Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | - |
Homo sapiens | 9986 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | urokinase-type plasmin activator, uPA, binding to uPA receptor, uPAR, induces migration/invasion through multiple interactors including integrins, overview. ECRG2 binds specifically to the kringle domain of uPA, and forms a complex with uPA-uPAR, the trinary complex modifies the dynamical association of uPAR with beta1 integrins. Identification of ECRG2-binding sequence in uPA, overview. Complex disruption inhibits the Src/mitogen-activated protein kinase pathway, resulting in suppression of cell migration/invasion | ? | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HT-1080 cell | a fibrosarcoma cell line | Homo sapiens | - |
MCF-7 cell | - |
Homo sapiens | - |
MDA-MB-231 cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | urokinase-type plasmin activator, uPA, binding to uPA receptor, uPAR, induces migration/invasion through multiple interactors including integrins, overview. ECRG2 binds specifically to the kringle domain of uPA, and forms a complex with uPA-uPAR, the trinary complex modifies the dynamical association of uPAR with beta1 integrins. Identification of ECRG2-binding sequence in uPA, overview. Complex disruption inhibits the Src/mitogen-activated protein kinase pathway, resulting in suppression of cell migration/invasion | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
uPA | - |
Homo sapiens |
urokinase-type plasmin activator | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the uPA-uPA receptor, uPAR, system plays a critical role in the regulation of cancer cell migration, extracellular matrix invasion, and metastasis. uPA binds with high affinity to a cell surface uPAR, that is a heavily glycosylated glycosylphosphatidylinositol-anchored protein formed by three cysteine-rich LY6-like extracellular domains. uPA-uPAR promotes extracellular proteolysis by regulating plasminogen activation, uPA-uPAR regulates cell-extracellular matrix interactions as an adhesion receptor for vitronectin and through its capacity to modulate integrin function, and uPA-uPAR regulates cell migration as a signal transduction molecule and by its intrinsic chemotactic activity. Src/MAP kinase, but not FAK and PI3K, is involved in ECRG2-regulated, uPA-dependent cell migration/invasion | Homo sapiens |