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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

40 ERM proteins are believed to be regulated by a transitio

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

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

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

44 All three ERM proteins are expressed predominantly at the membrane

45 While ERM proteins are involved in many important cellular eve

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

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

48 ERM proteins are membrane cytoskeletal linkers that are

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

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

51 ERM proteins are regulated by an intramolecular associat

52 ERM proteins are regulated by phosphatidylinositol 4, 5-

53 ERM proteins are regulated by phosphorylation of the mos

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

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

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

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

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

59 NHE1 and ERM proteins associate directly and colocalize in lamell

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

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

62 50 is required for the maintenance of active ERM proteins at the cortical brush border membranes (BBM

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

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

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

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

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

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

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

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

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

72 The ERM proteins contribute to cytoskeleton dynamics, and th

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

98 ERM proteins have been suggested to link the plasma memb

99 ERM proteins have previously been shown to interact with

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

150 ERM proteins regulate cell morphology and plasma membran

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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