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

The interaction between uPAR and vitronectin triggers ligand-independent adhesion signalling by integrins.

The EMBO journal - 3 Nov 2014

Ferraris Gian Maria Sarra, Schulte Carsten, Buttiglione Valentina, De Lorenzi Valentina, Piontini Andrea, Galluzzi Massimiliano, Podestà Alessandro, Madsen Chris D, Sidenius Nicolai

Abstract excerpt

The urokinase-type plasminogen activator receptor (uPAR) is a non-integrin vitronectin (VN) cell adhesion receptor linked to the plasma membrane by a glycolipid anchor. Through structure-function analyses of uPAR, VN and integrins, we document that uPAR-mediated cell adhesion to VN triggers a novel type of integrin signalling that is independent of integrin-matrix engagement. The signalling is fully active on VN...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion
Share to HEK293 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Integrins

Share to Mutation

Share to Receptors, Urokinase Plasminogen Activator

Share to Signal Transduction

Share to Vitronectin

Source

Open in PubMed Open full text

Identifiers

PMID: 25168639
DOI: 10.15252/embj.201387611
PMCID: PMC4283405

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

The interaction between uPAR and vitronectin triggers ligand-independent adhesion signalling by integrins.PMID 25168639Read ↗

Regulation of alpha5beta1 integrin conformation and function by urokinase receptor binding.Semantic proximity Read ↗

Rational Targeting of the Urokinase Receptor (uPAR): Development of Antagonists and Non-Invasive Imaging ProbesSemantic proximity Read ↗

Domain 2 of the urokinase receptor contains an integrin-interacting epitope with intrinsic signaling activity: generation of a new integrin inhibitor.Semantic proximity Read ↗

Crystal structure of the urokinase receptor in a ligand-free form.Semantic proximity Read ↗

Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growthSemantic proximity Read ↗

Integrin signalling and function in immune cellsSemantic proximity Read ↗

Sequences within domain II of the urokinase receptor critical for differential ligand recognition.Semantic proximity Read ↗

Crystal Structure and Cellular Functions of uPAR DimerSemantic proximity Read ↗

Negative regulation of uPAR activity by a GPI-specific phospholipase CSemantic proximity Read ↗

An uncleavable uPAR mutant allows dissection of signaling pathways in uPA-dependent cell migration.Semantic proximity Read ↗

Integrin signaling: it's where the action isSemantic proximity Read ↗

The integrin adhesome network at a glanceSemantic proximity Read ↗

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