Nucleoporin domain topology is linked to the transport status of the nuclear pore complex.

Nuclear pore complexes (NPCs) facilitate macromolecular exchange between the nucleus and cytoplasm of eukaryotic cells. The vertebrate NPC is composed of approximately 30 different proteins (nucleoporins), of which around one third contain phenylalanine-glycine (FG)-repeat domains that are thought to mediate the main interaction between the NPC and soluble transport receptors. We have recently shown that the FG-repeat domain of Nup153 is flexible within the NPC, although this nucleoporin is anchored to the nuclear side of the NPC.

Complex formation among the RNA export proteins Nup98, Rae1/Gle2, and TAP.

Most nucleocytoplasmic traffic through the nuclear pore complex is mediated by soluble receptors of the importin/exportin or karyopherin family. mRNA export is unique in that no receptor of this family has been implicated in trafficking of the bulk of mRNAs. Instead, many diverse proteins have been linked to mRNA export, but an all-encompassing model remains elusive.

A new species of fossil lorisid from the miocene of east africa.

Almost 50 years after its discovery, a cranium from the early Miocene of Rusinga Island, Kenya, is designated the type specimen for a new lorisid species in the genusMioeuoticus. This new species differs fromMioeuoticus bishopi in a number of dental attributes. Several cranial features place this species in Lorisidae, where it may represent the sister group to living lorises.