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NUP53 Nup53p

Nup53, Nup53p
This gene encodes a member of the nucleoporin family. The protein is localized to the nuclear rim and is part of the nuclear pore complex (NPC). All molecules entering or leaving the nucleus either diffuse through or are actively transported by the NPC. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Nucleoporin, Mlp1, CAN, Nup133, NUP120
Papers on Nup53
Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p.
Matsuura et al., Nagoya, Japan. In J Mol Biol, 2013
To understand the structural basis for Kap121p-mediated nuclear import and its unique regulatory mechanism during mitosis, we determined crystal structures of Kap121p in isolation and also in complex with either its import cargoes or nucleoporin Nup53p or RanGTP.
Improved native isolation of endogenous Protein A-tagged protein complexes.
Rout et al., New York City, United States. In Biotechniques, 2013
We tested this reagent for the elution of tagged endogenous protein complexes from yeast (Nup53p/Nup170p dimer; Nup1p/Kap95p/Kap60p trimer; pentameric GINS complex) and bacteria (RNAP holoenzyme).
Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance.
Weis et al., Berkeley, United States. In J Cell Biol, 2009
Ndc1 forms a distinct complex with the transmembrane proteins Pom152 and Pom34 and two alternative complexes with the soluble nucleoporins Nup53 and Nup59, which in turn bind to Nup170 and Nup157.
Nup53 is required for nuclear envelope and nuclear pore complex assembly.
Mattaj et al., Edmonton, Canada. In Mol Biol Cell, 2008
defined regions of Nup53 that bind to neighboring nucleoporins as well as those domains that target Nup53 to the nuclear pore complex.
Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction.
Marks et al., Durham, United States. In Plos One, 2007
These genes delineate a metabolic mRNA pathway that temporally links transcription elongation (SPT4, SPT5, CTK1, DEF1) to nucleopore-mediated mRNA export (ASM4, MLP1, MLP2, NUP2, NUP53, NUP120, NUP133, NUP170, NUP188, POM34) and cytoplasmic mRNA decay at P-bodies (CCR4, DHH1).
Nup53p is a target of two mitotic kinases, Cdk1p and Hrr25p.
Wozniak et al., Edmonton, Canada. In Traffic, 2007
NUP53 is a target of CDK1 and HRR25.
The crystal structure of mouse Nup35 reveals atypical RNP motifs and novel homodimerization of the RRM domain.
Yokoyama et al., Yokohama, Japan. In J Mol Biol, 2006
The vertebrate nuclear pore protein Nup35, the ortholog of Saccharomyces cerevisiae Nup53p, is suggested to interact with the NE membrane and to be required for nuclear morphology.
Interactions between Mad1p and the nuclear transport machinery in the yeast Saccharomyces cerevisiae.
Wozniak et al., Edmonton, Canada. In Mol Biol Cell, 2005
At the NPC, Mad1p interacts with Nup53p and a presumed Nup60p/Mlp1p/Mlp2p complex through two coiled coil regions within its N terminus.
Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex.
Wozniak et al., Edmonton, Canada. In Mol Biol Cell, 2005
We have investigated the function of the human nucleoporin Nup53, the ortholog of Saccharomyces cerevisiae Nup53p.
Identification of genes encoding putative nucleoporins and transport factors in the fission yeast Schizosaccharomyces pombe: a deletion analysis.
Balasundaram et al., Singapore, Singapore. In Yeast, 2004
encode putative nucleoporins with low similarity to the S. cerevisiae nucleoporins NUP2p, NUP53p and NUP133p, respectively.
Cell cycle regulated transport controlled by alterations in the nuclear pore complex.
Wozniak et al., Edmonton, Canada. In Cell, 2004
These changes allow a transport inhibitory nucleoporin, Nup53p, to bind the karyopherin Kap121p specifically during mitosis, slowing its movement through the NPC and inducing cargo release.
The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint.
Wozniak et al., Edmonton, Canada. In J Cell Biol, 2003
There they are associated with a subcomplex of nucleoporins containing Nup53p, Nup170p, and Nup157p.
Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes.
Wozniak et al., Edmonton, Canada. In J Cell Biol, 2002
We show that the yeast karyopherin Kap121p functions in the targeting and assembly of the nucleoporin Nup53p into NPCs by recognizing a nuclear localization signal (NLS) in Nup53p.
A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope.
Wozniak et al., Edmonton, Canada. In J Cell Biol, 2001
By altering the expression of a single nucleoporin gene, NUP53, we showed that the overproduction of Nup53p altered nuclear transport and had a profound effect on the structure of the nuclear membrane.
The yeast nucleoporin Nup53p specifically interacts with Nic96p and is directly involved in nuclear protein import.
Aebi et al., Basel, Switzerland. In Mol Biol Cell, 2000
By doing so, we identified the yeast nucleoporin Nup53p, which also exhibits multiple locations within the yeast NPC and colocalizes with Nic96p in all its locations.
Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p.
Wozniak et al., Edmonton, Canada. In J Cell Biol, 1999
The physiological relevance of the interaction between Nup53p and Kap121p was further underscored by the observation that NUP53 mutations alter the subcellular distribution of Kap121p and the Kap121p- mediated import of a ribosomal L25 reporter protein.
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