Range |
~100 nm
|
Organism |
Eukaryotes |
Reference |
Grünwald D, Singer RH, Rout M. Nuclear export dynamics of RNA-protein complexes. Nature. 2011 Jul 20 475(7356):333-41. doi: 10.1038/nature10318. p.333 left column top paragraphPubMed ID21776079
|
Primary Source |
Kubitscheck, U. et al. Nuclear transport of single molecules: dwell times at the nuclear pore complex. J. Cell Biol. 168, 233–243 (2005). & Grünwald, D. & Singer, R. In vivo imaging of labelled endogenous β-actin mRNA during nucleocytoplasmic transport. Nature 467, 604–607 (2010). doi: 10.1038/nature09438.PubMed ID15657394, 20844488
|
Comments |
P.333 left column top paragraph:"The NPC consists of several major domains (Fig. 1): the selective central channel, or central transporter region the core scaffold that supports the central channel the transmembrane regions the nuclear basket and the cytoplasmic filaments [ref 5]. The central channel is filled and surrounded with a distinct class of Nup [nucleoporin] that has numerous large domains rich in phenylalanine and glycine repeats, termed FG Nups. It is this central channel and the FG Nups that seem sufficient to mediate selective receptor-mediated transport [refs 6, 7]. The nuclear basket consists of eight filaments that reach into the nucleoplasm, attached to each other by a ring at the end. Electron microscopy tomographs have shown that filaments extend from this basket into the nucleus [refs 8, 9]. The cytoplasmic filaments are less ordered, forming highly mobile molecular rods projecting into the cytoplasm. The reach of NPCs can extend about 100 nm into the nucleus and cytoplasm [primary sources]." |
Entered by |
Uri M |
ID |
112220 |