Proximity-dependent proteomics identifies PARD3 scaffold protein as a novel effector in EPH receptor signaling

ABSTRACT: This submission contains the mass spectrometry files for the manuscript by Sara L. Banerjee et al. that describes identification of new downstream effector proteins for EPH receptors (EPHRs). To unravel EPHR-associated signaling complexes under native conditions, we applied a mass spectrometry (MS)-based proximity labeling approach, namely BioID. We obtained a composite signaling network from EPHA4, -B2, -B3 and -B4 receptors. This network comprises 395 proteins, most of which not previously linked to EPH signaling. We examined the requirement of some of BioID-identified candidates for EPHR-regulated functions and showed that depletion of the signaling scaffold PARD3, blocks EPH-dependent cell sorting. Using affinity purification combined to MS, we further delineated a signaling complex involving C-SRC kinase (CSK), whose recruitment to PARD3 complexes is dependent on EPHR signals. The BioID and AP-MS experiments were performed from HEK293 and HEK293T cells, respectively and 30 MS files were acquired on an Orbitrap Fusion mass spectrometer in data dependent acquisition mode. All the DDA files are associated with this deposition. Please refer to the Table 1 for additional details of submitted files. For questions, please contact Jean-Philippe Lambert ([e-mail]) or Nicolas Bisson ([e-mail]).

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Jean-Philippe Lambert  

PROVIDER: MSV000086054 | MassIVE |

SECONDARY ACCESSION(S): PXD021257

REPOSITORIES: MassIVE