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Required for efficient export of polyadenylated RNA. Plays a key structural role in the oligomerization of the THO-DDX39B complex. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6I9Y2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12951069"}],"value":"Tetramer; as part of a THO-DDX39B complex. Component of the THO subcomplex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7. Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; in the complex interacts with THOC1, THOC2 and THOC5; forms a coiled-coil dimer with THOC5; together with THOC5 and THOC6, plays a key structural role in the oligomerization of the THO-DDX39B complex. TREX seems to have a dynamic structure involving ATP-dependent remodeling. 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