gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Nucleoporin 50kDa

Nup50, Npap60, Npap60L
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins that functions as a soluble cofactor in importin-alpha:beta-mediated nuclear protein import. Pseudogenes of this gene are found on chromosomes 5, 6, and 14. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Nucleoporin, importin, Nup153, CAN, NUP98
Papers on Nup50
NUP50 is necessary for the survival of primordial germ cells in mouse embryos.
Lee et al., Seattle, United States. In Reproduction, Jan 2016
Nucleoporin 50 kDa (NUP50), a component of the nuclear pore complex, is highly expressed in male germ cells, but its role in germ cells is largely unknown.
Three cardiovirus Leader proteins equivalently inhibit four different nucleocytoplasmic trafficking pathways.
Palmenberg et al., Madison, United States. In Virology, Oct 2015
Recombinant Leader from encephalomyocarditis virus, Theiler׳s murine encephalomyelitis virus and Saffold virus target the same subset of Nups, including Nup62 and Nup98, but not Nup50.
Nuclear Localization of the DNA Repair Scaffold XRCC1: Uncovering the Functional Role of a Bipartite NLS.
London et al., United States. In Sci Rep, 2014
We predict that the stepwise dissociation of the NLS from Impα facilitates unloading by providing a partially complexed intermediate that is available for competitive binding by Nup50 or the Importin β binding domain.
Analysis of the initiation of nuclear pore assembly by ectopically targeting nucleoporins to chromatin.
Forbes et al., San Diego, United States. In Nucleus, 2014
Strikingly, Nup133 and Nup107 of the Nup107/160 subcomplex and Nup153 and Nup50 of the nuclear pore basket recruited a near full complement of nucleoporins to the LacO array.
Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics.
Hetzer et al., Los Angeles, United States. In Mol Biol Cell, 2014
Here we show that Nup50 is a mobile Nup with a pronounced presence both at the NPC and in the nucleoplasm that can move between these different localizations.
Structural characterization of altered nucleoporin Nup153 expression in human cells by thin-section electron microscopy.
Fahrenkrog et al., Charleroi, Belgium. In Nucleus, 2013
The nuclear basket is composed of the 3 nucleoporins Nup153, Nup50, and Tpr, but their specific role for the structural organization of this NPC substructure is, however, not well established.
Sequence-dependent structural dynamics of primate adenosine-to-inosine editing substrates.
Pinto et al., Canada. In Chembiochem, 2013
Sequence analysis of the Alu Sg elements (A-to-I RNA substrates) corresponding to the Nup50 gene in human, chimp, and rhesus reveals subtle sequence variations surrounding the edit sites.
Identification of genetic modifiers of TDP-43 neurotoxicity in Drosophila.
Tibbetts et al., Madison, United States. In Plos One, 2012
Finally, we showed that mutation of the nucleoporin Nup50 increased the lifespan of TDP-43 transgenic flies, suggesting that nuclear events contribute to TDP-43-dependent neurotoxicity.
The Nup153-Nup50 protein interface and its role in nuclear import.
Ullman et al., Salt Lake City, United States. In J Biol Chem, 2012
Interactions between Nup50 and soluble transport factors underlie the efficiency of certain nucleocytoplasmic transport pathways.
Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin α5.
Cingolani et al., Philadelphia, United States. In J Biol Chem, 2012
Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin alpha5.
Fulminant hepatic failure requiring liver transplantation in 22q13.3 deletion syndrome.
Haaf et al., Mainz, Germany. In Am J Med Genet A, 2010
--> qter; including approximately 55 genes; from NUP50 to RABL2B) and in the previous patient a 1.535 Mb deletion (22q13.32
Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import.
Yoneda et al., Suita, Japan. In Mol Biol Cell, 2010
Results suggest that Npap60L and Npap60S function differently in nuclear protein import.
Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm.
Fornerod et al., Amsterdam, Netherlands. In Cell, 2010
We analyzed genomic interactions of full-length nucleoporins Nup98, Nup50, and Nup62 and nucleoplasmic and NPC-tethered forms of Nup98.
Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Hetzer et al., Los Angeles, United States. In Cell, 2009
While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span.
Interaction of the melanocortin 2 receptor with nucleoporin 50: evidence for a novel pathway between a G-protein-coupled receptor and the nucleus.
Clark et al., London, United Kingdom. In Faseb J, 2007
Interacts with the melanocortin 2 receptor, participating in its translocation to the nucleus.
Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling.
Stewart et al., Cambridge, United Kingdom. In Embo J, 2005
findings show that the Nup50 N-terminal domain actively displaces NLSs from importin-alpha, which would be more consistent with Nup50 functioning to coordinate import complex disassembly and importin recycling
Npap60: a new player in nuclear protein import.
Moore, Houston, United States. In Trends Cell Biol, 2003
Until very recently, the vertebrate protein Npap60/Nup50 was thought merely to be a component of the nuclear pore complex (NPC).
Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import.
Macara et al., Charlottesville, United States. In Cell, 2002
We now show that Npap60 (also called Nup50), a protein previously believed to be a structural component of the NPC, is a Ran binding protein and a cofactor for importin-alpha:beta-mediated import.
share on facebooktweetadd +1mail to friends