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

Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation.

Experimental cell research - 15 Nov 2005

Hetey Sara E, Lalonde David P, Turner Christopher E

Abstract excerpt

The focal adhesion protein Hic-5, a homologue to paxillin, has been shown to be tyrosine-phosphorylated in fibroblasts in response to stimuli such as osmotic stress, serum, LPA and endothelin. However, the function of this modification to Hic-5 is unclear. Herein, we show that Hic-5 is tyrosine-phosphorylated on residues 38 and 60 following epidermal growth factor (EGF) treatment of COS-7 cells, coincident with...

Read the complete abstract on PubMed

Topics

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

Share to Chlorocebus aethiops
Share to Epidermal Growth Factor
Share to Focal Adhesions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to LIM Domain Proteins

Share to Paxillin

Share to Pseudopodia

Share to rac GTP-Binding Proteins

Share to Tyrosine

Source

Identifiers

PMID: 16183059
DOI: 10.1016/j.yexcr.2005.08.011

Genes

EGF
LPA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation.PMID 16183059Read ↗

Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn.Semantic proximity Read ↗

Transcriptional activation of the c-fos gene by a LIM protein, Hic-5.Semantic proximity Read ↗

[Regulation of cellular phenotypes by Hic-5 that localizes both in the focal adhesion and in the nucleus].Semantic proximity Read ↗

A LIM protein, Hic‐5, functions as a potential coactivator for Sp1Semantic proximity Read ↗

Hic-5 expression is a major indicator of cancer cell morphology, migration, and plasticity in three-dimensional matrices.Semantic proximity Read ↗

Hic-5 contributes to epithelial-mesenchymal transformation through a RhoA/ROCK-dependent pathway.Semantic proximity Read ↗

Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.Semantic proximity Read ↗

Hic-5 promotes the hypertrophic scar myofibroblast phenotype by regulating the TGF-beta1 autocrine loop.Semantic proximity Read ↗

Cell Cycle-Regulated Processing of HEF1 to Multiple Protein Forms Differentially Targeted to Multiple Subcellular CompartmentsSemantic proximity Read ↗

Hic-5 transduces mechanical force that drives a vicious cycle of bronchoconstrictionSemantic proximity Read ↗

Identification and characterization of hic-5/ARA55 as an hsp27 binding protein.Semantic proximity Read ↗

Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions.Semantic proximity Read ↗

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