This C-terminal domain includes a predicted nucleoporin, NUP160, from Arabidopsis []. NUP160 is required for nuclear mRNA export and for disease resistance [, ]and for proper expression of factors responsible for the repression of auxin signalling [].
This entry includes the nuclear pore complex proteins Nup133, Nup132, Nup131 and Nup15 (from Caenorhabditis elegans). Nup133 is a component of the Nup160 subcomplex, which consists of Nup160, Nup133, Nup107 and Nup96, and is important for mRNA export from the nucleus []. Nup160 subcomplexes are localized to both sides of the NPC during interphase. Nup133 also localizes to kinetochores []. Nup131 and Nup132 are components of the npc107-120 complex in Schizosaccharomyces pombe. This complex consists of nup85, nup107, nup120, nup131, nup132 and seh1 and is also required for mRNA export [].
Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth []. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export []. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 subcomplex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 subcomplex, but rather that it regulates the association of the subcomplex with the NPC and other proteins [].
