ライフサイエンスコーパス: ERM protein

1 hosphorylate ezrin, radixin, and moesin (the ERM proteins).

2 the S-adenosylmethionine binding site on the Erm protein.

3 sion and migration through direct binding to ERM proteins.

4 nan receptor CD44, a main binding partner of ERM proteins.

5 of a novel phenotype previously ascribed to ERM proteins.

6 phosphorylation of ROK-alpha, CD44, and the ERM proteins.

7 tea1-like protein with some similarities to ERM proteins.

8 C12 cells, which were then immunolabeled for ERM proteins.

9 ng Schwann cells that are highly enriched in ERM proteins.

10 osine-1-phosphate (S1P) in the regulation of ERM proteins.

11 n may be mediated through phosphorylation of ERM proteins.

12 ling the function of moesin as well as other ERM proteins.

13 ative regulatory role, as has been shown for ERM proteins.

14 thway and evaluate their ability to regulate ERM proteins.

15 depends exclusively on interactions with 4.1/ERM proteins.

16 results in phosphorylation and activation of ERM proteins.

17 trafficking depend on CD43 association with ERM proteins.

18 terminus of AQP0 and subdomains F1 and F3 of ERM proteins.

19 RRK2 further enhances the phosphorylation of ERM proteins.

20 as a binding site for ezrin/radixin/moesin (ERM) proteins.

21 its direct binding of ezrin/radixin/moesin (ERM) proteins.

22 1 that is conserved in ezrin/radixin/moesin (ERM) proteins.

23 osphorylation of ezrin, radixin, and moesin (ERM) proteins.

24 s the actin organizing Ezrin-Radixin-Moesin (ERM) proteins.

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

26 Ezrin-radixin-moesin (ERM) proteins, a family of adaptor molecules linking the

27 ion-competent DOC2b was required to increase ERM protein activation, and ERM protein knockdown impair

28 The functional relationship between ERM proteins and CLIC5A is incompletely understood and w

29 linkage is controlled by the conformation of ERM proteins and depends on the phosphorylation of a con

30 of the latter impairs the phosphorylation of ERM proteins and enhances death of cells exposed to reac

31 the actin filament assembly activated by the ERM proteins and for the tumor suppressor function of me

32 discuss how lymphocyte-specific knockouts of ERM proteins and high resolution imaging techniques have

33 ERM/NHERF-1 complex and reduction of hepatic ERM proteins and ICAM-1, molecules that are up-regulated

34 n with both the active and inactive forms of ERM proteins and implying a possible role of ELMO in loc

35 to NHERF1 associations, mediating binding to ERM proteins and inhibiting binding of PDZ domain ligand

36 argeting involves interactions with both 4.1/ERM proteins and proteins containing the COOH-terminal T

37 ction in vitro has been demonstrated between ERM proteins and the hyaluronan receptor, CD44.

38 ortant pathophysiological situation in which ERM proteins and their phosphorylation play a significan

39 horylation of CD44 and ezrin-radixin-moesin (ERM) proteins and CD44.ERM.actin complex formation.

40 al expression of EBP50, presence of specific ERM proteins, and functional effects of PDZ1 expression

41 specific siRNA, we generated T cells lacking ERM proteins, and investigated the effect on specific ev

42 Merlin, like the closely related ERM proteins, appears to provide regulated linkage betwe

43 Recently, we demonstrated that ERM proteins are also subject to counter regulation by t

44 ERM proteins are believed to be regulated by a transitio

45 In vivo, the ERM proteins are concentrated strikingly in the nodal pr

46 or the function and regulation of merlin and ERM proteins are discussed.

47 Here, we demonstrate that ERM proteins are expressed in extending neuronal process

48 All three ERM proteins are expressed predominantly at the membrane

49 While ERM proteins are involved in many important cellular eve

50 Taken together, these results show that ERM proteins are largely dispensable for T cell chemotax

51 and functional properties of merlin and the ERM proteins are largely distinct.

52 ERM proteins are membrane cytoskeletal linkers that are

53 This study tested the hypothesis that ERM proteins are phosphorylated on this critical threoni

54 Thus, ERM proteins are phosphorylated through p38 and PKC-depe

55 ERM proteins are regulated by an intramolecular associat

56 ERM proteins are regulated by phosphatidylinositol 4, 5-

57 ERM proteins are regulated by phosphorylation of the mos

58 These results suggest that ERM proteins are required for microvillar positioning of

59 In NHERF-1(-/-) mice, ERM proteins are significantly reduced in brush-border m

60 As the ezrin-radixin-moesin (ERM) proteins are expressed in the microvilli of many ep

61 required for binding to ezrin-radixinmoesin (ERM) proteins: arginine 357 and lysine 362.

62 n recent years, a novel role has emerged for ERM proteins as signaling scaffolds that can modulate B

63 NHE1 and ERM proteins associate directly and colocalize in lamell

64 Here we showed that ERM proteins associate directly with ELMO1 as purified r

65 Co-immunoprecipitation showed that ERM proteins associate with wild-type NEP protein but no

66 50 is required for the maintenance of active ERM proteins at the cortical brush border membranes (BBM

67 e specific ligands necessary for stabilizing ERM proteins at the membrane are not known.

68 ectly to recombinant N terminus fragments of ERM proteins at the positively charged amino acid cluste

69 During development, the ERM proteins become concentrated at the ends of Schwann

70 assays show that NIK interacts directly with ERM proteins, binding their N termini and phosphorylatin

71 deling and an additional key role of PIP2 in ERM protein biology, namely hydrolysis-mediated ERM inac

72 data suggest that direct phosphorylation of ERM proteins by NIK constitutes a signaling mechanism co

73 n the recruitment of ezrin, radixin, moesin (ERM) proteins by the intracellular domain of CD44 to the

74 gnaling pathway for Galpha(13) indicate that ERM proteins can be activated by and serve as effectors

75 mokine (e.g., SDF-1) stimulation inactivates ERM proteins, causing their release from the plasma memb

76 The ERM proteins contribute to cytoskeleton dynamics, and th

77 esults reveal a molecular mechanism by which ERM proteins control RhoA activity and suggest a novel l

78 cytoskeletal changes may be coordinated with ERM protein crosslinking activity during dynamic cellula

79 Silencing of ERM protein expression inhibits DCC-PKA interaction, DCC

80 d were completely prevented by inhibition of ERM protein expression using small interfering RNA.

81 The ERM protein ezrin, but not radixin or moesin, is markedl

82 d up-regulation of the metastasis-associated ERM protein Ezrin.

83 In this study, we show that the ERM proteins ezrin and moesin influence the organization

84 lacking binding sites for PI(4,5)P2 and the ERM proteins ezrin, radixin, and moesin is mislocalized

85 by growth factors and phosphorylation of the ERM proteins ezrin, radixin, and moesin.

86 The closely related ERM proteins (ezrin, radixin, and moesin) act as linkers

87 The ERM proteins (ezrin, radixin, and moesin) are a group of

88 tumor suppressor Merlin and closely related ERM proteins (Ezrin, Radixin, and Moesin) in generating

89 Like the closely related ERM proteins (Ezrin, Radixin, and Moesin), Merlin may or

90 It bears striking similarity to the ERM proteins, ezrin, radixin and moesin, members of the

91 ERM proteins facilitate this process, controlling direct

92 The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface

93 ezrin, a member of the ezrin-radixin-moesin (ERM) protein family that serves as a physical link betwe

94 founder member of the ezrin/radixin/moesin (ERM) protein family, but not expression of the related E

95 rin, a member of the ezrin, radixin, moesin (ERM) protein family, is a critical and ancient protein r

96 in member of the Ezrin, radixin, and moesin (ERM) protein family, plays a critical role in both osteo

97 ansmission and speculate on the potential of ERM proteins for regulating undesirable lymphocyte behav

98 In BBM, active ERM proteins formed distinct complexes with full-length

99 Finally, we describe scenarios in which ERM protein function is coopted by pathogens for their o

100 Disruption of ERM protein function using dominant-negative or constitu

101 ting a dormant and closed conformation of an ERM protein has previously been determined by x-ray crys

102 The study of mammalian ERM proteins has been hampered by presumed functional ov

103 No functional ortholog for any ERMES protein has been identified in metazoans.

104 Moesin (Moe), an ezrin, radixin, and moesin (ERM) protein, has the ability to bind to and organize co

105 ERM proteins have been suggested to link the plasma memb

106 ERM proteins have previously been shown to interact with

107 Here we show that NHERF-1 assembles ERM proteins, ICAM-1 and F-actin into a macromolecule co

108 T576, the analogous phosphorylation site in ERM proteins important for regulating their function, ha

109 , our studies demonstrate a critical role of ERM proteins in AML, with implications also for human ca

110 ible role of ELMO in localizing or retaining ERM proteins in certain cellular sites.

111 Restoring expression of ERM proteins in HER2(+) breast cancer cells was sufficie

112 phosphorylation, crucial to the role of the ERM proteins in linking the plasma membrane to actin fil

113 KCalpha and beta1 integrins co-sediment with ERM proteins in low-density sucrose gradient fractions t

114 cent studies that have redefined the role of ERM proteins in lymphocyte activation and migration.

115 rotubule and actin cytoskeletons mediated by ERM proteins in mitosis and have broad implications in b

116 ort here that NEP co-immunoprecipitates with ERM proteins in NEP-expressing LNCaP prostate cancer cel

117 iology, Kunda et al. describe a new role for ERM proteins in regulating rearrangements of the cortica

118 t to our understanding about the role of the ERM proteins in regulating signal transduction pathways

119 segments, or accumulations of phosphorylated-ERM proteins in Schwann cell nodal microvilli.

120 se data uncover fundamental roles for Merlin/ERM proteins in spatiotemporally organizing the cell cor

121 have focused on the individual roles of the ERM proteins in stabilizing the membrane-cytoskeleton in

122 abolic fate of deltaF508 CFTR and associated ERM proteins in the cystic fibrosis lung.

123 lioblastoma, we investigated roles for other ERM proteins in this malignancy.

124 eonine-phosphorylated) ezrin-radixin-moesin (ERM) proteins in nonraft compartments and increased colo

125 activity is necessary for phosphorylation of ERM proteins induced by EGF and PDGF, but not by thrombi

126 sociated proteins ezrin, radixin and moesin (ERM proteins), inhibits cell growth when overexpressed i

127 We show that both protein 4.1 and the ezrin ERM protein interact with the murine form of hDlg in a c

128 To determine whether ERM proteins interact with L1 in vivo, extracellular ant

129 Although conformational activation of the ERM protein is mediated by the membrane PIP2, the known

130 BCR-driven inactivation of ERM proteins is accompanied by a temporary increase in B

131 SDF-1-mediated inactivation of ERM proteins is blocked by phospholipase C (PLC) inhibit

132 hese results show that while CD43 binding to ERM proteins is crucial for S76 phosphorylation, CD43 mo

133 he activation of ezrin, radixin, and moesin (ERM) proteins is required for the P2X7R-dependent proteo

134 that the talin FERM domain, like that in the ERM proteins, is masked in the intact molecule.

135 ults in the mislocalization of actin and the ERM proteins, key cytoskeletal proteins that connect the

136 ired to increase ERM protein activation, and ERM protein knockdown impaired DOC2b-mediated boosting o

137 Mutations in ERM proteins lead to severe combined immunodeficiency, b

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

139 Activated ezrin-radixin-moesin (ERM) proteins link the plasma membrane to the actin cyto

140 nd the ability of ExoS to ADP-ribosylate the ERM proteins links ADP-ribosylation with the cytoskeleta

141 In cells, NIK and phosphorylated ERM proteins localize at the distal margins of lamellipo

142 or secondary lymphoid tissue cytokine), and ERM proteins lose their punctate distribution with kinet

143 differentiation, the interaction of AQP0 and ERM proteins may play an important role in fiber cell mo

144 phosphorylation of merlin, similar to other ERM proteins, may regulate its function.

145 These studies suggest that ERM proteins mediate the outside-in, rather than inside-

146 Thus, myosin-II and ERM proteins modulate mechanical properties in oocytes,

147 In this paper, we show that the ERM protein Moesin directly binds to microtubules in vit

148 Here, we show that the sole Drosophila ERM protein Moesin functions to promote cortical actin a

149 nucleation and branching, respectively, the ERM protein moesin supports the formation of F-actin net

150 codon-changing mutation (Arg(295)Cys) in the ERM protein moesin that markedly accelerated leukemogene

151 d selectively with the ezrin/radixin/moesin (ERM) protein moesin, but not with other ERM proteins or

152 ased expression of the ezrin/radixin/moesin (ERM) protein moesin.

153 NHE-RF binds to the related ERM proteins, moesin and radixin.

154 es for ankyrin and for ezrin/radixin/moesin (ERM) proteins on its cytoplasmic domain (DeltaANKDeltaER

155 CRISPR/Cas9 was used to knock out all ERM proteins or LOK/SLK in human cells.

156 sin (ERM) protein moesin, but not with other ERM proteins or several other cytoskeletal linker protei

157 These results indicate that ERM proteins organize a complex distal to the T cell/APC

158 n of L1CAM.Together, these data suggest that ERM proteins organize actin filaments in sensory neuron

159 SCLC cells, binds directly to phosphorylated ERM proteins (p-ERM), which is dependent on the central

160 asma membrane, which is regulated in part by ERM protein phosphorylation.

161 The Ezrin, Radixin, and Moesin (ERM) proteins play a major role in organizing cortical d

162 Ezrin, Radixin, and Moesin (ERM) proteins play important roles in many cellular proc

163 sis 2 tumor suppressor Merlin, Expanded, the ERM proteins, protein tyrosine phosphatases, and unconve

164 ERM proteins regulate cell morphology and plasma membran

165 Ezrin, radixin, and moesin (ERM) proteins regulate assembly of actin-based structure

166 Ezrin-radixin-moesin (ERM) proteins regulate the organization and function of

167 To assess whether phosphorylation of ERM proteins regulates lymphocyte migration and membrane

168 The similarities between merlin and ERM proteins suggest that merlin's growth-regulatory cap

169 in family, but not expression of the related ERM proteins, suggesting that ezrin has a distinct role

170 th actin-binding ezrin, radixin, and moesin (ERM) proteins, suggesting a role in linking the plasma m

171 Ezrin, Radixin, and Moesin (the ERM proteins) supply regulated linkage between membrane

172 logy with band 4.1 and ezrin/radixin/moesin (ERM) proteins termed a FERM domain.

173 d a defect in plasma membrane recruitment of ERM proteins that are involved in controlling membrane-t

174 ract with cytoskeletal ezrin-radixin-moesin (ERM) proteins that also interact with the PDZ protein, N

175 As RhoA-GTP activates LOK/SLK to activate ERM proteins, the ability of active ERMs to negatively r

176 In native autoinhibited ERM proteins, the POCKET is a cavity masked by an acidic

177 Disruption of the phospho-cycling nature of ERM proteins through dominant negative and constitutivel

178 roteolytically processed EBP50 would release ERM proteins to complex with F-actin.

179 Binding of ERM proteins to NEP results in decreased binding of ERM

180 Similarly, in vitro binding of ERM proteins to the cytoplasmic tail of CD44 is also dep

181 teins to NEP results in decreased binding of ERM proteins to the hyaluronan receptor CD44, a main bin

182 The contribution of ERM proteins to these structures depends on a conformati

183 However, little is known about ERM protein turnover at the membrane-cortex interface.

184 Using mice in which T cells lack all ERM proteins, we demonstrate a selective role for these

185 HERF1), which binds the N-terminal domain of ERM proteins, we found that EBP50 is required for the ma

186 In EBP50(-/-) mice, ERM proteins were significantly decreased specifically i

187 an ADP-ribosylating domain that affects the ERM proteins, which link the plasma membrane to the acti

188 Thus, although isoform 1 resembles the ERM proteins, which transition between inactive (closed)

189 The Ezrin-Radixin-Moesin (ERM) proteins, which link plasma membrane proteins with

190 ing the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to the plasma

191 cells are regulated by ezrin/radixin/moesin (ERM) proteins, which link the plasma membrane to the cor

192 ads to dephosphorylation and inactivation of ERM proteins, while S1P results in phosphorylation and a

193 Therefore, the kinetics of association of ERM proteins with the cortex likely influence the timesc

194 icated RhoA in regulating the association of ERM proteins with their membrane targets.