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Gene Review:

NUP85 - Nup85p

Saccharomyces cerevisiae S288c

Synonyms: J1624, Nuclear pore protein NUP85, Nucleoporin NUP85, RAT9, YJR042W

Allen, N.P. et al., Segref, A. et al., Goldstein, A.L. et al., Siniossoglou, S. et al., Rappsilber, J. et al., et al.

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High impact information on NUP85

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].
For the assembly of the complex, Nup85p, Nup120p, and Nup145p-C are essential [2].
MTR10, previously shown to be involved in mRNA export, was found in a synthetic lethal relationship with nucleoporin NUP85 [3].
An essential cellular factor for nuclear mRNA export called Mex67p which has homologous proteins in human and Caenorhabditis elegans was identified through its genetic interaction with nucleoporin Nup85p [4].
In contrast, no accumulation of any pre-tRNA was observed in strains mutant for Nup1p, Nup85p, or Nup100p [5].

Anatomical context of NUP85

At the permissive growth temperature in rat9-1 or RAT9 deletion strains, the nuclear envelope (NE) becomes detached from the main body of the nucleus, forming long thin double sheets of NE [6].
In this study, a member of the yeast nuclear pore complex (Nup85p) was tagged and a six-member sub-complex of the pore was cross-linked and analyzed by 1D SDS-PAGE [7].

Physical interactions of NUP85

More interestingly, we demonstrate that the Nup84p complex contains Nup133p as a subunit and binds to the FG repeat regions of Nups directly via the Nup85p subunit [8].

Other interactions of NUP85

Binding of Nup85p to the GLFG region of Nup116p was quantified in vitro (K(D) = 1.5 micro M) and was confirmed in vivo using the yeast two-hybrid assay [8].

References

A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Siniossoglou, S., Wimmer, C., Rieger, M., Doye, V., Tekotte, H., Weise, C., Emig, S., Segref, A., Hurt, E.C. Cell (1996) [Pubmed]
Structure and assembly of the Nup84p complex. Siniossoglou, S., Lutzmann, M., Santos-Rosa, H., Leonard, K., Mueller, S., Aebi, U., Hurt, E. J. Cell Biol. (2000) [Pubmed]
Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. Senger, B., Simos, G., Bischoff, F.R., Podtelejnikov, A., Mann, M., Hurt, E. EMBO J. (1998) [Pubmed]
Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. Segref, A., Sharma, K., Doye, V., Hellwig, A., Huber, J., Lührmann, R., Hurt, E. EMBO J. (1997) [Pubmed]
Yeast nucleoporin mutants are defective in pre-tRNA splicing. Sharma, K., Fabre, E., Tekotte, H., Hurt, E.C., Tollervey, D. Mol. Cell. Biol. (1996) [Pubmed]
Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p. Goldstein, A.L., Snay, C.A., Heath, C.V., Cole, C.N. Mol. Biol. Cell (1996) [Pubmed]
A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry. Rappsilber, J., Siniossoglou, S., Hurt, E.C., Mann, M. Anal. Chem. (2000) [Pubmed]
Deciphering networks of protein interactions at the nuclear pore complex. Allen, N.P., Patel, S.S., Huang, L., Chalkley, R.J., Burlingame, A., Lutzmann, M., Hurt, E.C., Rexach, M. Mol. Cell Proteomics (2002) [Pubmed]

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AGOS_AEL073C	Ashbya gossypii ATCC 10895
KLLA0E22463g	Kluyveromyces lactis NRRL Y-1140

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