Polyadenylate-binding protein 4 is a protein that in humans is encoded by the PABPC4gene.
Poly(A)-binding proteins (PABPs) bind to the poly(A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules.
Houng AK, Maggini L, Clement CY, Reed GL (1997). "Identification and structure of activated-platelet protein-1, a protein with RNA-binding domain motifs that is expressed by activated platelets". Eur. J. Biochem.243 (1–2): 209–18. doi:10.1111/j.1432-1033.1997.0209a.x. PMID9030741.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Hoshino S, Imai M, Kobayashi T, et al. (1999). "The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein". J. Biol. Chem.274 (24): 16677–80. doi:10.1074/jbc.274.24.16677. PMID10358005.
Goehler H, Lalowski M, Stelzl U, et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID15383276.