Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides - Wikidata - wikimedia - TriplyDB

Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides

Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides

http://www.wikidata.org/entity/Q24645681

about

Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP Advanced glycation end-products induce calpain-mediated degradation of ezrin Modulated interaction of the ERM protein, moesin, with CD93 Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes.Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane Imaging of dynamic changes of the actin cytoskeleton in microextensions of live NIH3T3 cells with a GFP fusion of the F-actin binding domain of moesin Biochemical, electron microscopic and immunohistological observations of cationic detergent-extracted cells: detection and improved preservation of microextensions and ultramicroextensions.A glimpse of the ERM proteins Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.Protein phosphatase 2C inactivates F-actin binding of human platelet moesin A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility Leucine-rich repeat kinase 2 modulates retinoic acid-induced neuronal differentiation of murine embryonic stem cells LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein moesin Characterization of a novel interaction between ELMO1 and ERM proteins.The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors.The PDZ-adaptor protein syntenin-1 regulates HIV-1 entry Characterization 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.G protein-coupled receptor kinase 2 activates radixin, regulating membrane protrusion and motility in epithelial cells.Talin 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.Dephosphorylation-dependent inhibitory activity of juxtanodin on filamentous actin disassembly.Molecular analysis of microscopic ezrin dynamics by two-photon FRAP.Activation of F-actin binding capacity of ezrin: synergism of PIP₂ interaction and phosphorylation.Drosophila PI4KIIIalpha is required in follicle cells for oocyte polarization and Hippo signaling.Emerging role for ERM proteins in cell adhesion and migration.Membrane-cytoskeleton interactions during the formation of the immunological synapse and subsequent T-cell activation.Ezrin regulates E-cadherin-dependent adherens junction assembly through Rac1 activation.The Na+/H+ Exchanger-3 (NHE3) Activity Requires Ezrin Binding to Phosphoinositide and Its Phosphorylation.Na(+)/H(+) exchanger NHE1 as plasma membrane scaffold in the assembly of signaling complexes.Phosphorylation and activity of the tumor suppressor Merlin and the ERM protein Moesin are coordinately regulated by the Slik kinase.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.

P2860

Q24291063-FEB554BD-ADBD-4326-88F4-B992CC6BAAF8 Q24291083-7AED7A75-ED79-4B20-A811-984F7658BFBF Q24293645-72206F45-A6CA-4402-A335-34F025A87924 Q24299770-3C8DE915-F892-40E9-BEB5-2183D8AD3FE5 Q24300262-47CE4C3F-DAF0-410A-AFCA-E9FF7E266AB5 Q24555712-38D9F016-FFD8-4AF0-9790-965634DCF25D Q24676944-F199FB38-F14A-41DF-8268-3927E00024FB Q24680124-A8673D01-7400-46AF-B04F-1C19BE6A0005 Q24683879-5750ED1B-13A9-44DB-B3E7-A05FD499BE39 Q24795269-A7D9B76F-42D4-4FBE-A2AC-3C88D4B819ED Q24800143-6DE8E972-78B4-4984-8A3B-2B2B13214891 Q26765004-F91291E0-EB24-499F-8802-4553BD58B5D6 Q27640373-8E73AB65-D8AC-45EC-8BC9-C67025234848 Q28144127-6CE1CAA4-C4D3-4924-8E16-EAEA651A1978 Q28215157-CE5266C2-E758-4FAA-A011-381EF769A048 Q28273758-7FCC036B-B729-4892-A48D-391E3F23A6D3 Q28365540-433D8FB9-B1E0-401D-BCF0-61612B5FA7BA Q28366134-DA0E0AA9-2923-466E-A425-E0CAC29A8522 Q28743800-60F4C203-E47C-409D-8643-CBEF34103693 Q29615144-4007873E-9C3E-490F-A112-DCDBED253971 Q30372875-3D4A2581-B706-4FA6-9724-36A1C1E60DD6 Q30439052-D070774E-359C-4A3C-86E7-7802BE63EE02 Q30477995-90BD7E58-0246-49B5-9760-F1068D327649 Q30515961-D220A769-7F3F-4A4A-80B1-81273F50427A Q31148511-8FE5B66E-3FD2-4890-8324-5DEBA62F60D3 Q31655533-02D38363-1CAC-4C3A-9DBE-7590C22D2FD2 Q33729244-E15688D5-DEDA-48AB-9A1E-38CE339B394F Q33731231-8149CD1C-E3E2-4E8C-BE33-F5A0B2375BB9 Q33748611-CD3B8948-AA71-4B04-919A-2E990A07640A Q34121369-D814FA47-CE06-4013-944A-17C903C6FD5F Q34189987-B640D74E-359C-4346-8C62-95C18A5E5D18 Q34771840-0A241E0B-524B-4CC6-BE70-4002A59EDCC3 Q34781388-5EFFBBFD-EF90-45AC-91BE-83DE9CE859CA Q34891331-79DFD025-609B-416A-9D82-AB7890C33D6C Q35005880-302F47A3-8399-4DD3-BCD2-754BEAC62857 Q35153735-56E66757-1FE0-43FE-AAA9-63CB475FD8FA Q35652619-5191069D-4A05-4542-A1E1-963A7A57C2D6 Q35882115-D35CD86B-8F78-44E4-833C-1EEFFA111C90 Q36119138-6E0BD3F8-93C3-4FA5-8ADC-4910F0530FD5 Q36326421-040A40B7-5A53-420B-9FB4-C9D151A7C4C4

P2860

Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides

http://www.wikidata.org/entity/Q24645681

description

1999 nî lūn-bûn

@nan

1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

name

Regulation of F-actin binding ...... and polyphosphatidylinositides

@ast

Regulation of F-actin binding ...... and polyphosphatidylinositides

@en

Regulation of F-actin binding ...... and polyphosphatidylinositides

@nl

type

label

Regulation of F-actin binding ...... and polyphosphatidylinositides

@ast

Regulation of F-actin binding ...... and polyphosphatidylinositides

@en

Regulation of F-actin binding ...... and polyphosphatidylinositides

@nl

prefLabel

Regulation of F-actin binding ...... and polyphosphatidylinositides

@ast

Regulation of F-actin binding ...... and polyphosphatidylinositides

@en

Regulation of F-actin binding ...... and polyphosphatidylinositides

@nl

P1433

Q24645681-0C409803-F438-4991-A190-8AAD8C8BE6CE

P1476

Q24645681-C8CEE280-1E07-460F-BB74-F504D3E72B91

P2093

Q24645681-1F379208-2CA1-4C95-A802-A6555DD10C71

Q24645681-B19CE855-55F9-450A-81C4-4058F4C26223

Q24645681-B53E620E-0A88-411E-888E-1B9355BFED82

Q24645681-CE94E0B0-8BC4-465F-9025-8F99BC35E143

Q24645681-D2ABB49A-A25C-4807-939C-F0756FF31412

P2860

Q24645681-034EC773-5F40-4717-AFBB-EE2EB7C5488A

Q24645681-0A4C1AD8-171E-4DE1-8037-880001DAC7D6

Q24645681-0A4DC020-C3C5-4FC9-A88A-ED9E30564134

Q24645681-0FF46B28-1858-42D3-96FD-82B983E04047

Q24645681-1B85955F-794B-4755-B84C-A1264214DE6C

Q24645681-1DAB2D0B-6DD7-4B95-81C3-A7C9AAF984C6

Q24645681-1F5B2827-C665-45F6-A55F-31788700533A

Q24645681-21E54FE2-E5A2-4683-B57A-6C585F7F3DB5

Q24645681-246917CD-BD9D-4A7F-80FD-D142EAA65A8A

Q24645681-2C4547F2-6D00-4623-BCB3-FA5CB0D8EE4E

P304

Q24645681-A58B5423-1242-4E8F-B6F1-2C06D20EE78D

P31

Q24645681-EF965B81-9A7B-4CEC-B1E7-F7A897289D92

P356

Q24645681-85BBD60A-505F-4733-8340-D4C1BDFA2863

P407

Q24645681-8B2215A8-C0D8-415F-879A-E3B949BD1CED

P433

Q24645681-476CD145-DF1E-4B7B-9309-2E983E5DFFE0

P478

Q24645681-B4AA5F46-2DA6-4A11-B424-0152CD2C74AB

P577

Q24645681-3874571E-7D46-4F1E-9F95-5EDA6A7C4BE4

P5875

Q24645681-F8773F04-70AB-4E9A-B900-980B606562D9

P698

Q24645681-6FB63DDF-0A93-426A-882E-8946CFED8AC2

P921

Q24645681-19264531-00A1-48EF-BADA-1483A4F8337A

P932

Q24645681-0F7C9F1C-1209-4B0C-A028-F2B9DDFD06F9

P356

P1433

Molecular Biology of the Cell

P1476

Regulation of F-actin binding ...... and polyphosphatidylinositides

@en

P2093

E J Luna

http://www.w3.org/2001/XMLSchema#string

F Nakamura

http://www.w3.org/2001/XMLSchema#string

H Furthmayr

http://www.w3.org/2001/XMLSchema#string

K Pestonjamasp

http://www.w3.org/2001/XMLSchema#string

L Huang

http://www.w3.org/2001/XMLSchema#string

P2860

F-actin binding site masked by the intramolecular association of vinculin head and tail domains

Moesin: a member of the protein 4.1-talin-ezrin family of proteins

A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation

Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site

Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway

Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association

Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family

A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization

Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization

A simple method for displaying the hydropathic character of a protein

P304

2669-85

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1091/MBC.10.8.2669

http://www.w3.org/2001/XMLSchema#string

P407

P433

8

http://www.w3.org/2001/XMLSchema#string

P478

10

http://www.w3.org/2001/XMLSchema#string

P577

1999-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12863800

http://www.w3.org/2001/XMLSchema#string

P698

10436021

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

25498

http://www.w3.org/2001/XMLSchema#string