SERBP1 is a multifunctional RNA-binding protein that serves as a ribosome-binding factor promoting ribosome hibernation, a process stabilizing ribosomes in an inactive state and protecting them from proteasomal degradation. It accomplishes this through association with the translation elongation factor EEF2, sequestering it at the ribosomal A-site. Beyond ribosomal regulation, SERBP1 binds the 3′-untranslated region of SERPINE1 mRNA and modulates its stability in response to cyclic nucleotides. SERBP1 also participates in PML-nuclear body formation and interacts with PARP1 in PARylation-dependent protein complexes regulating splicing and cell division 1. The protein functions across diverse biological contexts: it regulates CtIP translation during homologous recombination-mediated DNA repair in S phase 2, is required for dengue virus replication through ribosome-linked recruitment 3, and negatively regulates the ribotoxic stress kinase ZAK at collided ribosomes 4. Clinically, SERBP1 dysregulation is implicated in multiple malignancies. In breast cancer, elevated SERBP1 stabilizes MAD2L1 mRNA under high-glucose conditions, promoting tumorigenicity 5. In T-cell acute lymphoblastic leukemia, SERBP1 drives progression through the MYC signaling axis 6. In glioblastoma, HERC5-mediated stabilization of SERBP1 enhances stemness and chemoresistance 7. Conversely, SERBP1 overexpression in cervical cancer cells induces apoptosis by downregulating proliferation genes 8. SERBP1 also participates in reproductive system function, with dysregulation affecting endometrial decidualization 9. These findings position SERBP1 as a therapeutic target in cancer and metabolic diseases.