PABPC4

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.

PABPC4 has been shown to interact with PHLDA1.{{cite journal | vauthors = Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D | title = Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product | journal = Cell. Signal. | volume = 13 | issue = 5 | pages = 345–52 | date = May 2001 | pmid = 11369516 | doi = 10.1016/S0898-6568(01)00141-3 }}

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{{RNA-binding proteins}}

Category:Genes mutated in mice