Ribonucleic acid export 1–Nucleoporin 98 complex (Rae1–Nup98)

The Ribonucleic acid export 1–Nucleoporin 98 (Rae1–Nup98) complex is a conserved heterodimeric assembly essential for the nuclear export of mature messenger RNA (mRNA) through the nuclear pore complex (NPC) (UniProt O43237, P52948). Rae1, also known as Mrnp41, binds to the Gle2p-binding sequence (GLEBS) motif of Nup98 to facilitate the translocation of ribonucleoprotein particles across the nuclear envelope (PubMed: 11053435). Beyond transport, the complex plays a role in mitotic spindle assembly and preventing aneuploidy by regulating the Anaphase-Promoting Complex (APC) (PubMed: 14527411). This complex is a major target for various viruses; for instance, the SARS-CoV-2 non-structural protein 1 (Nsp1) binds to the Rae1–Nup98 complex to block the mRNA exit tunnel, effectively halting host cell protein synthesis and suppressing the interferon-mediated immune response (Science, 2020). Similarly, the Matrix (M) protein of the Vesicular Stomatitis Virus (VSV) targets this complex to inhibit host gene expression (PubMed: 15831455). While no drugs are currently approved to target this complex directly, it is a significant subject of research for antiviral strategies aimed at restoring host translation during infection.

Other names

RAE1-NUP98 complexmRNA export factor Rae1-Nup98Gle2p-binding sequence (GLEBS) complexMrnp41-Nup98 complex

Viral proteins (e.g., SARS-CoV-2 Nsp1) bind to the Rae1–Nup98 complex to sterically block the mRNA exit tunnel of the nuclear pore, thereby inhibiting the export of host mRNAs and suppressing the host's innate immune response.