Genomes and Genes
Gene Symbol: NUP159
Description: FG-nucleoporin NUP159
Alias: NUP158, RAT7, FG-nucleoporin NUP159
Species: Saccharomyces cerevisiae S288c
- 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..In particular, Nup159, a nucleoporin exclusively located on the cytoplasmic side of the NPC, was monoubiquitylated by the Cdc34/SCF (..
- Scarcelli J, Hodge C, Cole C. The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexes. J Cell Biol. 2007;178:799-812 pubmed..Thus, Apq12p connects nuclear pore biogenesis to the dynamics of the NE. ..
- 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. ..
- 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. ..
- Alber F, Dokudovskaya S, Veenhoff L, Zhang W, Kipper J, Devos D, et al. The molecular architecture of the nuclear pore complex. Nature. 2007;450:695-701 pubmed..These findings provide clues to the evolutionary origins of the NPC. ..
- Weirich C, Erzberger J, Berger J, Weis K. The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Mol Cell. 2004;16:749-60 pubmed..The cytoplasmically oriented nuclear pore protein Nup159 plays a critical role in mRNA export through its conserved N-terminal domain (NTD)...
- Gorsch L, Dockendorff T, Cole C. A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J Cell Biol. 1995;129:939-55 pubmed..for Saccharomyces cerevisiae genes required for nucleocytoplasmic transport of messenger RNA, we identified the RAT7 gene (ribonucleic acid trafficking), which encodes an essential protein of 1,460 amino acids...
- 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
- Hodge C, Colot H, Stafford P, Cole C. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 1999;18:5778-88 pubmed..the growth and mRNA export defects of rat7DeltaN cells and resulted in weaker suppression in cells carrying rat7-1 or the rss1-37 allele of GLE1. Dbp5p interacts with Gle1p independently of the N-terminus of Dbp5p...
- Pemberton L, Rosenblum J, Blobel G. A distinct and parallel pathway for the nuclear import of an mRNA-binding protein. J Cell Biol. 1997;139:1645-53 pubmed..Thus, at least two parallel pathways function in the import of mRNA-binding proteins, suggesting the need for the coordination of these pathways. ..
- Belgareh N, Snay Hodge C, Pasteau F, Dagher S, Cole C, Doye V. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell. 1998;9:3475-92 pubmed..In vivo transport assays further revealed that nup82Delta108 and nup159-1/rat7-1 mutant strains have little if any defect in nuclear protein import and protein export...
- Chadrin A, Hess B, San Roman M, Gatti X, Lombard B, Loew D, et al. Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution. J Cell Biol. 2010;189:795-811 pubmed publisher..We hypothesize that, by modifying or stabilizing the nuclear envelope-NPC interface, Pom33 may contribute to proper distribution and/or efficient assembly of nuclear pores. ..
- Bailer S, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001;21:7944-55 pubmed..Thus, distinct coiled-coil regions within Nsp1p-C have separate functions that are related to the assembly of different NPC subcomplexes, nucleocytoplasmic transport, and incorporation into the nuclear pores. ..
- 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. ..
- Strasser K, Bassler J, Hurt E. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J Cell Biol. 2000;150:695-706 pubmed
- Del Priore V, Snay C, Bahr A, Cole C. The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the RAT7/NUP159 nucleoporin, is required for efficient mRNA export. Mol Biol Cell. 1996;7:1601-21 pubmedRAT7/NUP159 was identified previously in a screen for genes whose products are important for nucleocytoplasmic export of poly(A)+ RNA and encodes an essential nucleoporin...
- 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. ..
- Stelter P, Kunze R, Flemming D, Höpfner D, Diepholz M, Philippsen P, et al. Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol. 2007;9:788-96 pubmed..is a previously undescribed nucleoporin that functions as molecular glue to dimerize and stabilize the Nup82-Nsp1-Nup159 complex, a module of the cytoplasmic pore filaments...
- Vasu S, Forbes D. Nuclear pores and nuclear assembly. Curr Opin Cell Biol. 2001;13:363-75 pubmed
- Brune C, Munchel S, Fischer N, Podtelejnikov A, Weis K. Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export. RNA. 2005;11:517-31 pubmed..Therefore, nuclear Pab1 may be required for efficient mRNA export and may function in the quality control of mRNA in the nucleus. ..
- West M, Hedges J, Lo K, Johnson A. Novel interaction of the 60S ribosomal subunit export adapter Nmd3 at the nuclear pore complex. J Biol Chem. 2007;282:14028-37 pubmed..These results suggest that in the absence of the ribosome, Nmd3 is not efficiently released from Crm1 at the NPC. ..
- Rollenhagen C, Hodge C, Cole C. The nuclear pore complex and the DEAD box protein Rat8p/Dbp5p have nonessential features which appear to facilitate mRNA export following heat shock. Mol Cell Biol. 2004;24:4869-79 pubmed..These studies also suggest that both nuclear pores and Rat8p have features not required for mRNA export in growing cells but which enhance the ability of mRNAs to be exported following heat shock. ..
- Romes E, Tripathy A, Slep K. Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction. J Biol Chem. 2012;287:15862-73 pubmed publisher..The conserved Nup82 complex, composed of Nsp1, Nup82, and Nup159, forms the unique cytoplasmic fibrils that regulate mRNA nuclear export...
- Zeitler B, Weis K. The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo. J Cell Biol. 2004;167:583-90 pubmed..These findings suggest that the biased distribution of FG repeats is not required for major nucleocytoplasmic trafficking events across the NPC. ..
- Albertini M, Pemberton L, Rosenblum J, Blobel G. A novel nuclear import pathway for the transcription factor TFIIS. J Cell Biol. 1998;143:1447-55 pubmed..Hence Kap119p is a novel karyopherin that is responsible for the import of the transcription elongation factor TFIIS. ..
- Gaik M, Flemming D, von Appen A, Kastritis P, MÃ¼cke N, Fischer J, et al. Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold. J Cell Biol. 2015;208:283-97 pubmed publisher..into the structure, assembly, and function of the cytoplasmic pore filaments, we reconstituted in yeast the Nup82-Nup159-Nsp1-Dyn2 complex, which was suitable for biochemical, biophysical, and electron microscopy analyses...
- Hilleren P, McCarthy T, Rosbash M, Parker R, Jensen T. Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature. 2001;413:538-42 pubmed..In exosome mutants, hypo- as well as hyperadenylated mRNAs are released and translated. These observations suggest that the exosome contributes to a checkpoint that monitors proper 3'-end formation of mRNA. ..
- 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..Our results show that release of Rlp24 by Drg1 defines a key event in large subunit formation that is a prerequisite for progression of cytoplasmic pre-60S maturation. ..
- Niño C, Hayakawa A, Dargemont C, Babour A. Mapping ubiquitin modifications reveals new functions for the yeast nuclear pore complex. Cell Logist. 2012;2:43-45 pubmed
- Colombi P, Webster B, Fröhlich F, Lusk C. The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1. J Cell Biol. 2013;203:215-32 pubmed publisher..It further supports the finding that NPC inheritance, not de novo NPC assembly, is primarily responsible for controlling NPC number in daughter cells. ..
- Das B, Guo Z, Russo P, Chartrand P, Sherman F. The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation. Mol Cell Biol. 2000;20:2827-38 pubmed..Furthermore, cbc1-Delta greatly suppressed the degradation of mRNAs and other phenotypes of a rat7-1 strain which is defective in mRNA export...
- Folkmann A, Collier S, Zhan X, Ohi M, Wente S. Gle1 functions during mRNA export in an oligomeric complex that is altered in human disease. Cell. 2013;155:582-93 pubmed publisher..These results identify a mechanistic step in Gle1's mRNA export function at nuclear pore complexes and directly implicate altered export in LCCS1 disease pathology...
- Braunwarth A, Fromont Racine M, Legrain P, Bischoff F, Gerstberger T, Hurt E, et al. Identification and characterization of a novel RanGTP-binding protein in the yeast Saccharomyces cerevisiae. J Biol Chem. 2003;278:15397-405 pubmed..Based on these results and the exclusive conservation of the protein in the fungal kingdom, we hypothesize that Yrb30p represents a novel modulator of the Ran GTPase switch related to fungal lifestyle. ..
- 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...
- Hilleren P, Parker R. Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause hyperadenylation during 3'-end formation of nascent transcripts. RNA. 2001;7:753-64 pubmed..Strains carrying lesions in RAT7, GLE1, MEX67, and RAT8, produce nascent transcripts carrying poly(A) tails roughly 30 residues longer than the ..
- Das B, Butler J, Sherman F. Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae. Mol Cell Biol. 2003;23:5502-15 pubmed..We propose that certain normal mRNAs retained in the nucleus are degraded by the DRN system, similar to degradation of transcripts with 3' end formation defects in certain mutants. ..
- Noble K, Tran E, Alcázar Román A, Hodge C, Cole C, Wente S. The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1. Genes Dev. 2011;25:1065-77 pubmed publisher..Evidence suggests that Dbp5 binding to Nup159 is required for controlling interactions with Gle1 and the mRNP...
- Gleizes P, Noaillac Depeyre J, Leger Silvestre I, Teulières F, Dauxois J, Pommet D, et al. Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. J Cell Biol. 2001;155:923-36 pubmed..Thus, the Nup82p-Nup159p-Nsp1p nucleoporin complex is part of the nuclear export pathways of preribosomes and mRNPs, but with distinct functions in these two processes. ..
- Trahan C, Oeffinger M. Targeted cross-linking-mass spectrometry determines vicinal interactomes within heterogeneous RNP complexes. Nucleic Acids Res. 2016;44:1354-69 pubmed publisher..Our results therefore show that this method provides a new tool to study the changing spatial organization of heterogeneous dynamic RNP complexes. ..
- 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. ..
- Adams R, Terry L, Wente S. Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex. Genetics. 2014;197:1213-24 pubmed publisher..In Saccharomyces cerevisiae, the NPC proteins Nup159 and Nup42 are asymmetrically localized to the cytoplasmic face and have distinct functional domains: a ..
- Hodge C, Tran E, Noble K, Alcázar Román A, Ben Yishay R, Scarcelli J, et al. The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1. Genes Dev. 2011;25:1052-64 pubmed publisher..This requires Dbp5 interaction with Nup159 in NPC cytoplasmic filaments and activation of Dbp5's ATPase activity by Gle1 bound to inositol hexakisphosphate (..
- 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..forms of the protein, in complex with the N-terminal domain of Nup82 and the C-terminal tail fragment of Nup159. The Nup82 β propeller serves as a noncooperative binding platform for both binding partners...
- 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...
- Schmitt C, von Kobbe C, Bachi A, Pante N, Rodrigues J, Boscheron C, et al. Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. EMBO J. 1999;18:4332-47 pubmed..Together, our data indicate that Dbp5 is a conserved RNA-dependent ATPase which is recruited to the cytoplasmic fibrils of the NPC where it participates in the export of mRNAs out of the nucleus. ..
- 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. ..
- Nyarko A, Song Y, Nováček J, Zídek L, Barbar E. Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly. J Biol Chem. 2013;288:2614-22 pubmed publisher..Dyn2 is proposed to dimerize and stabilize the Nup82-Nsp1-Nup159 complex of the nuclear pore assembly through its interaction with nucleoporin Nup159...
- Yoshida K, Seo H, Debler E, Blobel G, Hoelz A. Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex. Proc Natl Acad Sci U S A. 2011;108:16571-6 pubmed publisher..complex, composed of fragments of three cytoplasmically oriented nucleoporins of yeast: Nup82, Nup116, and Nup159. Our data show that the Nup82 fragment, representing more than the N-terminal half of the molecule, folds into an ..
- Grosshans H, Deinert K, Hurt E, Simos G. Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol. 2001;153:745-62 pubmed..This particle can then be targeted to the nuclear pores and is subsequently exported to the cytoplasm in an Xpo1p-dependent way. ..
- Paul B, Montpetit B. Altered RNA processing and export lead to retention of mRNAs near transcription sites and nuclear pore complexes or within the nucleolus. Mol Biol Cell. 2016;27:2742-56 pubmed publisher..These data show that alterations to various nuclear processes lead to the retention of mRNAs at discrete locations within the nucleus. ..