ライフサイエンスコーパス: moesin

1 e actin-binding proteins ezrin, radixin, and moesin.

2 titutively active, phosphomimetic version of moesin.

3 osomes, Dynein and the actin-membrane linker Moesin.

4 and downregulation of apical phosphorylated Moesin.

5 anied by enrichment of apical phosphorylated Moesin.

6 on of the ezrin/radixin/moesin (ERM) protein moesin.

7 atively regulated Rho by directly activating moesin.

8 nced in T cells deficient for both ezrin and moesin.

9 in II; and linker proteins such as ezrin and moesin.

10 tion of the ERM proteins ezrin, radixin, and moesin.

11 ng the dystrophic muscles were the source of moesin.

12 ortical association and proper activation of moesin.

13 th cone, namely phosphorylated Ezrin/Radixin/Moesin.

14 ype was suppressed by mutations in crumbs or Moesin.

15 plasma membrane, including alpha-actinin-1, moesin, 14-3-3 protein zeta/delta, annexin A1/A3/A4/A5/A

16 -Catenin, and the ERM family member Moesin1 (Moesin a), to define a novel cord hollowing process that

17 We identified moesin, a member of the ezrin-radixin-moesin family, in

18 ortantly, apical proteins Crumbs and phospho-Moesin accumulate to aberrantly high levels in braided t

19 y effect of nearby protein 4.1/ezrin/redixin/moesin acidic sites.

20 pregulate crumbs expression and downregulate Moesin activity.

21 e RNAi screen, looking for new regulators of moesin activity.

22 arized cytoskeletal structures, specifically moesin, actomyosin, and MTs, provide a directional memor

23 Unlike NF2, moesin acts as an oncogene by increasing cell proliferat

24 changes in the expression and activation of moesin and alpha-actinin-1, which associate with actin f

25 land epithelial cells, and overexpression of moesin and Ano1 in HEK cells alters the subcellular loca

26 Moesin and calmodulin (CaM) jointly associate with the c

27 Our findings establish moesin and CD44 as progression markers and drugable targ

28 K5 regulated the subcellular distribution of moesin and colocalized with moesin at the cell periphery

29 Our data thus show that moesin and cortactin are necessary for formation of F-ac

30 s homolog gene family, member A), stabilized moesin and directional memory while depolymerization of

31 nces both phosphorylation of substrates like Moesin and engagement of effectors of its non-catalytic

32 ne promotes release and dephosphorylation of moesin and ezrin.

33 distribution of phosphorylated ezrin-radixin-moesin and F-actin.

34 ddress this, we generated a fly in which RFP-Moesin and GFP-Moesin are expressed in mutually exclusiv

35 The decreases in moesin and radixin in HCV J6/JFH-1-infected Huh7.5 cells

36 Moesin and radixin, but not ezrin, expression were signi

37 sine (Y353) residue that is unconserved with moesin and radixin.

38 r distribution of F-actin and phosphorylated Moesin and rescued the cell rearrangement and apical dom

39 ically, we identified an interaction between moesin and TGF-beta receptor II (TbetaRII) that allows m

40 splayed increased association with actin and moesin and was found enriched in the Triton X-100-insolu

41 l FERM (band-four point one, Ezrin, Radixin, Moesin) and C-terminal CERMAD (ERM association domain) d

42 Glomerular labeling of ezrin, moesin, and gelsolin was altered at 3 wk, but expression

43 keleton linking proteins Ezrin, Radixin, and Moesin, and localization of Merlin to the cortical cytos

44 any cellular processes depend on ERM (ezrin, moesin, and radixin) proteins mediating regulated linkag

45 gnaling/scaffolding proteins ezrin, radixin, moesin, and RhoA, which link the plasma membrane to the

46 els of PI(4,5)P(2) and formation of a novel, Moesin- and PI(4,5)P(2)-enriched apical membrane sac con

47 line-rich domain-containing protein (RLTPR); moesin; and Janus kinase 1 (JAK1).

48 generated a fly in which RFP-Moesin and GFP-Moesin are expressed in mutually exclusive stripes withi

49 mily members expressed in T cells, ezrin and moesin, are implicated in promoting T cell activation an

50 Our findings reveal Moesin as a novel apical polarity protein that drives co

51 n complementary DNA libraries, we identified moesin as a novel gene whose overexpression blocks infec

52 f this study may pave the way for exploiting moesin as a novel target for intervention in MDs, and as

53 We identified amino acid T66 of moesin as a principal GRK5 phosphorylation site and show

54 the cytoskeletal-membrane attachment protein moesin as a putative GRK5 substrate.

55 Our study establishes moesin as an important regulator of the surface abundanc

56 ciency that could be referred to as X-linked moesin-associated immunodeficiency.

57 one side of the trans-axonal complex whereas Moesin association is likely required simultaneously in

58 distribution of moesin and colocalized with moesin at the cell periphery.

59 ents of intracellular dynamics revealed that moesin at the cell rear is a long-lived element that whe

60 binding to PIP2, and PIP2-induced release of moesin autoinhibition.

61 t the talin C terminus binds directly to the moesin band 4.1 ERM (FERM) domain to recruit a moesin-NH

62 of the N-terminal protein 4.1/ezrin/redixin/moesin basic patch with phosphatidylinositol 4,5-biphosp

63 PDZK1 and ezrin, radixin, moesin binding phosphoprotein 50 kDa (EBP50) are postsyn

64 H exchanger regulator factor 1/ezrin-radixin-moesin binding phosphoprotein 50), an adapter protein wi

65 mbrane localization of the expressed moesin, moesin binding to PIP2, and PIP2-induced release of moes

66 gion includes a FERM (band 4.1/ezrin/radixin/moesin) binding domain (FBD) whose mammalian binding par

67 nd was accompanied by a NHERF2 ezrin-radixin-moesin-binding domain-dependent increase in co-precipita

68 actor 1 (NHERF1; also known as ezrin-radixin-moesin-binding phosphoprotein 50) is a PSD-95, disc larg

69 Blockade of Rho signaling or inhibition of moesin both delayed maturation rates to those seen with

70 profilin, cofilin, Dia2, N-WASP, ezrin, and moesin, but the underlying molecular mechanisms have rem

71 l of progressive activation of autoinhibited moesin by a single PIP2 molecule in the membrane.

72 Therapeutic targeting of the moesin-CD44 interaction with the small-molecule inhibito

73 sphatase subunit Sds22 leads to defects in p-moesin clearance from cell poles at anaphase, a delay in

74 m LOK displayed preferential specificity for moesin compared to traditional basophilic kinase substra

75 Increasing the levels of moesin competitively displaced NF2 from CD44, increasing

76 signate the "FLAP." Analysis of three mutant moesin constructs predicted to influence FLAP function d

77 s, only modest interactions between CD44 and moesin could be demonstrated in chondrocytes.

78 hat the Pp1-87B phosphatase dephosphorylates moesin, counteracting its activation by the Ste20-like k

79 c domain capable of binding to ezrin-radixin-moesin cytoskeletal proteins is essential for optimal in

80 e metaphase-anaphase transition, in coupling moesin-dependent cell shape changes to mitotic exit.

81 In contrast, moesin dephosphorylation and removal, along with CD43, a

82 merization of microtubules (MTs) disoriented moesin deposition and also reduced directional memory.

83 In this paper, we show that the ERM protein Moesin directly binds to microtubules in vitro and stabi

84 that whereas the adaptor proteins ezrin and moesin do not detectably concentrate with the array of c

85 irect interaction with the 4.1/ezrin/radizin/moesin domain of focal adhesion kinase (FAK), which func

86 Lastly, we identified the 4.1/ezrin/radixin/moesin domain of SNX17 as being responsible in the bindi

87 ly localized Four-point-one, Ezrin, Radixin, Moesin domain protein Expanded (Ex) regulates Yki by pro

88 that MUC16 interacts with the ezrin/radixin/moesin domain-containing protein of Janus kinase (JAK2)

89 Protein 4.1B is a 4.1/ezrin/radixin/moesin domain-containing protein whose expression is fre

90 ) in the MSN four-point-one, ezrin, radixin, moesin domain.

91 nding members: band 4.1, ezrin, radixin, and moesin) domain and induced gain of function in JAK3.

92 sin tail homology; band 4.1, ezrin, radixin, moesin) domain in their C-terminal tails.

93 res that its FERM (band 4.1, ezrin, radixin, moesin) domain physically interact with both the small G

94 talin FERM (four-point-one, ezrin, radixin, moesin) domain to membrane-proximal sequences in the bet

95 nding of the talin-1 FERM (4.1/ezrin/radixin/moesin) domain to the beta3 cytosolic tail causes activa

96 talin FERM (four-point-one, ezrin, radixin, moesin) domain to the integrin beta tail provides one ke

97 minal FERM (4.1 protein, ezrin, radixin, and moesin) domain, responsible for substrate recognition an

98 ation in the FERM (protein 4.1/ezrin/radixin/moesin) domain-binding motif of Crumbs die due to an ove

99 , is a FERM (Four point one, Ezrin, Radixin, Moesin) domain-containing protein whose loss results in

100 inase and FERM (Band 41, ezrin, radixin, and moesin) domains of Jak3 interacted with beta-catenin, th

101 Indeed, mutations in Moesin dominantly suppressed seamless tube cyst formatio

102 Consequently, loss of moesin (encoded by the MSN gene) or MAP4K4 reduced adhes

103 the actin cytoskeleton through ezrin/radixin/moesin (ERM) actin-binding proteins.

104 and phosphorylation of MLC20, Ezrin-Radixin-Moesin (ERM) and p53 but not ERK1/2, effects recapitulat

105 served region along with the ezrin, radixin, moesin (ERM) binding domain.

106 Cytoskeletal proteins of the ezrin-radixin-moesin (ERM) family contribute to T cell activation in r

107 Proteins of the ezrin, radixin, and moesin (ERM) family control cell and tissue morphogenesi

108 Ezrin/radixin/moesin (ERM) family members provide a regulated link bet

109 und to directly associate with ezrin/radixin/moesin (ERM) family members, proteins that are involved

110 napse via association with the ezrin-radixin-moesin (ERM) family of actin regulatory proteins.

111 Members of the ezrin, radixin and moesin (ERM) family of actin-binding proteins have been

112 o interact with members of the ezrin/radixin/moesin (ERM) family of adaptor proteins, only modest int

113 association is mediated by the ezrin-radixin-moesin (ERM) family of plasma membrane-actin cytoskeleto

114 The evolutionarily conserved ezrin/radixin/moesin (ERM) family of proteins can tether actin filamen

115 Moesin is a member of the ezrin-radixin-moesin (ERM) family of proteins that are important for o

116 rylation and activation of the ezrin/radixin/moesin (ERM) family of proteins.

117 ease in phosphorylation of the ezrin/radixin/moesin (ERM) family proteins and myosin light chain 2 (M

118 The Ezrin-Radixin-Moesin (ERM) family proteins reversibly link the plasma

119 response, dephosphorylation of ezrin/radixin/moesin (ERM) family proteins, and potent tyrosine phosph

120 t alpha-1 and a homolog of the ezrin-radixin-moesin (ERM) family proteins, localize to puncta and ass

121 tative protein kinase of ezrin, radixin, and moesin (ERM) family proteins.

122 Ezrin, a protein of the ezrin, radixin, moesin (ERM) family, provides a regulated linkage betwee

123 tion of ezrin, a member of the ezrin-radixin-moesin (ERM) family, which plays a role in establishing

124 rlin, which is a member of the ezrin-radixin-moesin (ERM) family.

125 ction of shape signals through ezrin-radixin-moesin (ERM) family.

126 found mTOR inhibition reduced ezrin/radixin/moesin (ERM) phosphorylation, intercellular adhesion mol

127 ncreased levels of CD44, ezrin, radixin, and moesin (ERM) phosphorylation, stronger actin polymerizat

128 protein ezrin, a member of the ezrin-radixin-moesin (ERM) protein family that serves as a physical li

129 on increased expression of the ezrin/radixin/moesin (ERM) protein moesin.

130 ulator, Moesin (Moe), an ezrin, radixin, and moesin (ERM) protein, has the ability to bind to and org

131 pended on the recruitment of ezrin, radixin, moesin (ERM) proteins by the intracellular domain of CD4

132 ive (threonine-phosphorylated) ezrin-radixin-moesin (ERM) proteins in nonraft compartments and increa

133 e that the activation of ezrin, radixin, and moesin (ERM) proteins is required for the P2X7R-dependen

134 Ezrin, radixin, and moesin (ERM) proteins link cortical actin to the plasma

135 ding sites for ankyrin and for ezrin/radixin/moesin (ERM) proteins on its cytoplasmic domain (DeltaAN

136 The Ezrin, Radixin, and Moesin (ERM) proteins play a major role in organizing co

137 Ezrin, Radixin, and Moesin (ERM) proteins play important roles in many cellu

138 to interact with cytoskeletal ezrin-radixin-moesin (ERM) proteins that also interact with the PDZ pr

139 Ezrin-radixin-moesin (ERM) proteins, a family of adaptor molecules lin

140 The Ezrin-Radixin-Moesin (ERM) proteins, which link plasma membrane protei

141 controlling the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to th

142 her and are connected by ezrin, radixin, and moesin (ERM) proteins.

143 N)-terminal PDZ domains and an ezrin-radixin-moesin (ERM)-binding (EB) carboxyl (C)-terminal region.

144 hat the membrane-actin linkers ezrin/radixin/moesin (ERMs) are strongly and directly activated by the

145 Our data suggest that ezrin, radixin, and moesin (ERMs), a family of highly homologous, multifunct

146 Cells suppressed for moesin expression by short hairpin RNA had fewer, thinne

147 Our findings suggest that increased moesin expression promotes EMT by regulating adhesion an

148 e ezrin constructs or knockdown of ezrin and moesin expression quantitatively and qualitatively alter

149 Merlin (Moesin-ezrin-radixin-like protein, also known as schwann

150 Merlin/NF2 (moesin-ezrin-radixin-like protein/neurofibromatosis type

151 Ezrin is a member of the ezrin-radixin-moesin family (ERM) of adapter proteins that are localiz

152 Ezrin, a member of the ezrin-radixin-moesin family (ERM), is an essential regulator of the st

153 Ezrin is a member of the ezrin-radixin-moesin family of membrane-actin cytoskeleton cross-linke

154 rlin is closely related to the Ezrin-Radixin-Moesin family of membrane/cytoskeleton linker proteins,

155 Moesin (Moe), a member of the ezrin/radixin/moesin family of proteins, and downregulates the level o

156 of sequence similarity to the Ezrin-Radixin-Moesin family of proteins, the structural model of Ezrin

157 linked to the cytoskeleton by ezrin/radixin/moesin family proteins and is known to regulate invadopo

158 tified moesin, a member of the ezrin-radixin-moesin family, in dystrophic muscles of mice representin

159 dephosphorylation of the ERM (ezrin/radixin/moesin) family of cytoskeletal linker proteins, and the

160 , is related to the ERM (ezrin, radixin, and moesin) family of plasma membrane-actin cytoskeleton lin

161 actin, myosin-II, and the ERM (Ezrin/Radixin/Moesin) family of proteins are enriched in complementary

162 ein of 50 kDa) family and ERM (ezrin/radixin/moesin) family proteins.

163 e increased the apparent binding affinity of moesin FERM domain for CLS.

164 d bilayer, we showed that the association of moesin FERM domain induced the desorption of the basic-r

165 The dissociation constant of moesin FERM domain to CLS in the phosphatidylcholine lip

166 roscopy, we have examined the association of moesin FERM domain with the recombinant transmembrane an

167 teraction between the band 4.1/ezrin/radixin/moesin (FERM) and kinase domains of FAK.

168 Kindlin-2 (K2), a 4.1R-ezrin-radixin-moesin (FERM) domain adaptor protein, mediates numerous

169 Each of these contains a 4.1-ezrin-radixin-moesin (FERM) domain and a pleckstrin homology domain.

170 stsynaptic and its 4.1 protein/ezrin/radixin/moesin (FERM) domain binds SynCAM 1, assembling a synapt

171 ature with a C-terminal 4.1, ezrin, radixin, moesin (FERM) domain bisected by a pleckstrin-homology d

172 that the KRIT1 band 4.1, ezrin, radixin, and moesin (FERM) domain bound the HEG1 C terminus (K(d) = 1

173 imic mutation S249D in the 4.1-ezrin/radixin/moesin (FERM) domain of ezrin.

174 f SNX17 via its protein 4.1, ezrin, radixin, moesin (FERM) domain to the membrane-distal NPxY motif i

175 erates, via its band 4.1 ezrin, radixin, and moesin (FERM) domain, together with Src42A and Draper to

176 rgos via an atypical band, 4.1/ezrin/radixin/moesin (FERM) domain.

177 onal proteins via its band 4.1/ezrin/radixin/moesin (FERM) domain.

178 ces of the band four-point-one/ezrin/radixin/moesin (FERM) domain.

179 ght that the four-point one, ezrin, radixin, moesin (FERM)-kinase domain linker, which contains autop

180 as at the FRMD3 (4.1 protein ezrin, radixin, moesin [FERM] domain containing 3) locus (odds ratio [OR

181 with Rho1 in limiting apical phosphorylated Moesin for apical domain elongation.

182 tumor microenvironment, and the deletion of moesin from recipient mice supported the rapid expansion

183 ment and phosphorylation patterns, ezrin and moesin function together to promote T cell activation.

184 Epistasis analyses indicated that moesin functions downstream of MAP4K4 to inactivate inte

185 Thus, ezrin and moesin have distinct and critical functions in the T cel

186 cal junction proteins, and the ezrin-radixin-moesin homologue ERM-1, a protein that connects F-actin

187 egion in the regulatory 4.1, ezrin, radixin, moesin homology (FERM) domain.

188 eus, the FAK-FERM (band 4.1, ezrin, radixin, moesin homology) domain bound directly to GATA4 and enha

189 ne 58 in its FERM (band 4.1, ezrin, radixin, moesin) homology domain, which exposes a region importan

190 Loss of moesin impaired the development and function of both per

191 phosphorylated forms of ezrin, radixin, and moesin in cochlear cultures during the period of hair-bu

192 e20 kinase Slik phosphorylates and activates Moesin in developing epithelial tissues to promote epith

193 ing endothelial cells, MAP4K4 phosphorylates moesin in retracting membranes at sites of focal adhesio

194 ces reflect unique requirements for ezrin vs moesin in T cell signaling, we generated mice with condi

195 Crumbs in apical membrane generation and of Moesin in the cross-linking of the apical membrane to th

196 ly related ERM proteins (Ezrin, Radixin, and Moesin) in generating cortical asymmetry in the absence

197 We found that transient knockdown of moesin increased HCV RNA expression while overexpression

198 of stable microtubules, whereas knockdown of moesin increased stable microtubule formation.

199 xpression of either Crumbs or phosphomimetic Moesin induced lumenal cysts and decreased terminal bran

200 udy, we show that the ERM proteins ezrin and moesin influence the organization and integrity of BCR m

201 Moesin is a member of the ezrin-radixin-moesin (ERM) fam

202 ion pathways and suggests that modulation of moesin is a potential therapeutic target for Treg-relate

203 Moesin is an ERM family protein that connects the actin

204 This asymmetric distribution of p-Moesin is determined by components of the apical polarit

205 )P2 and the ERM proteins ezrin, radixin, and moesin is mislocalized and found uniformly along the pla

206 We also found that moesin is required for iTreg conversion in the tumor mic

207 Here, we have discovered that moesin is translationally regulated by TGF-beta and is a

208 During metaphase, phosphorylated Moesin (p-Moesin) is enriched at the apical cortex, and loss of Mo

209 We find that the actin-binding protein, Moesin, is essential for NB proliferation and mitotic pr

210 have elucidated the molecular basis for the moesin/l-selectin/CaM ternary complex and suggested an i

211 s enriched at the apical cortex, and loss of Moesin leads to defects in apical polarity maintenance a

212 e identify PP1-87B RNAi as having elevated p-moesin levels and reduced cortical compliance.

213 rotic agent, resulted in a major decrease in moesin levels in the muscles of DMD and CMD mice.

214 ghly homologous proteins ezrin, radixin, and moesin link proteins to the actin cytoskeleton.

215 During later stages of mitosis, p-Moesin localization shifts more basally, contributing to

216 ly related ERM proteins (Ezrin, Radixin, and Moesin), Merlin may organize the plasma membrane by asse

217 in tail homology 4-band 4.1, ezrin, radixin, moesin; MF) in the initiation and elongation of filopodi

218 in tail homology 4-band 4.1, ezrin, radixin, moesin; MF) in their cargo binding tails and are essenti

219 Moreover, interfering RNA for moesin modifies Ano1 current without affecting its surfa

220 teract through its juxtamembrane domain with Moesin (Moe), a FERM domain protein that regulates the c

221 omotes the phosphorylation and activation of Moesin (Moe), a member of the ezrin/radixin/moesin famil

222 Another important cytoskeletal regulator, Moesin (Moe), an ezrin, radixin, and moesin (ERM) protei

223 Loss of Moesin (Moe), an upstream regulator of Rho1 activity, re

224 utes: membrane localization of the expressed moesin, moesin binding to PIP2, and PIP2-induced release

225 We observed hemizygous mutations in the moesin (MSN) gene (located on the X chromosome and codin

226 ossible mechanisms, we generated informative moesin mutations and tested three attributes: membrane l

227 ail homology 4/band 4.1, ezrin, radixin, and moesin) myosins have roles in cellular adhesion, extensi

228 Together, these results suggest that moesin negatively regulates stable microtubule networks

229 esin band 4.1 ERM (FERM) domain to recruit a moesin-NHE-1 complex to invadopodia.

230 Here, we report that overexpression of moesin occurs generally in high-grade glioblastoma in a

231 In contrast, transient knockdown of moesin or radixin augmented HCV infection.

232 Overexpression of moesin or radixin significantly reduced HCV protein expr

233 in tail homology 4-band 4.1, ezrin, radixin, moesin, or MF) domains in their tails are found in a wid

234 Moesin overexpression was found to downregulate the form

235 During metaphase, phosphorylated Moesin (p-Moesin) is enriched at the apical cortex, and

236 The cytoskeletal proteins ezrin and moesin participate in parietal cell acid and chief cell

237 LOK's activity on moesin peptide and protein was comparable to reported ER

238 both T cell depolarization and ezrin-radixin-moesin phosphorylation after GC exposure.

239 ase in epithelial cells, is not required for Moesin phosphorylation but is critical for the growth-pr

240 Two new reports have found that moesin phosphorylation is essential for mitotic cell rou

241 involved either in the cytoskeleton (ezrin, moesin, plastin 1, lamin B1, vimentin, and beta-actin) o

242 Whether moesin plays any role during the generation of TGF-beta-

243 We also found that moesin plays no role during endocytosis and recycling to

244 Moesin-positive cells were embedded within the fibrotic

245 s the presence of interdigitated, actin- and Moesin-positive, microvilli-like structures wrapping the

246 teins, the structural model of Ezrin-Radixin-Moesin protein autoinhibition and cycling between closed

247 protein ezrin, a member of the ezrin-radixin-moesin protein family.

248 Radixin, the dominant ezrin-radixin-moesin protein in hepatocytes, has been reported to sele

249 blish a causal link between an ezrin-radixin-moesin protein mutation and a primary immunodeficiency t

250 tins scaffold F-actin, via the ezrin-radixin-moesin protein Tea1, and phosphatidylinositide interacti

251 zrin is a member of the ERM (ezrin, radixin, moesin) protein family and links F-actin to the cell mem

252 Because ezrin, radixin and moesin proteins (ERMs) link PSGL-1 to actin cytoskeleton

253 Ezrin-radixin-moesin proteins are cross-linkers between the plasma mem

254 horylation and inactivation of ezrin/radixin/moesin proteins at cell poles.

255 t of ezrin and moesin, the two ezrin/radixin/moesin proteins expressed in T cells.

256 Ezrin/radixin/moesin proteins link the actin cytoskeleton to the plasm

257 a is dependent on lipid rafts, whereas ezrin/moesin proteins mediate podoplanin ring assembly.

258 The ezrin-radixin-moesin proteins regulate B lymphocyte activation via the

259 tor of actin, Vav1, as well as ezrin-radixin-moesin proteins that connect actin filaments to membrane

260 ane-cytoskeleton cross-linking ezrin-radixin-moesin proteins, in the regulation of the earliest steps

261 e preceded by an activation of ezrin-radixin-moesin proteins, which transiently increases the cellula

262 in phosphatase, LIM kinase and ezrin/radixin/moesin proteins.

263 in F-actin and phosphorylated ezrin-radexin-moesin proteins.

264 lization of the phosphorylated ezrin-radixin-moesin proteins.

265 ERM (ezrin, radixin, and moesin) proteins are cytoskeletal interacting proteins t

266 ERM (Ezrin-Radixin-Moesin) proteins are key cross-linkers of the plasma mem

267 ERM (ezrin, radixin moesin) proteins in lymphocytes link cortical actin to p

268 ERM (ezrin-radixin-moesin) proteins mediate linkage of actin cytoskeleton t

269 Like the ERM (ezrin-radixin-moesin) proteins, merlin interacts with CD44, a cell-sur

270 closely related to the ERM (ezrin, radixin, moesin) proteins, which provide anchorage between membra

271 Proteins of the ERM family (ezrin, moesin, radixin) play a fundamental role in tethering th

272 Host cytoskeletal proteins of the ezrin-moesin-radixin (EMR) family have been shown to modulate

273 Ano1, ezrin, and moesin/radixin colocalize apically in salivary gland epi

274 at enforcing the expression of a T66-mutated moesin reduced cell spreading.

275 inal 45-kDa FERM (4.1, ezrin-, radixin-, and moesin-related protein) domain, also known as the talin

276 of the membrane-cortex link and depletion of moesin results in softer cortices that disrupt spindle o

277 eport the crystal structure of intact insect moesin, revealing that its essential yet previously unch

278 nce and stability of TbetaRII and identifies moesin's role in facilitating the efficient generation o

279 ditional deletion of ezrin in CD4+ cells and moesin-specific siRNA, we generated T cells lacking ERM

280 he end of FERM (protein 4.1, ezrin, radixin, moesin) subdomain 2, and the second mutation is a base d

281 and branching, respectively, the ERM protein moesin supports the formation of F-actin networks on ear

282 there were factors overexpressed (including moesins, syndecans, and integrins, among others) that co

283 Although expression of phosphomimetic moesin (T558D) or ezrin (T567D) mutants enhances membran

284 chemical inhibitors, we define here a MAP4K4-moesin-talin-beta1-integrin molecular pathway that promo

285 on and can phosphorylate ezrin, radixin, and moesin (the ERM proteins).

286 We previously reported that moesin, the only ERM in Drosophila, controls mitotic mor

287 Moesin, the sole Drosophila ERM-family protein [4], play

288 we investigated the involvement of ezrin and moesin, the two ezrin/radixin/moesin proteins expressed

289 TGF-beta receptor II (TbetaRII) that allows moesin to control the surface abundance and stability of

290 f ezrin-/- T cells or T cells suppressed for moesin using small interfering RNA showed intact early T

291 al models and patients' muscles, part of the moesin was in its active phosphorylated form.

292 Moesin was the major ERM member activated by phosphoryla

293 To elucidate the contributions of ezrin and moesin, we conducted a systematic analysis of their func

294 olved in the temporal and spatial control of moesin, we identify PP1-87B RNAi as having elevated p-mo

295 High levels of moesin were also observed in muscle biopsy specimens fro

296 In response to TCR engagement, ezrin and moesin were phosphorylated in parallel at the regulatory

297 luding intercellular adhesion molecule 1 and moesin, were selectively recruited to the cap of CD20 an

298 eration of glioblastoma cells overexpressing moesin, where the Wnt/beta-catenin pathway was activated

299 We demonstrate that ezrin and moesin, which are generally believed to be functionally

300 Ezrin and moesin, which link the actin cytoskeleton to the plasma