Interaction of HIV capsids with the cellular protein cleavage-and-polyadenylation factor 6 at the inner side of nuclear pores promotes nuclear entry of the viral replication complex in primary human macrophages.
Structural, biochemical, and proteomic analyses of a four-subunit core module of the cleavage and polyadenylation specificity factor complex reveal its molecular architecture and specific determinants of polyadenylation signal recognition in human mRNAs.
A robust method to quantitatively visualize HIV-1 replication complexes in infected cells shows that these complexes remain associated with the viral capsid beyond nuclear import in primary macrophages.
Conformational flexibility in HIV-1 capsid, provided by cyclophilin A binding, facilitates evasion of capsid-targeting restriction factor MxB, while allowing sequence change to facilitate cytotoxic T-cell evasion.
Transport-based high-throughput identification of cargo proteins specific to all 12 human importin-β family nuclear import receptors revealed biological processes that the cargo cohorts of each receptor are involved in.
CPEB4's switch from translational repressor to activator is regulated during cell cycle by hyperphosphorylation of its intrinsically disordered domain, which controls its phase-separation into RNA-containing liquid-like droplets.
Crosslink immunopreciptiation (iCLIP) studies reveal important mechanistic insights into how MARF1 post-transcriptionally regulates targeted mRNAs and uncover a novel mode by which EDC4 regulates mRNA metabolism.