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Murachelli, A.G., Ebert, J., Basquin, C., Le Hir, H., Conti, E. (2012). The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex.  Nat. Struct. Mol. Biol. 19(4): 378--386.
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The ASAP complex interacts with the exon-junction complex (EJC), a messenger ribonucleoprotein complex involved in post-transcriptional regulation. The three ASAP subunits (Acinus, RNPS1 and SAP18) have been individually implicated in transcriptional regulation, pre-mRNA splicing and mRNA quality control. To shed light on the basis for and consequences of ASAP's interaction with the EJC, we have determined the 1.9-Å resolution structure of a eukaryotic ASAP core complex. The RNA-recognition motif of RNPS1 binds to a conserved motif of Acinus with a recognition mode similar to that observed in splicing U2AF proteins. The Acinus-RNPS1 platform recruits the ubiquitin-like domain of SAP18, forming a ternary complex that has both RNA- and protein-binding properties. Unexpectedly, our structural analysis identified an Acinus-like motif in Pinin, another EJC-associated splicing factor. We show that Pinin physically interacts with RNPS1 and SAP18, forming an alternative ternary complex, PSAP.

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    Publication Type
    Nat. Struct. Mol. Biol.
    Nature Structural and Molecular Biology
    Publication Year
    1545-9993 1545-9985
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