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 ng the dystrophic muscles were the source of moesin.

5 and downregulation of apical phosphorylated Moesin.

6 anied by enrichment of apical phosphorylated Moesin.

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

8 atively regulated Rho by directly activating moesin.

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

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

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

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

13 ype was suppressed by mutations in crumbs or Moesin.

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

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

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

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

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

19 pregulate crumbs expression and downregulate Moesin activity.

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

21 Moesin acts as a crosslinker between plasma membrane and

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

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

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

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

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

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

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

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

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

31 ne promotes release and dephosphorylation of moesin and ezrin.

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

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

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

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

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

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

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

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

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

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

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

43 ds the cytoskeleton proteins ezrin, radixin, moesin, and merlin.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

70 Knockdown of moesin by RNA interference resulted in enhanced infectio

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

90 9) in the FERM (band 4.1, Ezrin, radixin and moesin) domain as a phosphorylation site.

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

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

93 of the FERM (Four-point one, Ezrin, Radixin, Moesin) domain superfamily, which consists of membrane-a

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

139 Ezrin, radixin, and moesin (ERM) regulate many cell processes that often req

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

141 r Map led to identification of ezrin/radixin/moesin (ERM)-binding phosphoprotein 50 (EBP50), also kno

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

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

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

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

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

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

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

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

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

151 actin-associated proteins, the ezrin-radixin-moesin family and fimbrin, and it is localized to actin-

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

191 ing that even the endogenous basal levels of moesin in rat fibroblasts are sufficient to limit virus

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

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

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

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

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

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

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

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

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

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

202 Moesin is an ERM family protein that connects the actin

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

231 Overexpression of moesin or radixin significantly reduced HCV protein expr

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

233 Moesin overexpression was found to downregulate the form

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

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

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

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

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

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

240 tion by NKG2D induced Vav1 and ezrin-radixin-moesin phosphorylation.

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

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

264 o acting through Rho kinase on ezrin-radixin-moesin proteins.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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