Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53 - Wikidata - wikimedia - TriplyDB

Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53

Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53

http://www.wikidata.org/entity/Q24557455

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The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis.Structural basis of membrane invagination by F-BAR domains.Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures Regulation of IRSp53-dependent filopodial dynamics by antagonism between 14-3-3 binding and SH3-mediated localization.Kank attenuates actin remodeling by preventing interaction between IRSp53 and Rac1 The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASP External push and internal pull forces recruit curvature-sensing N-BAR domain proteins to the plasma membrane The BAR domain proteins: molding membranes in fission, fusion, and phagy Targeted wild-type and jerker espins reveal a novel, WH2-domain-dependent way to make actin bundles in cells Let's go bananas: revisiting the endocytic BAR code Amphipathic motifs in BAR domains are essential for membrane curvature sensing Cortactin branches out: roles in regulating protrusive actin dynamics Structural basis for the actin-binding function of missing-in-metastasis Exploring the role of lipids in intercellular conduits: breakthroughs in the pipeline Membrane curvature and its generation by BAR proteins The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions IRSp53 senses negative membrane curvature and phase separates along membrane tubules.Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping Membrane sculpting by F-BAR domains studied by molecular dynamics simulations Murine missing in metastasis (MIM) mediates cell polarity and regulates the motility response to growth factors Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli.Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors Dynamic filopodia are required for chemokine-dependent intracellular polarization during guided cell migration in vivo Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex The insulin receptor substrate of 53 kDa (IRSp53) limits hippocampal synaptic plasticity Emergence of FGFR family gene fusions as therapeutic targets in a wide spectrum of solid tumours Depletion or over-expression of Sh3px1 results in dramatic changes in cell morphology.IRSp53 mediates podosome formation via VASP in NIH-Src cells.The BAR Domain Superfamily Proteins from Subcellular Structures to Human Diseases F-BAR domain proteins: Families and function.The proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins.The interplay between Eps8 and IRSp53 contributes to Src-mediated transformation.Membrane targeting of WAVE2 is not sufficient for WAVE2-dependent actin polymerization: a role for IRSp53 in mediating the interaction between Rac and WAVE2.Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac.Four-scale description of membrane sculpting by BAR domains Assembly of filopodia by the formin FRL2 (FMNL3)The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently.Dynamin1 is a novel target for IRSp53 protein and works with mammalian enabled (Mena) protein and Eps8 to regulate filopodial dynamics.

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P2860

Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53

http://www.wikidata.org/entity/Q24557455

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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Structural basis of filopodia ...... omology domain of human IRSp53

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SJ.EMBOJ.7600535

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The EMBO Journal

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Structural basis of filopodia ...... omology domain of human IRSp53

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Guillaume Bompard

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Laura M Machesky

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Man Yeung Heung

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Thomas H Millard

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P2860

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling

Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin

The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways

Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex

MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta

Novel espin actin-bundling proteins are localized to Purkinje cell dendritic spines and bind the Src homology 3 adapter protein insulin receptor substrate p53

IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness

A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein

Improved methods for building protein models in electron density maps and the location of errors in these models

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240-250

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10.1038/SJ.EMBOJ.7600535

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2

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24

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Klaus Fütterer

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8096677

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15635447

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545821

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