| Autor: |
Sara L. Banerjee, Frédéric Lessard, François J.M. Chartier, Kévin Jacquet, Ana I. Osornio-Hernandez, Valentine Teyssier, Karim Ghani, Noémie Lavoie, Josée N. Lavoie, Manuel Caruso, Patrick Laprise, Sabine Elowe, Jean-Philippe Lambert, Nicolas Bisson |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Cell Reports, Vol 40, Iss 1, Pp 111031- (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2211-1247 |
| DOI: |
10.1016/j.celrep.2022.111031 |
| Popis: |
Summary: EPH receptors (EPHRs) constitute the largest family among receptor tyrosine kinases in humans. They are mainly involved in short-range cell-cell communication events that regulate cell adhesion, migration, and boundary formation. However, the molecular mechanisms by which EPHRs control these processes are less understood. To address this, we unravel EPHR-associated complexes under native conditions using mass-spectrometry-based BioID proximity labeling. We obtain a composite proximity network from EPHA4, -B2, -B3, and -B4 that comprises 395 proteins, most of which were not previously linked to EPHRs. We examine the contribution of several BioID-identified candidates via loss-of-function in an EPHR-dependent cell-segregation assay. We find that the signaling scaffold PAR-3 is required for cell sorting and that EPHRs directly phosphorylate PAR-3. We also delineate a signaling complex involving the C-terminal SRC kinase (CSK), whose recruitment to PAR-3 is dependent on EPHR signals. Our work describes signaling networks by which EPHRs regulate cellular phenotypes. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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