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&lt;strong&gt;BACKGROUND&lt;/strong&gt; The oncogene PIM1, encoding a constitutively active serine/threonine protein kinase, is involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. There is a growing body of literature on the role of PIM1-mediated cellular senescence, but the precise mechanism remains unclear. &lt;strong&gt;MATERIAL AND METHODS&lt;/strong&gt; Silver staining and LC-MS/MS analysis were performed to investigate the protein interacting with PIM1. Immunofluorescence, Co-IP, and Western blot assay were used to assess the interaction of PIM1 and SND1. EdU incorporation and CCK8 assay were used to detect cell proliferation and immunohistochemistry was used to detect the level of the indicated protein. &lt;strong&gt;RESULTS&lt;/strong&gt; We found that PIM1 can bind directly and phosphorylate SND1. In addition, decreased expression of SND1 leads to the upregulation of SASP. SND1 is involved in cellular senescence induced by PIM1. &lt;strong&gt;CONCLUSIONS&lt;/strong&gt; We investigated the role of PIM1 in oncogene-induced normal cellular senescence. Our results promote further understanding of the mechanisms underlying OIS and suggest potential applications for preventing tumorigenesis.

The Oncogene PIM1 Contributes to Cellular Senescence by Phosphorylating Staphylococcal Nuclease Domain-Containing Protein 1 (SND1)