First-pass extracted concept

uPAR interactome

Candidate: concept label1 source documents5 linked claims
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Evidence Snippets

This review describes the soluble ligands and lateral partners of the uPAR interactome, the mechanisms regulating uPAR interactions and their proved and/or potential biological functions.
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1biological role summarysupports2011Source 1DOIPubMed

The diversity of the uPAR interactome links uPAR to major biological systems including blood coagulation, complement, and plasma kallikrein-kinin cascades.

Quoted textsource-backed
uPAR appears to be an essential player of major biological systems including the blood coagulation, complement and plasma kallikrein-kinin cascades.
Claim 2family interaction summarysupports2011Source 1DOIPubMed

uPAR interacts with members of the GPCR, receptor tyrosine kinase, and integrin receptor families, implying a broad interactome.

Quoted textsource-backed
The fact that uPAR interacts with members of three major families of membrane receptors i.e. G protein-coupled receptors, receptor tyrosine kinases, and integrins implies that the actual number of components constituting the uPAR interacome is extremely high.
Claim 3ligand example summarysupports2011Source 1DOIPubMed

The review identifies uPA, vitronectin, factor XII, and SRPX2 as reported uPAR ligands associated with proteolysis, adhesion, coagulation-related biology, and language-development-related biology.

Quoted textsource-backed
The urokinase receptor (uPAR) was originally identified as the membrane receptor of the serine protease urokinase (uPA)... Later on, vitronectin was showed to be another major ligand... Other unrelated ligands have been subsequently reported including for example factor XII and SRPX2 expanding the functions of uPAR to unexpected biological areas such as the initiation of the coagulation cascade or the regulation of language development.
Claim 4mechanistic summarysupports2011Source 1DOIPubMed

Because uPAR is GPI-anchored and lacks an intracellular domain, its signaling is mediated through lateral interactions with other plasma membrane components.

Quoted textsource-backed
Due to its glycosylphosphatidylinositol (GPI) anchor, uPAR has no intracellular domain and thus exerts its signaling capacity through lateral interactions with other components of the plasma membrane that actually mediate uPAR-induced signals.
Claim 5review scope summarysupports2011Source 1DOIPubMed

uPAR has been reported to interact directly with 42 proteins, comprising 9 soluble ligands and 33 lateral partners.

Quoted textsource-backed
As yet, a total 42 proteins interacting directly with uPAR can be numbered comprising 9 soluble ligands and 33 lateral partners.