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

WIP participates in actin reorganization and ruffle formation induced by PDGF.

Journal of cell science - 15 Jun 2003

Antón Inés M, Saville Stephen P, Byrne Michael J, Curcio Claudia, Ramesh Narayanaswamy, Hartwig John H, Geha Raif S

Abstract excerpt

Platelet-derived growth factor (PDGF) is a chemotactic factor for fibroblasts that triggers actin cytoskeleton reorganization by increasing the level of GTP-Rac, the activated form of a small Rho family GTPase. GTP-Rac induces membrane ruffling and lamellipodium formation that are required for adhesion, migration and macropinocytosis, among other functions. We have shown that WIP interacts with members of the...

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 Antibodies

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

Share to Cell Surface Extensions

Share to Fluorescent Antibody Technique

Share to Microscopy, Electron

Share to NIH 3T3 Cells

Share to Platelet-Derived Growth Factor

Source

Identifiers

PMID: 12724353
DOI: 10.1242/jcs.00433

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

WIP participates in actin reorganization and ruffle formation induced by PDGF.PMID 12724353Read ↗

WIP regulates N-WASP-mediated actin polymerization and filopodium formation.Semantic proximity Read ↗

Requirement for a Complex of Wiskott-Aldrich Syndrome Protein (WASP) with WASP Interacting Protein in Podosome Formation in MacrophagesSemantic proximity Read ↗

WIP and WASP play complementary roles in T cell homing and chemotaxis to SDF-1αSemantic proximity Read ↗

WHIMP links the actin nucleation machinery to Src-family kinase signaling during protrusion and motilitySemantic proximity Read ↗

WIP, a protein associated with Wiskott–Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cellsSemantic proximity Read ↗

N-WASP Involvement in Dorsal Ruffle Formation in Mouse Embryonic FibroblastsSemantic proximity Read ↗

Wiskott-Aldrich Syndrome Interacting Protein Deficiency Uncovers the Role of the Co-receptor CD19 as a Generic Hub for PI3 Kinase Signaling in B CellsSemantic proximity Read ↗

Filamin is essential in actin cytoskeletal assembly mediated by p21-activated kinase 1.Semantic proximity Read ↗

WIP is necessary for matrix invasion by breast cancer cellsSemantic proximity Read ↗

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

Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells.Semantic proximity Read ↗

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

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