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J Cell Biol 2010 Jun 28;1897:1129-42. doi: 10.1083/jcb.200912045.
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The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex.

Theerthagiri G , Eisenhardt N , Schwarz H , Antonin W .

All transport across the nuclear envelope (NE) is mediated by nuclear pore complexes (NPCs). Despite their enormous size, approximately 60 MD in vertebrates, they are comprised of only approximately 30 distinct proteins (nucleoporins or Nups), many of which form subcomplexes that act as building blocks for NPC assembly. One of these evolutionarily conserved subcomplexes, the Nup93 complex, is a major structural component linking the NPC to the membranes of the NE. Using in vitro nuclear assembly assays, we show that two components of the Nup93 complex, Nup188 and Nup205, are dispensable for NPC formation. However, nuclei lacking Nup188 increase in size by several fold compared with wild type. We demonstrate that this phenotype is caused by an accelerated translocation of integral membrane proteins through NPCs, suggesting that Nup188 confines the passage of membrane proteins and is thus crucial for the homeostasis of the different nuclear membranes.

PubMed ID: 20566687
PMC ID: PMC2894445
Article link: J Cell Biol

Species referenced: Xenopus
Genes referenced: fubp1 lmnb1 lmnb2 nup155 nup188 nup205 nup35 nup62 nup93 nup98 rcc1 sqstm1
Antibodies: Lmnb1 Ab1 Lmnb2 Ab1 Lmnb2 Ab4

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References [+] :
Alber, Determining the architectures of macromolecular assemblies. 2007, Pubmed