Genomes and Genes
Gene Symbol: NSP1
Description: FG-nucleoporin NSP1
Alias: FG-nucleoporin NSP1
Species: Saccharomyces cerevisiae S288c
- 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
- 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..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. ..
- Schrader N, Stelter P, Flemming D, Kunze R, Hurt E, Vetter I. Structural basis of the nic96 subcomplex organization in the nuclear pore channel. Mol Cell. 2008;29:46-55 pubmed publisherNic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC)...
- Strawn L, Shen T, Shulga N, Goldfarb D, Wente S. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol. 2004;6:197-206 pubmed..Significantly, symmetric deletions caused mild reductions in Kap95-Kap60-mediated import rates, but virtually abolished Kap104 import. These results suggest the existence of multiple translocation pathways. ..
- Frey S, Richter R, Gorlich D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science. 2006;314:815-7 pubmed..Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast. ..
- 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. ..
- Grandi P, Doye V, Hurt E. Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96. EMBO J. 1993;12:3061-71 pubmedThe essential C-terminal domain of NSP1 mediates assembly into the nuclear pore complex (NPC)...
- Fahrenkrog B, Hurt E, Aebi U, Pante N. Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes. J Cell Biol. 1998;143:577-88 pubmed..Accordingly, Nsp1p resides in three distinct subcomplexes which are located at the entry and exit of the central gated channel and at the terminal ring of the nuclear basket. ..
- Schlaich N, Haner M, Lustig A, Aebi U, Hurt E. In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p. Mol Biol Cell. 1997;8:33-46 pubmed..We conclude that Nsp1p, Nup49p, and Nup57p can reconstitute a complex in vitro which is competent for further assembly with other components of nuclear pores. ..
- Hurt E, Hannus S, Schmelzl B, Lau D, Tollervey D, Simos G. A novel in vivo assay reveals inhibition of ribosomal nuclear export in ran-cycle and nucleoporin mutants. J Cell Biol. 1999;144:389-401 pubmed..However, thermosensitive rna1-1 (Ran-GAP), prp20-1 (Ran-GEF), and nucleoporin nup49 and nsp1 mutants are impaired in ribosomal export as revealed by nuclear accumulation of L25-GFP...
- Frey S, Gorlich D. FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties. EMBO J. 2009;28:2554-67 pubmed publisher..NTRs not only left the barrier intact, they even tightened it against passive influx, pointing to a role for NTRs in establishing and maintaining the permeability barrier of NPCs. ..
- 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..Dyn2 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...
- Grandi P, Schlaich N, Tekotte H, Hurt E. Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p. EMBO J. 1995;14:76-87 pubmed..acid substitutions in the central domain yield thermosensitive mutants, which do not impair interaction with the Nsp1 complex; the C-terminal domain is neither essential nor required for binding to the nucleoporin complex, but ..
- Wong D, Corbett A, Kent H, Stewart M, Silver P. Interaction between the small GTPase Ran/Gsp1p and Ntf2p is required for nuclear transport. Mol Cell Biol. 1997;17:3755-67 pubmed..Taken together, these data demonstrate that the interaction between Gsp1p and Ntf2p is critical for nuclear transport. ..
- 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 pubmedb>NSP1 is a nuclear pore protein (nucleoporin) essential for cell growth...
- Hellmuth K, Lau D, Bischoff F, Kunzler M, Hurt E, Simos G. Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA. Mol Cell Biol. 1998;18:6374-86 pubmed..These data confirm the homology between Los1p and the recently identified human exportin for tRNA and reinforce the possibility of a role for Los1p in nuclear export of tRNA in yeast. ..
- 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. ..
- Rosenblum J, Pemberton L, Blobel G. A nuclear import pathway for a protein involved in tRNA maturation. J Cell Biol. 1997;139:1655-61 pubmed..In addition, through its association with ribosomal proteins, Sxm1p may have a role in coordinating ribosome biogenesis with tRNA processing. ..
- Nehrbass U, Kern H, Mutvei A, Horstmann H, Marshallsay B, Hurt E. NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain. Cell. 1990;61:979-89 pubmedb>NSP1 is located at the nuclear periphery in yeast and is essential for cell growth. Employing immunoelectron microscopy on yeast cells, we show that NSP1 is located at the nuclear pores...
- 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...
- 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. ..
- 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..Consistently, the Nsp1p-Nup57p-Nup49p core complex dissociates from the nuclear pores in nsp1 coil 3 and 4 mutant cells, and as a consequence, defects in nuclear protein import are observed...
- 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. ..
- 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. ..
- Gomar Alba M, del Olmo M. Hot1 factor recruits co-activator Sub1 and elongation complex Spt4/5 to osmostress genes. Biochem J. 2016;473:3065-79 pubmed publisher..Instead, other data presented herein indicate a key function of the Hot1 transcription factor in the recruitment of these proteins to the promoter or the 5'-coding region of the genes under its control. ..
- 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..NPCs and newly synthesized NPC protomers (nups) through anaphase, we uncovered a pool of the central channel nup Nsp1 that is actively targeted to the bud in association with endoplasmic reticulum...
- Treusch S, Lindquist S. An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol. 2012;197:369-79 pubmed publisher..Our work illustrates how the promiscuous interactions of an intrinsically disordered protein can produce highly specific cellular toxicities through illicit, yet highly specific, interactions with the proteome. ..
- 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
- Wagner R, Kapinos L, Marshall N, Stewart M, Lim R. Promiscuous binding of KaryopherinÎ²1 modulates FG nucleoporin barrier function and expedites NTF2 transport kinetics. Biophys J. 2015;108:918-927 pubmed publisher..This suggests that binding promiscuity confers kinetic advantages to NTF2 by expediting its facilitated diffusion and reinforces the proposal that KapÎ²1 contributes to the integral barrier function of the NPC. ..
- 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. ..
- 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. ..
- Hung N, Lo K, Patel S, Helmke K, Johnson A. Arx1 is a nuclear export receptor for the 60S ribosomal subunit in yeast. Mol Biol Cell. 2008;19:735-44 pubmed..These results show that Arx1 can directly bridge the interaction between the pre-60S particle and the NPC and thus is a third export receptor for the 60S subunit in yeast. ..
- Gao H, Sumanaweera N, Bailer S, Stochaj U. Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p. J Biol Chem. 2003;278:25331-40 pubmed..Taken together, components of the NPC subcomplex containing Rat2p/Nup120p, Nup133p, and Nup85p, in addition to proteins Nic96p and Mtr7p, are shown to be crucial for the formation of a nucleocytoplasmic Gsp1p gradient. ..
- Hobeika M, Brockmann C, Gruessing F, Neuhaus D, Divita G, Stewart M, et al. Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats. J Biol Chem. 2009;284:17575-83 pubmed publisher
- Jones A, Quimby B, Hood J, Ferrigno P, Keshava P, Silver P, et al. SAC3 may link nuclear protein export to cell cycle progression. Proc Natl Acad Sci U S A. 2000;97:3224-9 pubmed..Our results also demonstrate that SAC3 interacts genetically with the nuclear protein export factors Crm1p/Xpo1p and Yrb2p. Taken together, these data indicate a link between nuclear protein export and transition through the cell cycle. ..
- Huang L, Baldwin M, Maltby D, Medzihradszky K, Baker P, Allen N, et al. The identification of protein-protein interactions of the nuclear pore complex of Saccharomyces cerevisiae using high throughput matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry. Mol Cell Proteomics. 2002;1:434-50 pubmed..Other considerations essential for successful high throughput protein analysis are discussed. ..
- 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. ..
- Oeffinger M, Dlakic M, Tollervey D. A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits. Genes Dev. 2004;18:196-209 pubmed..We propose that Rrp12p binds to the RNA components of the pre-ribosomes and promotes export of both subunits via its interactions with the nucleoporins and Gsp1p. ..
- 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..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...
- Stochaj U, Hejazi M, Belhumeur P. The small GTPase Gsp1p binds to the repeat domain of the nucleoporin Nsp1p. Biochem J. 1998;330 ( Pt 1):421-7 pubmed..We further demonstrate that both Gsp1p and Nsp1p are components of larger protein complexes in vivo, supporting the idea that the association between both proteins takes place in growing cells. ..
- 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. ..
- 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..Finally, Bead Halo detected binding of the nups Gle1, Nup60, and Nsp1 to phospholipid bilayers...
- 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. ..
- 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. ..
- Ulrich A, Partridge J, Schwartz T. The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution. Mol Biol Cell. 2014;25:1484-92 pubmed publisher..For the homologous Nsp1 complex from Saccharomyces cerevisiae, we determine the same stoichiometry, indicating evolutionary conservation...
- Loeb J, Davis L, Fink G. NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex. Mol Biol Cell. 1993;4:209-22 pubmed..The NUP2 protein sequence shares a central repetitive domain with NSP1 and NUP1, the two previously characterized yeast nucleoporins...
- Tan Q, Li X, Sadhale P, Miyao T, Woychik N. Multiple mechanisms of suppression circumvent transcription defects in an RNA polymerase mutant. Mol Cell Biol. 2000;20:8124-33 pubmed..Taken together, these results demonstrate that these three proteins influence transcription and implicate Sro9p in both transcription and posttranscription events. ..