{"entity": "researcher", "timestamp": "2026-10-01T12:33:21.726Z", "family": "Olsson", "given": "Magnus", "initials": "M", "orcid": "0000-0002-6370-8423", "affiliations": ["Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/93f6641a8bcb4d3380c0f3ba3fef7cbf.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/93f6641a8bcb4d3380c0f3ba3fef7cbf"}}, "publications": [{"entity": "publication", "iuid": "6cfde89d60d944d3a17302c7e855897a", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/6cfde89d60d944d3a17302c7e855897a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/6cfde89d60d944d3a17302c7e855897a"}}, "title": "A caspase-2-RFXANK interaction and its implication for MHC class II expression.", "authors": [{"family": "Forsberg", "given": "Jeremy", "initials": "J"}, {"family": "Li", "given": "Xinge", "initials": "X"}, {"family": "Akpinar", "given": "Birce", "initials": "B"}, {"family": "Salvatori", "given": "Roger", "initials": "R"}, {"family": "Ott", "given": "Martin", "initials": "M"}, {"family": "Zhivotovsky", "given": "Boris", "initials": "B"}, {"family": "Olsson", "given": "Magnus", "initials": "M", "orcid": "0000-0002-6370-8423", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/93f6641a8bcb4d3380c0f3ba3fef7cbf.json"}}], "type": "journal article", "published": "2018-01-23", "journal": {"title": "Cell Death Dis", "issn": "2041-4889", "volume": "9", "issue": "2", "pages": "80", "issn-l": "2041-4889"}, "abstract": "Despite recent achievements implicating caspase-2 in tumor suppression, the enzyme stands out from the apoptotic caspase family as a factor whose function requires further clarification. To specify enzyme characteristics through the definition of interacting proteins in apoptotic or non-apoptotic settings, a yeast 2-hybrid (Y2H) screen was performed using the full-length protein as bait. The current report describes the analysis of a captured prey and putative novel caspase-2 interacting factor, the regulatory factor X-associated ankyrin-containing protein (RFXANK), previously associated with CIITA, the transactivator regulating cell-type specificity and inducibility of MHC class II gene expression. The interaction between caspase-2 and RFXANK was verified by co-immunoprecipitations using both exogenous and endogenous proteins, where the latter approach suggested that binding of the components occurs in the cytoplasm. Cellular co-localization was confirmed by transfection of fluorescently conjugated proteins. Enhanced caspase-2 processing in RFXANK-overexpressing HEK293T cells treated with chemotherapeutic agents further supported Y2H data. Yet, no distinct differences with respect to MHC class II expression were observed in plasma membranes of antigen-presenting cells derived from wild type and caspase-2-/- mice. In contrast, increased levels of the total MHC class II protein was evident in protein lysates from caspase-2 RNAi-silenced leukemia cell lines and B-cells isolated from gene-targeted mice. Together, these data identify a novel caspase-2-interacting factor, RFXANK, and indicate a potential non-apoptotic role for the enzyme in the control of MHC class II gene regulation.", "doi": "10.1038/s41419-017-0144-y", "pmid": "29362422", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC5833739"}, {"db": "pii", "key": "10.1038/s41419-017-0144-y"}], "notes": [], "created": "2018-12-05T12:22:54.137Z", "modified": "2026-09-23T12:19:39.274Z"}]}