The formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations. Here, we show that Diaphanous-related formin-3 (mDia2) localizes to the cytoplasmic side of the nuclear envelope. This localization of mDia2 to the nuclear rim required the presence of a nuclear localizati...

Regulation of nuclear-cytoplasmic trafficking of oncoproteins is critical for growth homeostasis. Dysregulated trafficking contributes to malignancy, whereas understanding the process can reveal unique therapeutic opportunities. Here, we focus on eukaryotic translation initiation factor 4E (eIF4E), a prooncogenic protein highly elevated in many cancers, including acute myeloid leukemia (AML). T...

uclear import is slowed by too much of a good thing. So says a new systems model of nuclear import from Riddick and Macara (page 1027), which predicts that high levels of the cargo carrier Importin-␤ or the RanGEF RCC1 inhibit import. With its simple nucleus-versus-cytoplasm architecture, import is a good candidate for systems analysis. Most of the components have been identified, and biochemic...

Influenza A viruses recruit components of the nuclear import pathway to enter the host cell nucleus and promote viral replication. Here, we analyzed the role of the nuclear import factor importin-α7 in H1N1 influenza virus pulmonary tropism by using various ex vivo imaging techniques (magnetic resonance imaging, confocal laser scanning microscopy, and correlative light-electron microscopy). We ...

and determines the directionality of nucleocytoplasmic transport by controlling the stability of complexes formed between cargo proteins carrying specific tar-leases proteins required for mitotic spindle assembly from inhibitory complexes with importin-␤ [5–7]. Peking University Beijing 100871 Ran also functions in the assembly of the nuclear envelope (NE) at the end of mitosis when the compart...

Classic nuclear shuttling is mediated by an importin-α∙β heterodimer that binds to cargoes containing a nuclear localization signal, and shuttles most nuclear proteins immediately after their translation. Aside from this canonical mechanism, kariopheryn-βs or β-like importins operate by binding to non-canonical nuclear localization signals to mediate translocation without the assistance of impo...

The Ran GTPase plays a key role in nucleocytoplasmic transport. In its GTP-bound form, it directly interacts with members of the importin beta family of nuclear transport receptors and modulates their association with cargo. Work in cell-free higher-eukaryote systems has demonstrated additional roles for Ran in spindle and nuclear envelope formation during mitosis. However, until recently, no R...

STAT transcription factors are tyrosine phosphorylated upon cytokine stimulation and enter the nucleus to activate target genes. We show that Rac1 and a GTPase-activating protein, MgcRacGAP, bind directly to p-STAT5A and are required to promote its nuclear translocation. Using permeabilized cells, we find that nuclear translocation of purified p-STAT5A is dependent on the addition of GTP-bound ...