20.500.12556/DiRROS-30318 Phosphorylation of YBX1 in the kidneys is altered in legumain knockout-mice Protein phosphorylation is a common post-translational modification that plays a crucial role in cellular signal transduction. Disruptions in this process can lead to phenotypic deviations in healthy organisms. Legumain is a cysteine proteinase present in plants and animals. Legumain is involved in the regulation of kidney and hematopoietic homeostasis, as well as immune response. Its dysregulation is associated with various types of cancers and neurodegenerative diseases. Legumain knockout mice generally exhibit a normal phenotype, except for altered kidney function, hemophagocytic syndrome, and extramedullary hematopoiesis. In this study, we analyzed the changes in protein phosphorylation in legumain knockout mice compared to their wild-type counterparts to elucidate how legumain deficiency affects protein phosphorylation and related cell signaling. Phosphopeptides from the kidney and liver samples were enriched and analyzed using mass spectrometry and validated with Western blot and immunohistochemistry. Several phosphorylation sites on the RNA- and DNA-binding protein Y-box binding protein 1 were identified. A site on the serine 100 residue was found to activate the NF-κB pathway in legumain knockout mice, resulting in an enhanced inflammatory response. This was supported by the increased expression of several NF-κB genes. Overall, this study provides valuable insights into the role of legumain and its impact on various cellular processes. legumain knockout mice cellular signal transduction legumain true false true American Chemical Society ZDA Angleški jezik Slovenski jezik © 2026 The Authors. Neznano 2026-06-19 12:48:53 2026-06-19 12:48:53 2026-06-20 03:51:45 0000-00-00 00:00:00 2026 0 0 Nasl. z nasl. zaslona; Soavtorji: Tea Sinožić, Matej Kolarič, Boris Turk, Marko Fonović; Opis vira z dne 16. 5. 2026; str. 3078-3091 iss. 6 Vol. 25 Jun. 2026 0000-00-00 Zaloznikova Objavljeno NiDoloceno 2026-02-02 2026-04-28 2026-05-06 577 1535-3907 10.1021/acs.jproteome.6c00105 281767683 https://pubs.acs.org/doi/10.1021/acs.jproteome.6c00105?ref=pdf 1 b3a3933a-6bbb-11f1-be3d-001a4af901a5 https://dirros.openscience.si/Dokument.php?lang=slv&id=45976 RAZ_Sever_Tilen_2026.pdf RAZ_Sever_Tilen_2026.pdf 1 18AEC32870B7EF3AAB2030855800BF3F 7b6ed15aaf7194b0fa0ef2c3e4d3e270ec54eb63d0e010a79852bbaa81ec78a7 1d32509b-6bbc-11f1-be3d-001a4af901a5 https://dirros.openscience.si/Dokument.php?lang=slv&id=45977 Institut Jožef Stefan 0 0 0