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

Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex.

The Journal of biological chemistry - 14 Apr 2006

Kelly Alexander E, Kranitz Heather, Dötsch Volker, Mullins R Dyche

Abstract excerpt

The Arp2/3 complex nucleates and cross-links actin filaments at the leading edge of motile cells, and its activity is stimulated by C-terminal regions of WASP/Scar proteins, called VCA domains. VCA domains contain a verprolin homology sequence (V) that binds monomeric actin and central (C) and acidic sequences (A) that bind the Arp2/3 complex. Here we show that the C domain binds to monomeric actin with higher...

Read the complete abstract on PubMed

Topics

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

Share to Actin-Related Protein 2-3 Complex
Share to Actins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Anisotropy

Share to Cross-Linking Reagents

Share to Glutathione Transferase

Share to Magnetic Resonance Spectroscopy

Share to Microscopy, Fluorescence

Share to Wiskott-Aldrich Syndrome Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 16403731
DOI: 10.1074/jbc.M507470200
PMCID: PMC3077991

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex.PMID 16403731Read ↗

Activation of Arp2/3 complex-dependent actin polymerization by plant proteins distantly related to Scar/WAVESemantic proximity Read ↗

Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complexSemantic proximity Read ↗

Regulation of Actin Dynamics by WASP Family ProteinsSemantic proximity Read ↗

The WASP and WAVE family proteinsSemantic proximity Read ↗

Branching out in different directions: Emerging cellular functions for the Arp2/3 complex and WASP-family actin nucleation factorsSemantic proximity Read ↗

ARPC5 Isoforms and Their Regulation by Calcium-Calmodulin-N-WASP Drive Distinct Arp2/3-dependent Actin Remodeling Events in CD4 T CellsSemantic proximity Read ↗

Direct Actin Monomer Delivery is a WASP-specific Requirement for Arp2/3 Complex Activation.Semantic proximity Read ↗

Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization.Semantic proximity Read ↗

Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments.Semantic proximity Read ↗

Requirement of the basic region of N-WASP/WAVE2 for actin-based motility.Semantic proximity Read ↗

WICH, a Novel Verprolin Homology Domain-Containing Protein That Functions Cooperatively with N-WASP in Actin-Microspike FormationSemantic proximity Read ↗

Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton.Semantic proximity Read ↗

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