Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets.
about
Evolution and origin of merlin, the product of the Neurofibromatosis type 2 (NF2) tumor-suppressor geneIdentification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARPAndrogen regulation of the human FERM domain encoding gene EHM2 in a cell model of steroid-induced differentiationArp2/3 complex is required for actin polymerization during platelet shape changeRegulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositidesRegulation 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-2ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosisRho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail associationMoesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarizationMorphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membraneImaging of dynamic changes of the actin cytoskeleton in microextensions of live NIH3T3 cells with a GFP fusion of the F-actin binding domain of moesinBiochemical, electron microscopic and immunohistological observations of cationic detergent-extracted cells: detection and improved preservation of microextensions and ultramicroextensions.A glimpse of the ERM proteinsAn in vivo EGF receptor localization screen in C. elegans Identifies the Ezrin homolog ERM-1 as a temporal regulator of signalingProtein phosphatase 2C inactivates F-actin binding of human platelet moesinOrganizing the cell cortex: the role of ERM proteinsNormal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockoutA congenital activating mutant of WASp causes altered plasma membrane topography and adhesion under flow in lymphocytes.Asymmetric division of cyst stem cells in Drosophila testis is ensured by anaphase spindle repositioning.Radixin is involved in lamellipodial stability during nerve growth cone motilityCharacterization of protein kinase A-mediated phosphorylation of ezrin in gastric parietal cell activation.Hierarchy of merlin and ezrin N- and C-terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP.Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism.MiR-200c Inhibits the Tumor Progression of Glioma via Targeting MoesinTalin regulates moesin-NHE-1 recruitment to invadopodia and promotes mammary tumor metastasis.Sip1, the Drosophila orthologue of EBP50/NHERF1, functions with the sterile 20 family kinase Slik to regulate Moesin activity.Down-regulation of protein kinase C alpha/ezrin signals in light-induced phagocytic crisis of retinal pigment epithelium cells.Spatial regulation of cyclic AMP-Epac1 signaling in cell adhesion by ERM proteins.Functional analysis of the neurofibromatosis type 2 protein by means of disease-causing point mutationsRole of moesin in renal fibrosis.Spatial control of proton pump H,K-ATPase docking at the apical membrane by phosphorylation-coupled ezrin-syntaxin 3 interaction.Telencephalin protects PAJU cells from amyloid beta protein-induced apoptosis by activating the ezrin/radixin/moesin protein family/phosphatidylinositol-3-kinase/protein kinase B pathway.Emerging role for ERM proteins in cell adhesion and migration.Slik and the receptor tyrosine kinase Breathless mediate localized activation of Moesin in terminal tracheal cells.Ezrin regulates NHE3 translocation and activation after Na+-glucose cotransport.Constitutively active ezrin increases membrane tension, slows migration, and impedes endothelial transmigration of lymphocytes in vivo in miceEzrin, radixin, and moesin are phosphorylated in response to 2-methoxyestradiol and modulate endothelial hyperpermeability.Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes.Activation of moesin, a protein that links actin cytoskeleton to the plasma membrane, occurs by phosphatidylinositol 4,5-bisphosphate (PIP2) binding sequentially to two sites and releasing an autoinhibitory linker.
P2860
Q21283962-2CC8DC24-57FC-46CD-946C-5CFB026210EAQ24291083-8329DE02-1CB3-4999-BC45-97F5BD92FE5FQ24296691-27709994-B175-46DD-8122-246D600AA9BAQ24603149-8712D1A4-AFA3-41F1-8E29-1A1A7C307289Q24645681-7BDA8EC8-AA83-4799-B0B5-751459D4C901Q24671083-99141CA9-FEB7-4613-9FAA-853E1BB78ED0Q24676628-345C1B28-023F-4FBD-B65B-E138EDCACEF8Q24676652-C32E566E-E469-4CD4-A2F4-625A8C846CE6Q24678197-F43932F0-0F41-476F-892E-98B59EE3B803Q24683747-D3EC9013-DDAA-404D-91BF-88A8885EFC40Q24683879-509068CB-38F5-4310-AFEB-B12190DD43B8Q24795269-402B3C85-314B-4BCC-BAB9-9C605967BAC3Q24800143-8C2D5A46-72E7-4276-BFFA-3E05F9539D3DQ26765004-28807815-E8BB-48B9-8DA3-A66D2BA3401EQ27315937-7C5FFACE-614F-4197-97EA-0F235ED1C3DCQ28144127-4FC6DF01-1F1E-4BA3-AEFC-6C68F72FC36BQ28277373-C8C61641-5B42-4B9A-A315-BBA0C45A880DQ28508442-A958E566-17C2-47F2-8FBE-8C1C5A13934FQ30496909-C249D8AD-64AF-4590-82EF-68AB73495C11Q30498121-C9FAC1DA-27A5-433A-9D54-931AD29BD2B4Q30629181-40C29F51-E3F5-4EFC-84E5-8E30B24D6E4FQ31148511-F7DD3EDB-1DB9-40B8-A7CB-7D7863C75B90Q31655533-2B55709A-3E9C-4F2B-91C7-8A0B9C4C56B1Q33591167-EC0CAD4D-A3DF-40EA-8B3C-409DCFAD1940Q33703121-E07BCDF2-DCD5-418F-9A8F-F06897F35B9CQ33731231-64B1FC66-CAF2-4088-9789-D2939D4CDEA6Q33748611-00B8532F-4309-45A3-A282-8FD50BD3A0D9Q33912446-883D98D4-BCC6-4A9B-9983-58A4388241D4Q34139017-E55AD7CA-B0DD-40A0-B785-47CA759BA315Q34145489-804B42D1-92FA-4DC8-B1DF-91CEAE358FBFQ34535574-232D280F-A63D-448C-8516-BD18BC2F71AAQ34580303-85ED4F26-67B0-4D93-9D10-D9466F3124E2Q34720146-A8420793-31F3-4ECE-9747-1B7AEC8DAEB3Q34891331-D1BC48B6-C267-4237-A0C5-542C47DD4330Q35213087-F3854C9A-5996-4E02-9E84-4A27DB901B0AQ35322212-75D34B72-B33A-4F1C-8D80-BADB34DC5388Q35669213-AC06EFEE-F273-4396-8727-885405EFA286Q35684785-D33CD33F-7D3B-46EA-9F5C-5096A510E68BQ35775396-20E7D1D2-B4F9-4BAA-B20D-6D01316387B1Q35956572-65EAFA84-5E44-4091-9249-455004E5F3C2
P2860
Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets.
description
1995 nî lūn-bûn
@nan
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Phosphorylation of threonine 5 ...... activation of human platelets.
@ast
Phosphorylation of threonine 5 ...... activation of human platelets.
@en
Phosphorylation of threonine 5 ...... activation of human platelets.
@nl
type
label
Phosphorylation of threonine 5 ...... activation of human platelets.
@ast
Phosphorylation of threonine 5 ...... activation of human platelets.
@en
Phosphorylation of threonine 5 ...... activation of human platelets.
@nl
prefLabel
Phosphorylation of threonine 5 ...... activation of human platelets.
@ast
Phosphorylation of threonine 5 ...... activation of human platelets.
@en
Phosphorylation of threonine 5 ...... activation of human platelets.
@nl
P2093
P2860
P356
P1476
Phosphorylation of threonine 5 ...... activation of human platelets.
@en
P2093
Furthmayr H
Nakamura F
P2860
P304
31377-31385
P356
10.1074/JBC.270.52.31377
P407
P577
1995-12-01T00:00:00Z