High impact information on NUP84

• Thus, the Nup84p complex in conjunction with Sec13-type proteins is required for correct nuclear pore biogenesis [1].
• Disruption of any of the genes encoding Nup84p, Nup85p, or Nup120p caused defects in nuclear membrane and nuclear pore complex organization, as well as in poly(A)+ RNA transport [1].
• Taken together, our data document that the Nup84p-Nup133p complex self-assembles in a modular concept from distinct smaller nucleoporin construction sets [2].
• Thus, Spo7p and Nem1p, which exhibit a strong genetic link to nucleoporins of the Nup84p complex, fulfil an essential role in formation of a spherical nucleus and meiotic division [3].
• Two membrane proteins were identified through their genetic interaction with the nucleoporin Nup84p and shown to participate in nuclear envelope morphogenesis in yeast [3].

Biological context of NUP84

• These chromosomal translocations fuse a homeobox DNA-binding domain to the human homolog (hNup98) of a transcriptionally active component of the yeast Nup84 subcomplex [4].
• Using a genetic screen, we have identified a previously uncharacterized Saccharomyces cerevisiae open reading frame (renamed PML39) that displays a specific interaction with nucleoporins of the Nup84 complex [5].

Physical interactions of NUP84

• Moreover, we show that Nup157 and Nup145N bind to the heptameric Nup84 complex [6].
• Unexpectedly, the same Nups also captured the hexameric Nup84p complex and Nup2p [7].

Other interactions of NUP84

• Reconstitution of Nup157 and Nup145N into the Nup84 complex [6].
• Nucleoporins required for mRNA export in Saccharomyces cerevisiae are found in the Nup84p and Nup82p subcomplexes of the NPC [8].

Analytical, diagnostic and therapeutic context of NUP84

• A highly purified Nup84p complex was isolated from yeast under native conditions and its molecular mass was determined to be 375 kD by quantitative scanning transmission electron microscopy and analytical ultracentrifugation, consistent with a monomeric complex [9].
• During the sequential reconstitution of the Nup84p complex, smaller assembly intermediates can be isolated, which exhibit modular structures determined by electron microscopy that finally make up the whole Y-shaped Nup84p complex [2].

References