The nuclear pore complex (NPC) facilitates nucleocytoplasmic transport, a 
crucial process for various cellular activities. The NPC comprises ~30 
nucleoporins and is well characterized in vertebrates and yeast. However, only 
eight plant nucleoporins have been identified, and little information is 
available about the complete molecular structure of plant NPCs. In this study, 
an interactive proteomic approach was used to identify Arabidopsis thaliana 
nucleoporins. A series of five cycles of interactive proteomic analysis was 
performed using green fluorescent protein (GFP)-tagged nucleoporins. The 
identified nucleoporins were then cloned and subcellular localization analyses 
were performed. We found that the plant NPC contains at least 30 nucleoporins, 
22 of which had not been previously annotated. Surprisingly, plant nucleoporins 
shared a similar domain organization to their vertebrate (human) and yeast 
(Saccharomyces cerevisiae) counterparts. Moreover, the plant nucleoporins 
exhibited higher sequence homology to vertebrate nucleoporins than to yeast 
nucleoporins. Plant NPCs lacked seven components (NUCLEOPORIN358 [Nup358], 
Nup188, Nup153, Nup45, Nup37, NUCLEAR DIVISION CYCLE1, and PORE MEMBRANE PROTEIN 
OF 121 kD) that were present in vertebrate NPCs. However, plants possessed a 
nucleoporin, Nup136/Nup1, that contained Phe-Gly repeats, and sequence analysis 
failed to identify a vertebrate homolog for this protein. Interestingly, 
Nup136-GFP showed greater mobility on the nuclear envelope than did other 
nucleoporins, and a Nup136/Nup1 deficiency caused various defects in plant 
development. These findings provide valuable new information about plant NPC 
structure and function.