Polyadenylate-binding protein 1 (PABPC1)

Polyadenylate-binding protein 1 (PABPC1) is an RNA-binding protein that binds specifically to the poly(A) tail at the 3' end of eukaryotic messenger RNAs. It plays a central role in regulating various aspects of mRNA metabolism, including stability, transport between nucleus and cytoplasm, translation efficiency, and degradation. PABPC1 contains four RNA recognition motifs (RRMs) that mediate its binding to polyadenylated RNA sequences with high specificity. In addition to its interaction with RNA, it has a C-terminal MLLE/PABC domain that mediates interactions with regulatory proteins such as eukaryotic release factor 3 (eRF3), PAIP1, PAIP2, and others involved in translational control. While essential for normal cell function and implicated in processes like stress granule formation or viral infection response, PABPC1 itself is not considered a classical therapeutic target such as an enzyme or receptor. The submitted name "Ribonucleoprotein complex containing polyadenylate binding protein‑1" is overly broad; the canonical molecular entity relevant for structured data is "Polyadenylate-binding protein 1" (PABPC1).

Other names

Poly(A)-binding protein cytoplasmic 1PABP1Cytosolic poly(A)-binding protein 1