In eukaryotic cells, many RNA species are exported from the nucleus to the cytoplasms. Different RNA species form distinct ribonucleoprotein (RNP) complexes for export, indicating specific RNA recognition by export proteins. Specific RNA recognition is usually achieved by specific RNA sequences or structures, but we have recently reported a molecular mechanism by which the formation of export RNP complexes is specified by RNA length. ( 1) RNA polymerase II (Pol II) synthesizes not only mRNAs but also shorter RNAs, including spliceosomal U snRNAs. Although the key U snRNA export factor, PHAX, can bind to mRNA in vitro, PHAX is excluded from mRNA in vivo. The heterotetramer of the heterogeneous nuclear RNP (hnRNP) C1/C2 specifically binds Pol II transcripts longer than 200-300 nt, and funnels them into the mRNA export pathway by inhibiting their binding by PHAX, whereas shorter transcripts not bound by the heterotetramer are committed to the U snRNA export pathway. Although this finding reveals a novel function of the C1/C2 heterotetramer and highlights the biological importance of RNA recognition by length, it has raised a number of new questions, some of which will be discussed in this article, together with some historical background of this finding.
Keywords: Aly; PHAX; RNA polymerase II; U snRNA; cap-binding complex (CBC); hnRNP; mRNA; nuclear export.