Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Villin severing activity enhances actin-based motility in vivo.

Molecular biology of the cell - 1 Mar 2007

Revenu Céline, Courtois Matthieu, Michelot Alphée, Sykes Cécile, Louvard Daniel, Robine Sylvie

Abstract excerpt

Villin, an actin-binding protein associated with the actin bundles that support microvilli, bundles, caps, nucleates, and severs actin in a calcium-dependant manner in vitro. We hypothesized that the severing activity of villin is responsible for its reported role in enhancing cell plasticity and motility. To test this hypothesis, we chose a loss of function strategy and introduced mutations in villin based on...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Actin Cytoskeleton
Share to Actins
Share to Dogs

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Microfilament Proteins

Share to Microspheres

Share to Mutant Proteins

Share to Rabbits

Share to Shigella flexneri

Source

Open in PubMed Open full text

Identifiers

PMID: 17182858
DOI: 10.1091/mbc.e06-05-0423
PMCID: PMC1805090

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Villin severing activity enhances actin-based motility in vivo.PMID 17182858Read ↗

Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin.Semantic proximity Read ↗

Arabidopsis VILLIN5, an actin filament bundling and severing protein, is necessary for normal pollen tube growth.Semantic proximity Read ↗

Arabidopsis VILLIN4 is involved in root hair growth through regulating actin organization in a Ca2+-dependent manner.Semantic proximity Read ↗

An actin footprint on villin. Single site substitutions in a cluster of basic residues inhibit the actin severing but not capping activity of villin.Semantic proximity Read ↗

An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin.Semantic proximity Read ↗

Enterocyte loss of polarity and gut wound healing rely upon the F-actin-severing function of villin.Semantic proximity Read ↗

Arabidopsis villins promote actin turnover at pollen tube tips and facilitate the construction of actin collars.Semantic proximity Read ↗

Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton.Semantic proximity Read ↗

High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.Semantic proximity Read ↗

Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility.Semantic proximity Read ↗

High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity.Semantic proximity Read ↗

Multiple actin binding domains of Ena/VASP proteins determine actin network stiffening.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.