NSP1/YJL041W Summary Help

NSP1 BASIC INFORMATION

Standard Name NSP1
Systematic Name YJL041W
Feature Type ORF, Verified
Description Essential component of the nuclear pore complex, which mediates nuclear import and export, found in both the Nup82 and Nic96 complexes (1, 2, 3, 4 and see Summary Paragraph)
Name Description NucleoSkeletal-like Protein 1
GO Annotations All NSP1 GO evidence and references
    View Computational GO annotations for NSP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All NSP1 Phenotype details and references
Classical genetics
conditional
Large-scale survey
null
Interactions NSP1 All interactions details and references
132 total interaction(s) for 45 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 63
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 20
  • Co-fractionation: 2
  • Co-purification: 6
  • PCA: 4
  • Reconstituted Complex: 12
  • Two-hybrid: 7
Genetic Interactions
  • Dosage Rescue: 1
  • Phenotypic Enhancement: 2
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 12
Sequence Information
ChrX:365778 to 368367 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2009-02-18 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1 365778..365778 2009-02-18 1996-07-31
Intron 2..119 365779..365896 2009-02-18 1996-07-31
CDS 120..2590 365897..368367 2009-02-18 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000003577

NSP1 RESOURCES

Click on map for expanded view
SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for NSP1

NOMENCLATURE CONFLICT NOTE

NameRelevanceDescription
TFS1Nomenclature conflictBoth YJL041W/NSP1 and YLR178C/TFS1 have been called NSP1

SUMMARY PARAGRAPH for NSP1

NSP1 encodes an essential nuclear pore protein (1, 5, 6, 7). Transport of macromolecules between the nucleus and the cytoplasm of eukaryotic cells occurs through the nuclear pore complex (NPC), a large macromolecular complex that spans the nuclear envelope (reviewed in 7, 6, 8, 9). The structure of the vertebrate NPC has been studied extensively; recent reviews include 10, 11, 12, and 13. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate (14, 15). Many yeast nuclear pore proteins, or nucleoporins, have been identified by a variety of genetic approaches (reviewed in 7, 6, 16, 17, 18).

Numerous lines of evidence suggest that Nsp1p plays a key role in nucleocytoplasmic transport. Conditional mutations in NSP1 or depletion of Nsp1p cause defects in protein import into the nucleus (19), and Nsp1p depletion also reduces the number of NPCs (20). nsp1 mutants are also defective in export of ribosome subunits from the nucleus (21). Further, several other nucleoporin genes have been identified in yeast by screening for mutations that are synthetically lethal with conditional nsp1 mutations. (7)

Nsp1p is found in a subcomplex of the NPC that also contains Nup49p, Nup57p, and Nic96p (7, 22, 23). This complex has been detected at both the nuclear and cytoplasmic periphery of the NPC central channel (2). A second complex containing Nsp1p and Nup82p (24) is found only at the cytoplasmic periphery of the channel (2). Nsp1p also binds to the small GTPase Gsp1p in vitro (25), and can associate with the importin Pse1p (26).

Nsp1p is one of a group of nucleoporins that contain multiple repeats of the amino acids FXFG; deletion of the FXFG repeats has no effect on cell viability (5, 6, 7). Nsp1p shows sequence similarity to a nucleoporin, p62, found in NPCs from higher eukaryotes such as human (27) and rat (7).

Last updated: 1999-06-25

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for NSP1]

1) Hurt EC  (1988) A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae. EMBO J 7(13):4323-34
2) Fahrenkrog B, et al.  (1998) Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes. J Cell Biol 143(3):577-88
3) Bailer SM, et al.  (2001) 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 21(23):7944-55
4) Lutzmann M, et al.  (2005) Reconstitution of Nup157 and Nup145N into the Nup84 complex. J Biol Chem 280(18):18442-51
5) Nehrbass U, et al.  (1990) NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain. Cell 61(6):979-89
6) Wente SR, et al.  (1997) "The nucleus and nucleocytoplasmic transport in Saccharomyces cerevisiae." Pp. 471-546 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Cell Cycle and Cell Biology, edited by Pringle JR, Broach JR and Jones EW. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
7) Fabre E and Hurt E  (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31:277-313
8) Pemberton LF, et al.  (1998) Transport routes through the nuclear pore complex. Curr Opin Cell Biol 10(3):392-9
9) Izaurralde E and Adam S  (1998) Transport of macromolecules between the nucleus and the cytoplasm. RNA 4(4):351-64
10) Hinshaw JE  (1994) Architecture of the nuclear pore complex and its involvement in nucleocytoplasmic transport. Biochem Pharmacol 47(1):15-20
11) Pante N and Aebi U  (1996) Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol 31(2):153-99
12) Davis LI  (1995) The nuclear pore complex. Annu Rev Biochem 64:865-96
13) Pante N and Aebi U  (1994) Toward the molecular details of the nuclear pore complex. J Struct Biol 113(3):179-89
14) Rout MP and Blobel G  (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123(4):771-83
15) Yang Q, et al.  (1998) Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol Cell 1(2):223-34
16) Doye V and Hurt E  (1997) From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol 9(3):401-11
17) Doye V and Hurt EC  (1995) Genetic approaches to nuclear pore structure and function. Trends Genet 11(6):235-41
18) Newmeyer DD  (1993) The nuclear pore complex and nucleocytoplasmic transport. Curr Opin Cell Biol 5(3):395-407
19) Nehrbass U, et al.  (1993) Analysis of nucleo-cytoplasmic transport in a thermosensitive mutant of nuclear pore protein NSP1. Eur J Cell Biol 62(1):1-12
20) Mutvei A, et al.  (1992) NSP1 depletion in yeast affects nuclear pore formation and nuclear accumulation. Eur J Cell Biol 59(2):280-95
21) Hurt E, et al.  (1999) A novel in vivo assay reveals inhibition of ribosomal nuclear export in ran-cycle and nucleoporin mutants. J Cell Biol 144(3):389-401
22) Schlaich NL, et al.  (1997) In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p. Mol Biol Cell 8(1):33-46
23) Grandi P, et al.  (1993) Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96. EMBO J 12(8):3061-71
24) Grandi P, et al.  (1995) A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J Cell Biol 130(6):1263-73
25) Stochaj U, et al.  (1998) The small GTPase Gsp1p binds to the repeat domain of the nucleoporin Nsp1p. Biochem J 330 ( Pt 1)():421-7
26) Seedorf M, et al.  (1999) Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol Cell Biol 19(2):1547-57
27) Carmo-Fonseca M, et al.  (1991) Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur J Cell Biol 55(1):17-30