Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
about
Association of villin with phosphatidylinositol 4,5-bisphosphate regulates the actin cytoskeletonBinding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed endMammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulatedMammalian CARMIL inhibits actin filament capping by capping proteinThe two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers.Review series: The cell biology of hearingSwf1p, a member of the DHHC-CRD family of palmitoyltransferases, regulates the actin cytoskeleton and polarized secretion independently of its DHHC motifThe role of CKIP-1 in cell morphology depends on its interaction with actin-capping proteinThe yeast actin cytoskeleton: from cellular function to biochemical mechanismEna/VASP proteins enhance actin polymerization in the presence of barbed end capping proteinsCapping protein regulators fine-tune actin assembly dynamicsStructural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilinCrystal structure of CapZ: structural basis for actin filament barbed end cappingStructural basis and evolutionary origin of actin filament capping by twinfilin.Capping protein binding to actin in yeast: biochemical mechanism and physiological relevance.High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo.Actin filament elongation in Arp2/3-derived networks is controlled by three distinct mechanisms.V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping proteinSingle molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteinsAllosteric N-WASP activation by an inter-SH3 domain linker in NckDistinct Actin and Lipid Binding Sites in Ysc84 Are Required during Early Stages of Yeast EndocytosisCARMIL is a bona fide capping protein interactant.WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.Arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.Ena/VASP proteins capture actin filament barbed ends.Formation of filopodia-like bundles in vitro from a dendritic network.Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motilityDirect observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3.Arp2/3 complex ATP hydrolysis promotes lamellipodial actin network disassembly but is dispensable for assemblyProtein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural dataCharacterization of engineered actin binding proteins that control filament assembly and structure.Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast.Twinfilin-2a is dispensable for mouse developmentActin filament attachments for sustained motility in vitro are maintained by filament bundling.End versus side branching by Arp2/3 complexVASP is a processive actin polymerase that requires monomeric actin for barbed end association.A balance of capping protein and profilin functions is required to regulate actin polymerization in Drosophila bristle.Genetic evidence of a role for membrane lipid composition in the regulation of soluble NEM-sensitive factor receptor function in Saccharomyces cerevisiaeActin and endocytosis in budding yeast.
P2860
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P2860
Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
description
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2001
@ast
im Oktober 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/10/15)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/10/15)
@nl
наукова стаття, опублікована в жовтні 2001
@uk
مقالة علمية (نشرت في 15-10-2001)
@ar
name
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@ast
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@en
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@nl
type
label
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@ast
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@en
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@nl
prefLabel
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@ast
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@en
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@nl
P2093
P2860
P356
P1476
Interactions with PIP2, ADP-ac ...... ocalization of yeast twinfilin
@en
P2093
P Lappalainen
S Palmgren
P2860
P304
P356
10.1083/JCB.200106157
P407
P577
2001-10-15T00:00:00Z