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. Author manuscript; available in PMC: 2020 Nov 1.
Published in final edited form as: Traffic. 2019 Sep 12;20(11):829–840. doi: 10.1111/tra.12691

Figure 1.

Figure 1.

Nuclear mRNA export is mediated by the principal export receptor yeast Mex67•Mtr2/ human NXF1•NXT1. (A) Domain schematic of yeast Mex67•Mtr2. (B) Structure of the NXF1-UBA domain bound to a FXFG peptide (PDB ID 1OAI). (C) Structure of the NXF1-NTF2L domain bound to a FG peptide (PDB ID 1JN5). (D) Structure of yeast Mex67 (RRM, LRR, and NTF2L domains) associated with Mtr2 (PDB ID 4WWU). (E) Structure of NXF1 (LRR and NTF2L domains) associated with NXT1 (PDB ID 4WYK). (F) A working model of Mex67•Mtr2 mediated mRNA export. Export is driven by specific alterations of the mRNP protein composition. In the nucleus, Sub2 facilitates the assembly of export-competent mRNPs by recruiting the principal mRNA export receptor Mex67•Mtr2. At the cytoplasmic side of the NPC, Dbp5 mediates disassembly of the export complex by displacing proteins including Mex67•Mtr2 and the poly(A) RNA binding protein Nab2 from the mRNP.