YIL115C
(Redirected from NUP158)
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| Systematic name | YIL115C |
| Gene name | NUP159 |
| Aliases | NUP158, RAT7 |
| Feature type | ORF, Verified |
| Coordinates | Chr IX:148709..144327 |
| Primary SGDID | S000001377 |
Description of YIL115C: FG-nucleoporin component of central core of the nuclear pore complex (NPC); also part of the NPC cytoplasmic filaments; contributes directly to nucleocytoplasmic transport; regulates ADP release from the ATP-dependent RNA helicase Dbp5p; forms a stable association with Nup82p, Gle2p and two other FG-nucleoporins (Nsp1p and Nup116p)[1][2][3][4][5][6][7][8][9][10][11]
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References
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- ↑ Bailer SM, et al. (2000) Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem 275(31):23540-8 SGD PMID 10801828
- ↑ Grosshans H, et al. (2001) 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 153(4):745-62 SGD PMID 11352936
- ↑ Hodge CA, et al. (1999) 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 18(20):5778-88 SGD PMID 10523319
- ↑ Lutzmann M, et al. (2005) Reconstitution of Nup157 and Nup145N into the Nup84 complex. J Biol Chem 280(18):18442-51 SGD PMID 15741174
- ↑ Noble KN, et al. (2011) 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 25(10):1065-77 SGD PMID 21576266
- ↑ Patel SS, et al. (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129(1):83-96 SGD PMID 17418788
- ↑ Rout MP, et al. (2000) The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148(4):635-51 SGD PMID 10684247
- ↑ Stage-Zimmermann T, et al. (2000) Factors affecting nuclear export of the 60S ribosomal subunit in vivo. Mol Biol Cell 11(11):3777-89 SGD PMID 11071906
- ↑ Strasser K, et al. (2000) Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J Cell Biol 150(4):695-706 SGD PMID 10952996
- ↑ Strawn LA, et al. (2004) Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol 6(3):197-206 SGD PMID 15039779
- ↑ Weirich CS, et al. (2004) 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 16(5):749-60 SGD PMID 15574330
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