Ezrin has properties to self-associate at the plasma membrane
about
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304The ERM proteins interact with the HOPS complex to regulate the maturation of endosomesEzrin is a cyclic AMP-dependent protein kinase anchoring proteinStructural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domainEzrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding siteEzrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathwayRegulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathwayEzrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail associationMorphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membraneTunneling nanotubes provide a unique conduit for intercellular transfer of cellular contents in human malignant pleural mesotheliomaStructural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44Ezrin ubiquitylation by the E3 ubiquitin ligase, WWP1, and consequent regulation of hepatocyte growth factor receptor activityActivated ezrin promotes cell migration through recruitment of the GEF Dbl to lipid rafts and preferential downstream activation of Cdc42Ezrin/Radixin/Moesin proteins and flotillins cooperate to promote uropod formation in T cellsG protein-coupled receptor kinase 2 activates radixin, regulating membrane protrusion and motility in epithelial cells.Alveolar echinococcosis: characterization of diagnostic antigen Em18 and serological evaluation of recombinant Em18.Interleukin-7 compartmentalizes its receptor signaling complex to initiate CD4 T lymphocyte response.Ezrin promotes invasion and metastasis of pancreatic cancer cells.Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes.Activation of F-actin binding capacity of ezrin: synergism of PIP₂ interaction and phosphorylation.Tailor-made ezrin actin binding domain to probe its interaction with actin in-vitro.Ezrin regulates microvillus morphogenesis by promoting distinct activities of Eps8 proteins.Ezrin NH2-terminal domain inhibits the cell extension activity of the COOH-terminal domain.Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains.Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis.Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cellsReconstruction and signal propagation analysis of the Syk signaling network in breast cancer cells.Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium.Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution.Analysis of SRC oncogenic signaling in colorectal cancer by stable isotope labeling with heavy amino acids in mouse xenograftsBeta4 integrin promotes osteosarcoma metastasis and interacts with ezrin.Three determinants in ezrin are responsible for cell extension activity.Human ezrin-moesin-radixin proteins modulate hepatitis C virus infection.Phosphoinositides regulate membrane-dependent actin assembly by latex bead phagosomes.Regulation of Cdc42-mediated morphological effects: a novel function for p53.Involvement of ezrin/moesin in de novo actin assembly on phagosomal membranes.Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal componentsGem associates with Ezrin and acts via the Rho-GAP protein Gmip to down-regulate the Rho pathway.
P2860
Q24313074-676B3BBD-2654-44C6-B4D3-3658D4C3FC37Q24314977-8A1AAB14-3FC7-4543-B039-33B082068BD1Q24532065-9E5496FD-B461-4BEF-8DF6-2CC030B61B1AQ24598762-77AB3E9E-E04C-4A03-BCC0-385FE4A92301Q24617964-1679C0A0-2479-4152-89E5-F07589B4C4D4Q24648522-2A7E92D3-CEF9-4AB6-AEAC-74006A4E9053Q24671083-D9A27518-BDE5-4B71-9009-32A07217831FQ24676628-D8C76A5A-0DE5-49CB-8EAF-B20C30D91C07Q24678197-5B3C910C-F79A-406B-922E-00B1569E2090Q24683879-3FA9593D-5A04-4968-89E1-6D4BEDF1A844Q27307288-8B3EC5A2-F76A-4E1A-9A96-F317B37AC4A7Q27640373-A34B9807-3FBD-47D9-8776-336E7BF658ABQ28363493-62138CE9-04D9-48DE-84FE-840F0D67709BQ28729756-CEF4EA27-1B91-462E-ADFF-96C922656C2CQ30479901-9E02FA33-DE07-4212-B6B1-53636419AFC7Q30538458-EB6A828B-148E-4FB1-A61A-2BA7AD4541F4Q33729244-D0740642-11F6-41EA-8F3D-F8C0285B8A34Q33964812-B90C0952-0596-4AF6-A90E-026C3C5531B0Q34021307-B71DE666-A02D-40BB-840D-93F401EEFE21Q34047483-C3BF6FF0-236D-44E0-9416-ABB9B712F231Q34446936-82D89FB8-70BB-4357-AE2B-8EF5CF1E22ACQ34771840-6FF6F684-3A00-45BE-8138-35A447462F9CQ35362918-74309624-0EDE-4845-99A1-63F1FB7B737BQ35827509-B630E9E5-02B8-46E5-896A-68C4555E734FQ36235486-6D112C65-6D35-4742-847A-DC396C173314Q36235682-2E057B37-1B1F-44B0-8B70-5F5CAECC06A8Q36236171-6824DCC0-A4AD-4F62-B7C3-65B75A2E628FQ36268138-EC54D904-7A65-4F7B-8A9C-BF4D47489F9EQ36312079-8D088E3C-4282-4FE9-9AE1-E8AD56214752Q36326132-CDF7FAFC-51C8-4B0A-8CB4-3A70E58FC87BQ36326421-E4F6C52A-C5F1-4546-8B42-8AFCE3356A1CQ36455713-BA60C473-4C54-475F-8E41-3C683197A5E9Q37366329-5D1844B3-DBFD-44A1-8E18-5E01937F87E1Q37387020-F568E6F9-4516-4279-B271-43719037BA37Q39148009-BFD9258C-325F-4E1E-B8E9-A8DEB5296195Q39540596-DEB3D883-21F2-47F3-84F8-9884C47031E2Q39647231-AED09E59-8F2B-40FA-AF6E-46989D90C0E7Q40386859-428C8DC1-11AA-4326-BC1C-9EF0E4E7F718Q40407916-87E78416-44B5-4514-91DA-8C4586070069Q42831434-80F630B1-C0C1-4FA5-B03D-64B904CA080F
P2860
Ezrin has properties to self-associate at the plasma membrane
description
1994 nî lūn-bûn
@nan
1994 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Ezrin has properties to self-associate at the plasma membrane
@ast
Ezrin has properties to self-associate at the plasma membrane
@en
Ezrin has properties to self-associate at the plasma membrane
@en-gb
Ezrin has properties to self-associate at the plasma membrane
@nl
type
label
Ezrin has properties to self-associate at the plasma membrane
@ast
Ezrin has properties to self-associate at the plasma membrane
@en
Ezrin has properties to self-associate at the plasma membrane
@en-gb
Ezrin has properties to self-associate at the plasma membrane
@nl
prefLabel
Ezrin has properties to self-associate at the plasma membrane
@ast
Ezrin has properties to self-associate at the plasma membrane
@en
Ezrin has properties to self-associate at the plasma membrane
@en-gb
Ezrin has properties to self-associate at the plasma membrane
@nl
P2093
P1476
Ezrin has properties to self-associate at the plasma membrane
@en
P2093
P304
P407
P478
107 ( Pt 9)
P577
1994-09-01T00:00:00Z