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

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

Biochemical and biophysical research communications - 4 Feb 1998

Miki H, Takenawa T

Abstract excerpt

Verprolin is a yeast protein whose inactivation leads to a cytoskeletal defect characterized by the abnormal organization of actin filaments. Recently, two mammalian proteins previously shown to regulate the actin cytoskeleton, Wiskott-Aldrich Syndrome Protein (WASP) and its homolog expressed in neurons (N-WASP), were found to possess short peptide motifs homologous to one part of verprolin. However, the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Fungal Proteins

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

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Fusion Proteins

Share to Saccharomyces cerevisiae Proteins

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 9473482
DOI: 10.1006/bbrc.1997.8064

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

Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization.PMID 9473482Read ↗

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

The WASP and WAVE family proteinsSemantic proximity Read ↗

N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases.Semantic proximity Read ↗

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

Wiskott-Aldrich syndrome (role of WASP).Semantic proximity Read ↗

WASP family proteins: Molecular mechanisms and implications in human diseaseSemantic proximity Read ↗

The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization.Semantic proximity Read ↗

Wiskott–Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinasesSemantic proximity Read ↗

A Complex of Wiskott-Aldrich Syndrome Protein with Mammalian Verprolins Plays an Important Role in Monocyte ChemotaxisSemantic proximity Read ↗

Regulation of Actin Dynamics by WASP Family ProteinsSemantic proximity Read ↗

The mammalian verprolin homologue WIRE participates in receptor-mediated endocytosis and regulation of the actin filament system by distinct mechanisms.Semantic proximity Read ↗

A DOCK8-WIP-WASp complex links T cell receptors to the actin cytoskeletonSemantic proximity Read ↗

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