Genomes and Genes
Gene Symbol: NUP116
Description: FG-nucleoporin NUP116
Alias: NSP116, FG-nucleoporin NUP116
Species: Saccharomyces cerevisiae S288c
- Miao M, Ryan K, Wente S. The integral membrane protein Pom34p functionally links nucleoporin subcomplexes. Genetics. 2006;172:1441-57 pubmed..We speculate that multiple integral membrane proteins, either within the nuclear pore domain or in the nuclear envelope, execute coordinated roles in NPC structure and function. ..
- Rout M, Blobel G. Isolation of the yeast nuclear pore complex. J Cell Biol. 1993;123:771-83 pubmed..It retains all but one of the eight known NPC proteins. In addition it contains as many as 80 uncharacterized proteins that are candidate NPC proteins. ..
- Wente S, Blobel G. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J Cell Biol. 1994;125:955-69 pubmed..analyzed the synthetic lethal phenotypes among GLFG nucleoporin mutant alleles, and found that strains harboring nup116 and either nup100 or nup145 mutations were not viable...
- Wente S, Rout M, Blobel G. A new family of yeast nuclear pore complex proteins. J Cell Biol. 1992;119:705-23 pubmed..Three individual members of this family, NUP49, NUP100, and NUP116, have been isolated and then characterized by a combination of molecular genetics and immunolocalization...
- Iovine M, Wente S. A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p. J Cell Biol. 1997;137:797-811 pubmed..This finding highlights an important role for a subfamily of GLFG nucleoporins in nuclear export processes. ..
- Aitchison J, Blobel G, Rout M. Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science. 1996;274:624-7 pubmed..This finding suggests that the major function of Kap104p lies in returning mRNA binding proteins to the nucleus after mRNA export. ..
- Siniossoglou S, Santos Rosa H, Rappsilber J, Mann M, Hurt E. A novel complex of membrane proteins required for formation of a spherical nucleus. EMBO J. 1998;17:6449-64 pubmed..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. ..
- Fischer T, Strasser K, Rácz A, Rodriguez Navarro S, Oppizzi M, Ihrig P, et al. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. EMBO J. 2002;21:5843-52 pubmed..Taken together, our data suggest that the novel Sac3p-Thp1p complex functions by docking the mRNP to specific nucleoporins at the nuclear entrance of the NPC. ..
- Strawn L, Shen T, Wente S. The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. J Biol Chem. 2001;276:6445-52 pubmed..protein (GFP)-tagged mRNA transport factors were individually examined in yeast cells overexpressing the Nup116-GLFG region. The essential mRNA export factors Mex67-GFP, Mtr2-GFP, and Dbp5-GFP accumulated in the nucleus...
- Patel S, Belmont B, Sante J, Rexach M. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell. 2007;129:83-96 pubmed..The results support a two-gate model of NPC architecture featuring a central diffusion gate formed by a meshwork of cohesive FG nucleoporin filaments and a peripheral gate formed by repulsive FG nucleoporin filaments...
- Ho A, Raczniak G, Ives E, Wente S. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Mol Biol Cell. 1998;9:355-73 pubmed..200 amino acids of the nucleoporin Nup116p had no effect on wild-type yeast cells, but it rendered the nup116 null strain inviable at all temperatures and coincidentally resulted in the formation of nuclear membrane ..
- Murphy R, Watkins J, Wente S. GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function. Mol Biol Cell. 1996;7:1921-37 pubmed..We propose that Gle2p has a novel role in mediating nuclear transport. ..
- Iovine M, Watkins J, Wente S. The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J Cell Biol. 1995;131:1699-713 pubmed..Previous experiments characterized the unique morphological perturbations that occur in a nup116 null mutant: temperature-sensitive formation of nuclear envelope seals over the cytoplasmic face of the NPC (Wente,..
- Stage Zimmermann T, Schmidt U, Silver P. Factors affecting nuclear export of the 60S ribosomal subunit in vivo. Mol Biol Cell. 2000;11:3777-89 pubmed..Together, these data further define the requirements for ribosomal subunit export and suggest a biological function for KAP120. ..
- Takano A, Kajita T, Mochizuki M, Endo T, Yoshihisa T. Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus. elife. 2015;4: pubmed publisher..Ssa2p also binds Nup116, one of the yeast nucleoporins...
- McGuire A, Mangroo D. Cex1p facilitates Rna1p-mediated dissociation of the Los1p-tRNA-Gsp1p-GTP export complex. Traffic. 2012;13:234-56 pubmed publisher..It is possible that this tRNA unloading mechanism is conserved in evolutionarily diverse organisms and that other Gsp1p-GTP-dependent export processes use a pathway-specific component to recruit Rna1p to the NPC. ..
- Wu X, Jiang Y. Overproduction of non-translatable mRNA silences. The transcription of Ty1 retrotransposons in S. cerevisiae via functional inactivation of the nuclear cap-binding complex and subsequent hyperstimulation of the TORC1 pathway. Yeast. 2008;25:327-47 pubmed publisher..Although overproduction of non-translatable mRNA causes transient Ty1 transcriptional silencing, it does not play a detectable role in controlling Ty1 retrotransposition. ..
- Seedorf M, Damelin M, Kahana J, Taura T, Silver P. Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol Cell Biol. 1999;19:1547-57 pubmed..These data indicate that transport receptors such as Pse1p interact in a Ran-dependent manner with certain nucleoporins. These nucleoporins may represent major docking sites for Pse1p as it moves in or out of the nucleus via the NPC. ..
- Schmidt H, GÃ¶rlich D. Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity. elife. 2015;4: pubmed publisher..Their exquisite NPC-typical sorting selectivity and strong intrinsic assembly propensity suggest that Nup98 FG phases can form in authentic NPCs and indeed account for the permeability properties of the pore. ..
- Patel S, Rexach M. Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium. Mol Cell Proteomics. 2008;7:121-31 pubmed..As the Bead Halo assay detected molecular interactions in cell lysates, as well as between purified components, it can be adapted for large-scale proteomic studies using automated robotics and microscopy. ..
- Liu S, Stewart M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p. J Mol Biol. 2005;349:515-25 pubmed..The length and composition of this linker is crucial and suggests how differences in affinity for Kap95p both between and within FG-nucleoporins arise. ..
- Olsson I, Berrez J, Leipus A, Ostlund C, Mutvei A. The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100. Exp Cell Res. 2007;313:1778-89 pubmed..In addition, a genome-wide transcription study of the rmt2Delta mutant shows significant downregulation of the transcription of MYO1, encoding the Type II myosin heavy chain required for cytokinesis and cell separation. ..
- Stuwe T, von Borzyskowski L, Davenport A, Hoelz A. Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex. J Mol Biol. 2012;419:330-46 pubmed publisher..Thus, the cytoplasmic filament network of the NPC is robust, consistent with its essential function in nucleocytoplasmic transport. ..
- Kumar N, Gaur D, Masison D, Sharma D. The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones. G3 (Bethesda). 2014;4:461-70 pubmed publisher..Furthermore, the short amino-terminal extension of the BAG domain profoundly affects its function. ..
- Webster B, Thaller D, Jager J, Ochmann S, Borah S, Lusk C. Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing. EMBO J. 2016;35:2447-2467 pubmed
- Wimmer C, Doye V, Grandi P, Nehrbass U, Hurt E. A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. EMBO J. 1992;11:5051-61 pubmed..The genes of two complementation groups, NSP116 and NSP49, were cloned...
- Fernandez Martinez J, Kim S, Shi Y, Upla P, Pellarin R, Gagnon M, et al. Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform. Cell. 2016;167:1215-1228.e25 pubmed publisher..We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC. ..
- Sarkar A, Pech M, Thoms M, Beckmann R, Hurt E. Ribosome-stalk biogenesis is coupled with recruitment of nuclear-export factor to the nascent 60S subunit. Nat Struct Mol Biol. 2016;23:1074-1082 pubmed publisher..Thus, a spatiotemporal mark on the ribosomal stalk controls the recruitment of an RNA-export receptor to the nascent 60S subunit. ..
- Kerr S, Azzouz N, Fuchs S, Collart M, Strahl B, Corbett A, et al. The Ccr4-Not complex interacts with the mRNA export machinery. PLoS ONE. 2011;6:e18302 pubmed publisher..These results shed further insight into the biological functions of Ccr4-Not and suggest that this complex is involved in all aspects of mRNA biogenesis, from the regulation of transcription to mRNA export and turnover. ..
- Dawson T, Lazarus M, Hetzer M, Wente S. ER membrane-bending proteins are necessary for de novo nuclear pore formation. J Cell Biol. 2009;184:659-75 pubmed publisher..We hypothesize that these ER membrane-bending proteins mediate early NPC assembly steps...
- Hayakawa A, Babour A, Sengmanivong L, Dargemont C. Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae. J Cell Biol. 2012;196:19-27 pubmed publisher..This led to defects in nuclear segregation at the onset of mitosis. Thus, defining ubiquitylation of the yeast NPC highlights yet-unexplored functions of this essential organelle in cell division. ..
- Damelin M, Silver P. Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Mol Cell. 2000;5:133-40 pubmed..These data demonstrate the utility of FRET in mapping dynamic protein interactions in a genetic system. Furthermore, the data indicate that an importin and exportin have overlapping pathways through the NPC. ..
- Nazarenus T, Cedarberg R, Bell R, Cheatle J, Forch A, Haifley A, et al. Upf1p, a highly conserved protein required for nonsense-mediated mRNA decay, interacts with the nuclear pore proteins Nup100p and Nup116p. Gene. 2005;345:199-212 pubmed
- Sharma K, Fabre E, Tekotte H, Hurt E, Tollervey D. Yeast nucleoporin mutants are defective in pre-tRNA splicing. Mol Cell Biol. 1996;16:294-301 pubmed..Mutation of NUP49, NUP116, or NUP145 has previously been shown to lead to nuclear poly(A)+ RNA accumulation, indicating that these ..
- Das S, Saha U, Das B. Cbc2p, Upf3p and eIF4G are components of the DRN (Degradation of mRNA in the Nucleus) in Saccharomyces cerevisiae. FEMS Yeast Res. 2014;14:922-32 pubmed publisher..been shown to act on RNAs preferentially retained in the nucleus, such as: (1) global mRNAs in export defective nup116-? mutant strains at the restrictive temperature; (2) a certain class of normal mRNAs called special mRNAs (e.g...
- Grant R, Neuhaus D, Stewart M. Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution. J Mol Biol. 2003;326:849-58 pubmed
- Ho A, Shen T, Ryan K, Kiseleva E, Levy M, Allen T, et al. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol Cell Biol. 2000;20:5736-48 pubmed..the absence of Nup116p had no effect on the NPC localization of Nup82p, overexpression of C-terminal Nup116p in a nup116 null mutant resulted in Nup82p mislocalization...
- McGuire A, Mangroo D. Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery. EMBO J. 2007;26:288-300 pubmed..cerevisiae. They also suggest that Cex1p collects aminoacyl-tRNAs from the nuclear export receptors at the cytoplasmic side of the nuclear pore complex, and transfers them to eEF-1A using a channelling mechanism. ..
- Bailer S, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, et al. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem. 2000;275:23540-8 pubmed..Finally, synthetic lethal interactions were found between mutant alleles of NUP116 and all members of the Nup82p complex...
- Robinson M, Park S, Sun Z, Silver P, Wagner G, Hogle J. Multiple conformations in the ligand-binding site of the yeast nuclear pore-targeting domain of Nup116p. J Biol Chem. 2005;280:35723-32 pubmed..This study offers a high resolution view of a yeast nucleoporin structural domain and may provide insights into NPC architecture and function. ..
- Lord C, Timney B, Rout M, Wente S. Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae. J Cell Biol. 2015;208:729-44 pubmed publisher..Mutants lacking the GLFG domain of Nup116 displayed decreased RLSs, whereas longevity was increased in nup100-null mutants...
- Damelin M, Silver P. In situ analysis of spatial relationships between proteins of the nuclear pore complex. Biophys J. 2002;83:3626-36 pubmed..We suggest that the approach may serve as a prototype for the in situ study of other large macromolecular complexes. ..
- Kiseleva E, Allen T, Rutherford S, Bucci M, Wente S, Goldberg M. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. J Struct Biol. 2004;145:272-88 pubmed..We conclude that peripheral NPC components appear similar in yeasts compared to higher organisms and present a revised model for yeast NPC structural composition. ..
- Gómez Navarro N, Peiró Chova L, Rodriguez Navarro S, Polaina J, Estruch F. Rtp1p is a karyopherin-like protein required for RNA polymerase II biogenesis. Mol Cell Biol. 2013;33:1756-67 pubmed publisher..Our results define Rtp1p as a new component of the RNA pol II biogenesis machinery that plays roles in subunit assembly and likely in transport through the nuclear pore complex. ..
- Kappel L, Loibl M, Zisser G, Klein I, Fruhmann G, Gruber C, et al. Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S maturation. J Cell Biol. 2012;199:771-82 pubmed publisher..Rlp24 release required ATP and was promoted by the interaction of Drg1 with the nucleoporin Nup116. Subsequent ATP hydrolysis in the first AAA domain dissociated Drg1 from Rlp24, liberating both proteins for ..
- Sarkar S, Hopper A. tRNA nuclear export in saccharomyces cerevisiae: in situ hybridization analysis. Mol Biol Cell. 1998;9:3041-55 pubmed..Our results also argue against inappropriate subnuclear compartmentalization causing defects in pre-tRNA splicing. Rather, the data support "feedback" of nucleus/cytosol exchange to the pre-tRNA splicing machinery. ..
- Occhipinti L, Chang Y, Altvater M, Menet A, Kemmler S, Panse V. Non-FG mediated transport of the large pre-ribosomal subunit through the nuclear pore complex by the mRNA export factor Gle2. Nucleic Acids Res. 2013;41:8266-79 pubmed publisher..basic patch required to bind pre-60S, and a second surface that makes non-FG contacts with the nucleoporin Nup116. A basic patch mutant of Gle2 is able to function in mRNA export, but not pre-60S export...
- Miller A, Suntharalingam M, Johnson S, Audhya A, Emr S, Wente S. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. J Biol Chem. 2004;279:51022-32 pubmed..Enhanced lethality was observed with a specific subset of mutants, including nup42, nup116, nup159, dbp5, and gle2, all of which had been previously connected to Gle1 function...
- Fabre E, Hurt E. Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet. 1997;31:277-313 pubmed..We review here our current knowledge on the role of nucleoporins, and on the mechanism of nucleocytoplasmic transport, with emphasis on the yeast Saccharomyces cerevisiae. ..
- Das B, Butler J, Sherman F. Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae. Mol Cell Biol. 2003;23:5502-15 pubmedA nuclear mRNA degradation (DRN) system was identified from analysis of mRNA turnover rates in nup116-Delta strains of Saccharomyces cerevisiae lacking the ability to export all RNAs, including poly(A) mRNAs, at the restrictive ..
- Lei E, Stern C, Fahrenkrog B, Krebber H, Moy T, Aebi U, et al. Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex. Mol Biol Cell. 2003;14:836-47 pubmed..Finally, Mex67 accumulates at the nuclear rim when SAC3 is mutated, suggesting that Sac3 functions in Mex67 translocation through the NPC. ..
- Ratner G, Hodel A, Powers M. Molecular determinants of binding between Gly-Leu-Phe-Gly nucleoporins and the nuclear pore complex. J Biol Chem. 2007;282:33968-76 pubmed..We previously proposed that Nup145N, and possibly the other orthologs Nup116 and Nup100, might bind to Nup145C as demonstrated for Nup98 and Nup96...