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Nucleoporin 153kDa

Nup153
Nuclear pore complexes are extremely elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are pore complex-specific glycoproteins characterized by cytoplasmically oriented O-linked N-acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG. The protein encoded by this gene has three distinct domains: a N-terminal region within which a pore targeting domain has been identified, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Nucleoporin, CAN, NUP98, SET, STEP
Papers on Nup153
Stage-dependent remodeling of the nuclear envelope and lamina during rabbit early embryonic development.
New
Zakhartchenko et al., Martinsried, Germany. In J Reprod Dev, Jan 2016
UNASSIGNED: Utilizing 3D structured illumination microscopy, we investigated the quality and quantity of nuclear invaginations and the distribution of nuclear pores during rabbit early embryonic development and identified the exact time point of nucleoporin 153 (NUP153) association with chromatin during mitosis.
Spermatid head elongation with normal nuclear shaping requires ADP-ribosyltransferase PARP11 (ARTD11) in mice.
New
Meyer et al., Konstanz, Germany. In Biol Reprod, Mar 2015
In transfected somatic cells, PARP11 colocalizes with nuclear pore components, such as NUP153.
Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.
Yeager et al., Charlottesville, United States. In Proc Natl Acad Sci U S A, 2015
Here we report biochemical experiments showing that PF-3450074 (PF74), a drug that inhibits HIV-1 infection, as well as host proteins cleavage and polyadenylation specific factor 6 (CPSF6) and nucleoporin 153 kDa (NUP153), bind to the CA hexamer with at least 10-fold higher affinities compared with nonassembled CA or isolated CA domains.
The Small Molecule R-(-)-β-O-Methylsynephrine Binds to Nucleoporin 153 kDa and Inhibits Angiogenesis.
Kwon et al., Seoul, South Korea. In Int J Biol Sci, 2014
To elucidate the underlying mechanisms responsible for the antiangiogenic activity of OMe-Syn, we used phage display cloning to isolate potential OMe-Syn binding proteins from human cDNA libraries and identified nucleoporin 153 kDa (NUP153) as a primary binding partner of OMe-Syn.
Remodeling of the Nuclear Envelope and Lamina during Bovine Preimplantation Development and Its Functional Implications.
Cremer et al., Martinsried, Germany. In Plos One, 2014
In addition, a deposit of extranuclear clusters of NUP153 (a marker for NPCs) without associated lamin B was frequently observed from the zygote stage up to MGA.
Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.
James et al., Cambridge, United Kingdom. In Plos Pathog, 2014
Here we show that a multi-subunit interface formed exclusively within CA hexamers mediates binding to linear epitopes within cellular cofactors NUP153 and CPSF6, and is competed for by the antiretroviral compounds PF74 and BI-2.
Positive selection of primate genes that promote HIV-1 replication.
Sawyer et al., Austin, United States. In Virology, 2014
Some of these genes (CD4, NUP153, RANBP2/NUP358) have been characterized with respect to the HIV lifecycle, while others (ANKRD30A/NY-BR-1 and MAP4) remain relatively uncharacterized.
Functional networks of nucleocytoplasmic transport-related genes differentiate ischemic and dilated cardiomyopathies. A new therapeutic opportunity.
Rivera et al., Valencia, Spain. In Plos One, 2013
DDX3X, KPNA2, and PTK2B were related to ICM, while SMURF2, NUP153, IPO5, RANBP3, NOXA1, and RHOJ were involved in DCM pathogenesis.
Serum bilirubin concentration in healthy adult North-Europeans is strictly controlled by the UGT1A1 TA-repeat variants.
Urdal et al., Oslo, Norway. In Plos One, 2013
The individuals were examined for the TA6>TA7 variant in the UGT1A1 promoter and 7 tag-SNPs in an extended promoter region of UGT1A1 (haplotype analysis) and in selected SNPs in candidate genes (SLCO1B3, ABCC2 and NUP153).
Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.
Review
Engelman et al., Boston, United States. In Viruses, 2013
Furthermore, capsid was found to be responsible for the viral requirement of various nuclear transport proteins, including transportin 3 and nucleoporins NUP153 and NUP358, during infection.
Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.
Engelman et al., Boston, United States. In Plos Pathog, 2012
We previously showed that the viral capsid (CA) protein mediated the dependency on cellular nucleoporin (NUP) 153 during HIV-1 infection, and now demonstrate a direct interaction between the CA N-terminal domain and the phenylalanine-glycine (FG)-repeat enriched NUP153 C-terminal domain (NUP153(C)).
Integrative genomic and functional profiling of the pancreatic cancer genome.
Pollack et al., Stanford, United States. In Bmc Genomics, 2012
Most notably, the analysis also revealed novel possible oncogenic functions of nucleoporin NUP153 (ostensibly by modulating TGFβ signaling) and Kruppel-like transcription factor KLF5 in pancreatic cancer.
The interaction between importin-α and Nup153 promotes importin-α/β-mediated nuclear import.
GeneRIF
Yoneda et al., Suita, Japan. In Traffic, 2012
Nup153 binds to importin alpha
Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1.
GeneRIF
Bartek et al., Praha, Czech Republic. In Cell Death Differ, 2012
Data show that the C-terminal part of NUP153 is required for effective 53BP1 nuclear import, and that 53BP1 is imported to the nucleus through the NUP153-importin-beta interplay.
Specific armadillo repeat sequences facilitate β-catenin nuclear transport in live cells via direct binding to nucleoporins Nup62, Nup153, and RanBP2/Nup358.
GeneRIF
Henderson et al., Sydney, Australia. In J Biol Chem, 2012
Specific armadillo repeat sequences facilitate beta-catenin nuclear transport in live cells via direct binding to nucleoporins Nup62, Nup153, and RanBP2/Nup358
A genome-wide search for non-UGT1A1 markers associated with unconjugated bilirubin level reveals significant association with a polymorphic marker near a gene of the nucleoporin family.
GeneRIF
Majumder et al., Calcutta, India. In Ann Hum Genet, 2012
A significant association of a polymorphic marker (rs2328136) near the NUP153 gene (which produces a 153 kDa nucleoporin) was obtained
Distinct association of the nuclear pore protein Nup153 with A- and B-type lamins.
GeneRIF
Fahrenkrog et al., Basel, Switzerland. In Nucleus, 2011
The N-terminal domain of Nup153 and its C terminus associate with the Ig-fold domain of A- and B-type lamins.
Flexible structures and ligand interactions of tandem repeats consisting of proline, glycine, asparagine, serine, and/or threonine rich oligopeptides in proteins.
Review
Kretsinger et al., Sapporo, Japan. In Curr Protein Pept Sci, 2008
The tandem repeats in tropoelastin, flagelliform silk, wheat HMW glutenin, abductin, titin, and human nucleoporin, nup153, are responsible for elastomeric properties.
A giant nucleopore protein that binds Ran/TC4.
Impact
Aebi et al., Fukuoka, Japan. In Nature, 1995
This giant protein comprises an amino-terminal 700-residue leucine-rich region, four RanBP1-homologous (refs 9, 10) domains, eight zinc-finger motifs similar to those of NUP153 (refs 11, 12), and a carboxy terminus with high homology to cyclophilin.
A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm.
Impact
Blobel et al., New York City, United States. In Cell, 1993
We have molecularly cloned and sequenced a cDNA for a rat liver nucleoporin with a molecular mass of 152.8 kd, termed nup153, that shares a repetitive degenerate pentapeptide motif with a subgroup of nucleoporins of yeast and vertebrates.
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