Members of this family belong to the nucleor pore complex, NPC, the only gateway between the nucleus and the cytoplasm. The NPC consists of several subcomplexes each one of which is made up of multiple copies of several individual Nup, Nic or Sec protein subunits. In yeast, this Nup or nucleoporin subunit is numbered Nup53, Nup40 in Schizo. pombe and in vertebrates as Nup35. This subunit forms part of the inner ring within the membrane and interacts directly with Nup-Ndc1, considered to be an anchor for the NPC in the pore membrane [1]. This region of the Nup is the RNA-recognition region [2].
The nuclear pore complex (NPC) mediates the transport of macromolecules across the nuclear envelope (NE). The NPC is composed of a relatively small number of proteins (~30), termed nucleoporins or Nups. The vertebrate nuclear pore protein Nup35, the ortholog of Saccharomyces cerevisiae Nup53p, is suggested to interact with the NE membrane and to be required for nuclear morphology. The highly conserved region between vertebrate Nup35 and yeast Nup53p is predicted to contain an RNA-recognition motif (RRM) domain.
Brohawn SG, Partridge JR, Whittle JR, Schwartz TU;, Structure. 2009;17:1156-1168.: The nuclear pore complex has entered the atomic age. PUBMED:19748337 EPMC:19748337 .
Handa N, Kukimoto-Niino M, Akasaka R, Kishishita S, Murayama K, Terada T, Inoue M, Kigawa T, Kose S, Imamoto N, Tanaka A, Hayashizaki Y, Shirouzu M, Yokoyama S;, J Mol Biol. 2006;363:114-124.: The crystal structure of mouse Nup35 reveals atypical RNP motifs and novel homodimerization of the RRM domain. PUBMED:16962612 EPMC:16962612.
