gene 88 (MyD88), to the membrane, which in turn recruit IRAKs via

280 CXCR4 and MYD88 transcription were negatively correlated, demonstr

281 e antigen 96 (MD-2), and downstream signals (MyD88, TRIF, and TAK1).

282 The utilization of macrophages derived from MyD88-, TRIF-, Toll-like receptor 2 (TLR2)-, TLR4-, and

283 Mutated MYD88 triggers BTK, IRAK1/IRAK4, and HCK growth and surv

284 Over-expression of mutated MYD88 triggers HCK and IL-6 transcription, whereas knock

285 SHP1 and SYK-dependent counterregulation of MyD88 tyrosine phosphorylation, we have demonstrated tha

286 athway, indicating that IL-18R is a critical MyD88-upstream pathway involved in the establishment of

287 MYD88 was a component of a wider acetylation signature i

288 ains and ubiquitylation of IRAK1, IRAK4, and MyD88 was abolished in TRAF6/Pellino1/Pellino2 triple-kn

289 88 conditional knockout (CKO) mice, in which Myd88 was deleted in sodium channel subunit Nav1.8-expre

290 to the expression of serum IFN-beta, whereas MyD88 was not.

291 TLR2 and its downstream adaptor protein MyD88 were required for IAPP-induced cytokine production

292 IL1 receptor or the receptor adapter protein MyD88, were not protected from tumor-induced decreases i

293 metic poly I:C is dependent on signaling via MyD88 when it is delivered centrally, whereas this respo

294 endent of myeloid differentiation factor 88 (MyD88), which is the only known signaling adaptor for TL

295 patients genetically deficient for IRAK4 or MYD88, which mediate the function of Toll-like receptors

296 Our study defines acetylation of MYD88, which, by regulating TLR-dependent signaling to c

297 identified aberrant methylation patterns in MYD88 wild-type patients.

298 We observed that mutated MYD88 WM and ABC DLBCL cell lines, as well as primary WM

299 supports the growth and survival of mutated MYD88 WM and ABC DLBCL cells, and is a direct target of

300 signal-regulated kinase signaling in mutated MYD88 WM and/or ABC DLBCL cells.