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.

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.

Item

http://www.wikidata.org/entity/Q35956572

Q35956572

about

Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering Ezrin/Radixin/Moesin proteins and flotillins cooperate to promote uropod formation in T cells The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition Ezrin activation by LOK phosphorylation involves a PIP2-dependent wedge mechanism.Dynamics of ezrin and EBP50 in regulating microvilli on the apical aspect of epithelial cells.PIP2 regulates psychostimulant behaviors through its interaction with a membrane protein.Morphogenesis of the mouse neural plate depends on distinct roles of cofilin 1 in apical and basal epithelial domains.Inhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin.Coordinate control of cytoskeletal remodeling and calcium mobilization during T-cell activation Interactome analysis reveals ezrin can adopt multiple conformational states.FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.Class I myosins in B-cell physiology: functions in spreading, immune synapses, motility, and vesicular traffic.Interactions between Epac1 and ezrin in the control of endothelial barrier function.Phosphatidylinositol 4,5-bisphosphate alters the number of attachment sites between ezrin and actin filaments: a colloidal probe study Actin, actin-binding proteins, and actin-related proteins in the nucleus.Mode of Ezrin-Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation.The actin-binding ERM protein Moesin directly regulates spindle assembly and function during mitosis.Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes.PIPKIγ and talin couple phosphoinositide and adhesion signaling to control the epithelial to mesenchymal transition.A phosphatidylinositol 4,5-bisphosphate redistribution-based sensing mechanism initiates a phagocytosis programing Sequential binding of ezrin and moesin to L-selectin regulates monocyte protrusive behaviour during transendothelial migration

P2860

Q28273758-603F0203-637D-49EE-B818-5DF6B82F38CE Q30538458-2A1CE35B-4C01-476D-AAF3-55272F47EDBF Q30544681-232D4F55-45C8-40F7-9F98-21782BE30D26 Q33591167-834B6C83-3D35-4DD7-B6EE-66DC88033B55 Q33692637-E32BDDDF-7425-49D2-A33E-CFAB4DADD371 Q33773594-965BABCF-E3A7-4F36-8E68-782D246780AA Q35228886-5CC0BBCE-C702-4FFB-8895-2B87639E05BF Q37114717-9053997C-EA8B-40A3-AD28-A04A8762C5DA Q37298815-D45F1CE0-64E7-4EF8-BAF5-A583DACC025B Q37368704-680AFD22-F3D7-4FB0-A190-CC3C6C06CD37 Q37382363-637E9FD2-00A3-40A9-B7B5-1B48B9D95055 Q38151852-20F0242B-EE53-42F8-93DF-35B7C2402937 Q38197313-7108D061-5F85-4FBD-823A-11CCCCEC647B Q38609066-FA42A902-6133-4204-8ACC-F19F3475903B Q38723568-077837A8-9620-4920-B994-45B23495C100 Q42547381-EC5870BE-85B7-4B5B-85A9-31CC936B52F9 Q46357719-6A4861AA-0F0A-4795-B3DC-982B1563F81D Q47213612-30E75701-9512-4648-B168-1C214DEAFF95 Q48144836-95C58A80-7E4E-43FC-8E3B-FA87C57D49F8 Q57464729-C4A34F4A-747C-4348-98A8-A0A9A78A12A1 Q58195107-B926C7FB-C25F-4F1E-AB86-EE584511398A

P2860

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.

Item

http://www.wikidata.org/entity/Q35956572

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@ast

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@en

type

Item

label

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@ast

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@en

prefLabel

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@ast

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@en

P1476

Activation of moesin, a protei ...... sing an autoinhibitory linker.

@en

P2093

Catherine Picart

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

Genaro Patino-Lopez

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

Jay R Knutson

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

Jian-Jiang Hao

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

Khadija Ben-Aissa

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

Michael J Kruhlak

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

Natalya V Belkina

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

Ofelia Maniti

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

Stephen Shaw

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

Tilman Rosales

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

P2860

NHERF1/EBP50 head-to-tail intramolecular interaction masks association with PDZ domain ligands

The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain

LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation

Discovery of the principal specific transcription factors of Apicomplexa and their implication for the evolution of the AP2-integrase DNA binding domains

Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain

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

Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

General and Versatile Autoinhibition of PLC Isozymes

Structural Basis for CD44 Recognition by ERM Proteins

P304

16311-16323

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

P31

scholarly article

P356

10.1074/JBC.M111.304881

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

P407

English

P433

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

P478

287

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

P577

2012-03-20T00:00:00Z

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

P698

22433855

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

P921

cytoskeleton

P932

3351316

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

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.

about

P2860

P2860

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.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932