YTHDC1 is an essential factor controlling satellite cell regenerative ability through multifaceted gene regulatory mechanisms in myoblast cells.

Structural studies reveal the mechanism by which the mRNA nuclear export machinery engages with nascent transcripts through interaction with the cap binding complex.

The cryo-EM structure of the human transcription-export THO–UAP56 complex reveals mechanisms of mRNA nuclear export licensing.

YTHDC1 facilitates selective clearance of N6-methyladenosine methylated mRNAs from the nucleus to the cytoplasm through binding by nuclear 'reader' proteins and incorporation into the canonical mRNA export pathway.

Ubp15 regulates the ubiquitylation of the export adaptor Mex67.

The stimulation of lipopolysaccharides induced nuclear localization of IRAK2 to facilitate nuclear export of a specific subset of inflammation-related messenger RNAs for translation in murine macrophages.

Biochemical and structural analyses of a universal mRNP remodeling pathway suggest an ATPase-powered targeted deposition of export factors onto mRNP.

Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.

In vivo and in vitro characterization demonstrates a direct interaction of Dbp5 with tRNA that requires Gle1 to spatially activate the Dbp5 ATPase cycle for tRNA export in Saccharomyces cerevisiae.