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SERPINE1 mRNA-binding protein 1 (SERBP1) is an RNA-binding protein characterized by two RG/RGG repeat regions but lacking canonical RNA-binding motifs such as RRM, KH, or zinc finger domains. It is intrinsically disordered, localized to both cytoplasm and nucleus, and interacts with ribosomes to promote ribosome hibernation—a process preserving inactive ribosomes from degradation. SERBP1 binds preferentially to GC-rich RNA motifs, including G-quadruplex structures, and regulates the stability and decay of specific mRNAs, most notably SERPINE1/PAI-1 mRNA, which plays key roles in vascular biology and cancer. The protein modulates splicing, chromosome structure, and participates in assembly of stress granule and epigenetic regulatory complexes. Elevated expression of SERBP1 correlates with poor prognosis in multiple cancers such as glioblastoma, liver, prostate, and ovarian cancer, suggesting a role in tumorigenesis. While often considered a candidate therapeutic target, no drugs are currently known to selectively modulate SERBP1 function. Its biological effects span translation inhibition, phase separation, and subcellular localization changes depending on cellular stress and methylation status.
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