NUP159/YIL115C Literature Guide Help

Other names published for NUP159: NUP158, RAT7, YIL115C

NUP159 - Cellular Location (23)

ReferenceOther Genes Addressed
Steinberg G, et al.  (2012) Motor-driven motility of fungal nuclear pores organizes chromosomes and fosters nucleocytoplasmic transport. J Cell Biol 198(3):343-55
Yoshida K, et al.  (2011) 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 108(40):16571-6
Chadrin A, et al.  (2010) Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution. J Cell Biol 189(5):795-811
Flemming D, et al.  (2009) Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores. J Cell Biol 185(3):387-95
Makio T, et al.  (2009) The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly. J Cell Biol 185(3):459-73
Alber F, et al.  (2007) Determining the architectures of macromolecular assemblies. Nature 450(7170):683-94
Alber F, et al.  (2007) The molecular architecture of the nuclear pore complex. Nature 450(7170):695-701
Patel SS, et al.  (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129(1):83-96
Stelter P, et al.  (2007) Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol 9(7):788-96
Madrid AS, et al.  (2006) The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function. J Cell Biol 173(3):361-71
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
Bailer SM, et al.  (2000) Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem 275(31):23540-8
Ho AK, et al.  (2000) Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol Cell Biol 20(15):5736-48
Rout MP, et al.  (2000) The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148(4):635-51
Schmitt C, et al.  (1999) 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 18(15):4332-47
Belgareh N, et al.  (1998) Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell 9(12):3475-92
Bucci M and Wente SR  (1998) A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly. Mol Biol Cell 9(9):2439-61
Hurwitz ME, et al.  (1998) Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex. Proc Natl Acad Sci U S A 95(19):11241-5
Del Priore V, et al.  (1997) A structure/function analysis of Rat7p/Nup159p, an essential nucleoporin of Saccharomyces cerevisiae. J Cell Sci 110 ( Pt 23):2987-99
Winey M, et al.  (1997) Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes. Mol Biol Cell 8(11):2119-32
Del Priore V, et al.  (1996) 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 7(10):1601-21
Gorsch LC, et al.  (1995) 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 129(4):939-55
Kraemer DM, et al.  (1995) The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate. J Biol Chem 270(32):19017-21