| Online-Ressource |
Verfasst von: | Thomas, Markus [VerfasserIn]  |
| Felcht, Moritz [VerfasserIn]  |
| Kruse, Karoline [VerfasserIn]  |
| Kretschmer, Stella [VerfasserIn]  |
| Deppermann, Carleen [VerfasserIn]  |
| Biesdorf, Andreas [VerfasserIn]  |
| Rohr, Karl [VerfasserIn]  |
| Benest, Andrew V. [VerfasserIn]  |
| Fiedler, Ulrike [VerfasserIn]  |
| Augustin, Hellmut [VerfasserIn]  |
Titel: | Angiopoietin-2 stimulation of endothelial cells induces αvβ3 integrin internalization and degradation |
Werktitel: | Angiopoietin-2 stimulation of endothelial cells induces alpha v beta 3 integrin internalization and degradation |
Verf.angabe: | Markus Thomas, Moritz Felcht, Karoline Kruse, Stella Kretschmer, Carleen Deppermann, Andreas Biesdorf, Karl Rohr, Andrew V. Benest, Ulrike Fiedler, and Hellmut G. Augustin |
E-Jahr: | 2010 |
Jahr: | 2 June 2010 |
Umfang: | 8 S. |
Fussnoten: | Gesehen am 15.11.2023 |
Titel Quelle: | Enthalten in: The journal of biological chemistry |
Ort Quelle: | Bethesda, Md. : ASBMB Publications, 1905 |
Jahr Quelle: | 2010 |
Band/Heft Quelle: | 285(2010), 31, Seite 23842-23849 |
ISSN Quelle: | 1083-351X |
Abstract: | The angiopoietins (Ang-1 and Ang-2) have been identified as agonistic and antagonistic ligands of the endothelial receptor tyrosine kinase Tie2, respectively. Both ligands have been demonstrated to induce translocation of Tie2 to cell-cell junctions. However, only Ang-1 induces Tie2-dependent Akt activation and subsequent survival signaling and endothelial quiescence. Ang-2 interferes negatively with Ang-1/Tie2 signaling, thereby antagonizing the Ang-1/Tie2 axis. Here, we show that both Ang-1 and Ang-2 recruit β3 integrins to Tie2. This co-localization is most prominent in cell-cell junctions. However, only Ang-2 stimulation resulted in complex formation among Tie2, αvβ3 integrin, and focal adhesion kinase as evidenced by co-immunoprecipitation experiments. Focal adhesion kinase was phosphorylated in the FAT domain at Ser910 upon Ang-2 stimulation and the adaptor proteins p130Cas and talin dissociated from αvβ3 integrin. The αvβ3 integrin was internalized, ubiquitinylated, and gated toward lysosomes. Taken together, the experiments define Tie2/αvβ3 integrin association-induced integrin internalization and degradation as mechanistic consequences of endothelial Ang-2 stimulation. |
DOI: | doi:10.1074/jbc.M109.097543 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1074/jbc.M109.097543 |
| Volltext: https://www.sciencedirect.com/science/article/pii/S0021925820618506 |
| DOI: https://doi.org/10.1074/jbc.M109.097543 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Angiopoietin |
| Cell Adhesion |
| Cell Junctions |
| Endothelium |
| Integrin |
| Protein-tyrosine Kinase (Tyrosine Kinase) |
| Tie |
| Vascular Biology |
K10plus-PPN: | 1870346769 |
Verknüpfungen: | → Zeitschrift |
Angiopoietin-2 stimulation of endothelial cells induces αvβ3 integrin internalization and degradation / Thomas, Markus [VerfasserIn]; 2 June 2010 (Online-Ressource)