A homopolymer-sphere model is shown to accurately reproduce the interactions that underpin selective gating of macromolecular transport into and out of the cell nucleus.
Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.
Comprehensive investigation reveals the variability and importance of the nuclear pore complex in HIV-1 infection and the activity of the antiretroviral protein, MX2.
How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.
Nup98-HoxA9 is recruited to Hox gene cluster regions together with the chromosomally pre-bound nuclear export factor Crm1, which induces aberrant expression of several Hox genes and affecting the differentiation of embryonic stem cells.
The Ran GTPase plays a role in defining the physical properties of the nuclear pore complex transport channel by remodeling the binding interactions of importin-β with the nucleoporin Nup153 at the nuclear face of the pore.
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.
The SAGA complex binds non-chromosomal DNA circles and prevents their spreading by attaching them to nuclear pores, thereby leading to the concomitant accumulation of DNA circles and pores in ageing yeast mother cells.
