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

Ena/VASP proteins have an anti-capping independent function in filopodia formation.

Molecular biology of the cell - 1 Jul 2007

Applewhite Derek A, Barzik Melanie, Kojima Shin-Ichiro, Svitkina Tatyana M, Gertler Frank B, Borisy Gary G

Abstract excerpt

Filopodia have been implicated in a number of diverse cellular processes including growth-cone path finding, wound healing, and metastasis. The Ena/VASP family of proteins has emerged as key to filopodia formation but the exact mechanism for how they function has yet to be fully elucidated. Using...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules
Share to Cell Polarity
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to Fluorescence Recovery After Photobleaching

Share to Microfilament Proteins

Share to Pseudopodia

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 17475772
DOI: 10.1091/mbc.e06-11-0990
PMCID: PMC1924831

Genes

VASP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17475772-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ena/VASP proteins have an anti-capping independent function in filopodia formation.PMID 17475772Read ↗

Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration.Semantic proximity Read ↗

Defining functional interactions during biogenesis of epithelial junctions.Semantic proximity Read ↗

GEF at work: Vav in protruding filopodia.Semantic proximity Read ↗

Looking over the edge: a new role for Ena/VASP proteins in lamellipodial dynamics.Semantic proximity Read ↗

CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility.Semantic proximity Read ↗

Exploring the roles of diaphanous and enabled activity in shaping the balance between filopodia and lamellipodia.Semantic proximity Read ↗

Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.Semantic proximity Read ↗

Filopodia formation and endosome clustering induced by mutant plus-end-directed myosin VI.Semantic proximity Read ↗

Filopodia are required for cortical neurite initiation.Semantic proximity Read ↗

Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Semantic proximity Read ↗

SWAP-70 identifies a transitional subset of actin filaments in motile cells.Semantic proximity Read ↗

Actin capping protein alpha maintains vestigial-expressing cells within the Drosophila wing disc epithelium.Semantic proximity Read ↗

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