High impact information on NUP82

• Mutations in the genes encoding the nucleoporin Nup82 and in the NES exporter Xpo1/Crm1 also caused the nucleoplasmic accumulation of 5' ITS1 [1].
• Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex [2].
• NUP82 encodes a protein that functions within the nuclear pore complex subsequent to docking [3].
• A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p [4].
• Yeast cells depleted of Nup82p stop cell growth and concomitantly show a defect in poly(A)+RNA export, but no major alterations of nuclear envelope structure and nuclear pore density are seen by EM [4].

Biological context of NUP82

• They do, however, accumulate poly(A)+ RNA in their nuclei at 37 degrees C. We propose that NUP82 acts as a linker to tether nucleoporins directly involved in nuclear transport to pore scaffolding via its coiled-coil domain [5].

Physical interactions of NUP82

• This suggests that Nup82p may act as a docking site for a core complex composed of the repeat-containing nucleoporins Nup159p and Nsp1p [6].
• Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p [7].

Other interactions of NUP82

• The Nup82 protein can be divided into at least two different domains both required for the essential function, but it is only the carboxy-terminal domain, exhibiting heptad repeats, which binds to Nsp1p [4].
• Together our data suggest that the poly(A)+ RNA export defect previously observed in nup82 mutant cells might be due to the loss from the NPCs of the repeat-containing nucleoporin Nup159p [6].
• Using a synthetic lethal screen with the nucleoporin NUP1, we have identified a conditional allele of NUP82, encoding an essential nuclear pore complex protein in Saccharomyces cerevisiae [8].
• Finally, synthetic lethal interactions were found between mutant alleles of NUP116 and all members of the Nup82p complex [9].
• We show here that overexpression of Rss1/Gle1 also partially rescued depletion of Nup82 [10].

Analytical, diagnostic and therapeutic context of NUP82

• Indirect immunofluorescence of cells containing an epitope tagged copy of the NUP82 localized it to the nuclear pore complex (NPC) [5].
• We sublocalized the yeast nucleoporin Nup82 to the cytoplasmic side of the nuclear pore complex (NPC) by immunoelectron microscopy [10].
• Immunoprecipitation experiments using yeast cell lysates resulted in the coisolation of a Nup116p-Nup82p subcomplex [7].

References