{"entity": "researcher", "timestamp": "2026-08-20T20:43:06.257Z", "family": "Barbera", "given": "Stefano", "initials": "S", "orcid": "0000-0001-9544-455X", "affiliations": ["Department of Immunology, Genetics and Pathology, Science for Life Laboratory, Uppsala University, Uppsala, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/666ca561c7494caa90336bddf52b4f09.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/666ca561c7494caa90336bddf52b4f09"}}, "publications": [{"entity": "publication", "iuid": "1cbd88174bb94040ad897cc3f47cc7cb", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1cbd88174bb94040ad897cc3f47cc7cb.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1cbd88174bb94040ad897cc3f47cc7cb"}}, "title": "Trogocytosis of chimeric antigen receptors between T cells is regulated by their transmembrane domains.", "authors": [{"family": "Barbera", "given": "Stefano", "initials": "S", "orcid": "0000-0001-9544-455X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/666ca561c7494caa90336bddf52b4f09.json"}}, {"family": "Schuiling", "given": "Matthijs J A", "initials": "MJA", "orcid": "0009-0005-2049-3601", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/127743eb9ad34ee5915cca1fd3958fef.json"}}, {"family": "Sanjaya", "given": "Nathaniel A", "initials": "NA", "orcid": "0009-0001-8912-9921", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7a0c2cf45419465b9d2d1c5e3677839b.json"}}, {"family": "Pietil\u00e4", "given": "Ilkka", "initials": "I", "orcid": "0000-0001-7398-5769", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b6056d3fa76c41c6943f50faba0d8cd7.json"}}, {"family": "Sar\u00e9n", "given": "Tina", "initials": "T", "orcid": "0000-0001-5227-6779", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ed75a6dcbb9940e49481280af6183d69.json"}}, {"family": "Essand", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9725-0422", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a2e56cdd77634c01ab6d98dea8c60430.json"}}, {"family": "Dimberg", "given": "Anna", "initials": "A", "orcid": "0000-0003-4422-9125", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6f5d91c4b8784d8081a41604bb3d78d4.json"}}], "type": "journal article", "published": "2025-01-31", "journal": {"title": "Sci Immunol", "issn": "2470-9468", "volume": "10", "issue": "103", "pages": "eado2054", "issn-l": "2470-9468"}, "abstract": "Trogocytosis is an exchange of membrane-associated molecules between cells that can either halt or boost immune responses. However, the mechanism that regulates trogocytosis in T cells and its consequences are not yet clear. Here, we demonstrate that T cells can exchange chimeric antigen receptors (CARs) by trogocytosis, thereby arming recipient T cells with the capacity to respond to tumor antigens by up-regulating proteins associated with a cytotoxic response and killing of target cells. We demonstrate that although trogocytosis is dependent on cell-cell contact, the exchange of a specific cell membrane protein does not require a cognate binding partner on the surface of recipient cells. Instead, the probability that a protein is exchanged by trogocytosis is determined by its transmembrane domain. This finding opens new avenues for modulating this process in CAR-T cells.", "doi": "10.1126/sciimmunol.ado2054", "pmid": "39888980", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:59:43.101Z", "modified": "2026-08-20T11:59:43.364Z"}, {"entity": "publication", "iuid": "1ee1e79d053b4d2eaf4936bcbeb03436", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1ee1e79d053b4d2eaf4936bcbeb03436.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1ee1e79d053b4d2eaf4936bcbeb03436"}}, "title": "CD93 Signaling via Rho Proteins Drives Cytoskeletal Remodeling in Spreading Endothelial Cells.", "authors": [{"family": "Barbera", "given": "Stefano", "initials": "S", "orcid": "0000-0001-9544-455X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/666ca561c7494caa90336bddf52b4f09.json"}}, {"family": "Raucci", "given": "Luisa", "initials": "L"}, {"family": "Lugano", "given": "Roberta", "initials": "R"}, {"family": "Tosi", "given": "Gian Marco", "initials": "GM"}, {"family": "Dimberg", "given": "Anna", "initials": "A"}, {"family": "Santucci", "given": "Annalisa", "initials": "A", "orcid": "0000-0001-6976-9086", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7201262f0072492285079f8855d443c0.json"}}, {"family": "Galvagni", "given": "Federico", "initials": "F", "orcid": "0000-0003-1967-9554", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/615bf67e0d0749b0a6672e5006a131d2.json"}}, {"family": "Orlandini", "given": "Maurizio", "initials": "M", "orcid": "0000-0002-6112-4889", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f48bca1c017e4f8f878b38766e8c1c32.json"}}], "type": "journal article", "published": "2021-11-17", "journal": {"title": "Int J Mol Sci", "issn": "1422-0067", "volume": "22", "issue": "22", "issn-l": null}, "abstract": "During angiogenesis, cell adhesion molecules expressed on the endothelial cell surface promote the growth and survival of newly forming vessels. Hence, elucidation of the signaling pathways activated by cell-to-matrix adhesion may assist in the discovery of new targets to be used in antiangiogenic therapy. In proliferating endothelial cells, the single-pass transmembrane glycoprotein CD93 has recently emerged as an important endothelial cell adhesion molecule regulating vascular maturation. In this study, we unveil a signaling pathway triggered by CD93 that regulates actin cytoskeletal dynamics responsible of endothelial cell adhesion. We show that the Src-dependent phosphorylation of CD93 and the adaptor protein Cbl leads to the recruitment of Crk, which works as a downstream integrator in the CD93-mediated signaling. Moreover, confocal microscopy analysis of FRET-based biosensors shows that CD93 drives the coordinated activation of Rac1 and RhoA at the cell edge of spreading cells, thus promoting the establishment of cell polarity and adhesion required for cell motility.", "doi": "10.3390/ijms222212417", "pmid": "34830297", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC8622518"}, {"db": "pii", "key": "ijms222212417"}], "notes": [], "created": "2026-08-20T13:41:30.374Z", "modified": "2026-08-20T13:41:30.599Z"}]}