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RAN binding protein 3

RanBP3, Ran-binding protein 3
This gene encodes a protein with a RanBD1 domain that is found in both the nucleus and cytoplasm. This protein plays a role in nuclear export as part of a heteromeric complex. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: RAN, CRM1, CAN, Smad2, ACID
Papers on RanBP3
RanBP3 Regulates Melanoma Cell Proliferation via Selective Control of Nuclear Export.
New
Wagner et al., Vienna, Austria. In J Invest Dermatol, Jan 2016
However, the role of the most characterized chromosome region maintenance 1 cofactor ran binding protein 3 (RanBP3) in cancer cell biology has never been investigated.
Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export.
New
Kehlenbach et al., Göttingen, Germany. In Cell Rep, Nov 2015
Comparative studies with RanBP3 and Nup62 shed light on specificities of CRM1-nucleoporin binding, which serves as a paradigm for transport receptor-nucleoporin interactions.
RanBP3 Regulates Melanoma Cell Proliferation via Selective Control of Nuclear Export.
New
Wagner et al., Vienna, Austria. In J Invest Dermatol, Nov 2015
However, the role of the most characterized CRM1 cofactor RanBP3 in cancer cell biology has never been investigated.
Structural insights into how Yrb2p accelerates the assembly of the Xpo1p nuclear export complex.
Matsuura et al., Nagoya, Japan. In Cell Rep, 2014
Efficient export of NES-cargoes requires Yrb2p (yeast RanBP3), a primarily nuclear protein containing nucleoporin-like phenylalanine-glycine (FG) repeats and a low-affinity Gsp1p-binding domain (RanBD).
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.
AKT activation drives the nuclear localization of CSE1L and a pro-oncogenic transcriptional activation in ovarian cancer cells.
Di Renzo et al., Torino, Italy. In Exp Cell Res, 2013
Nuclear accrual of CSE1L was associated to the nuclear accumulation of the phosphorylated Ran Binding protein 3 (RanBP3), which depended on AKT as well.
The role of Ran-binding protein 3 during influenza A virus replication.
Zhou et al., Saskatoon, Canada. In J Gen Virol, 2013
Ran-binding protein 3 (RanBP3) is a Ran-interacting protein that is best known for its role as a cofactor of CRM1-mediated cargo nuclear export.
Sphingosine kinase 1 serves as a pro-viral factor by regulating viral RNA synthesis and nuclear export of viral ribonucleoprotein complex upon influenza virus infection.
Hahm et al., Columbia, United States. In Plos One, 2012
Further, SK blockade interfered with activation of Ran-binding protein 3 (RanBP3), a cofactor of chromosome region maintenance 1 (CRM1), to inhibit CRM1-mediated nuclear export of the influenza viral ribonucleoprotein complex.
Ran and calcineurin can participate collaboratively in the regulation of spermatogenesis in scallop.
Nakatomi et al., Sapporo, Japan. In Mar Biotechnol (ny), 2012
The C-terminal region of CaNBP75 is homologous to the C-terminal region of RanBP3, a Ran-binding domain-containing protein.
Click strategies for single-molecule protein fluorescence.
Lemke et al., Heidelberg, Germany. In J Am Chem Soc, 2012
Using this optimized system, we present a biocompatible one-step dual-labeling strategy of the regulatory protein RanBP3 with full labeling position freedom.
PPM1A dephosphorylates RanBP3 to enable efficient nuclear export of Smad2 and Smad3.
Feng et al., Houston, United States. In Embo Rep, 2011
Here we report that protein phosphatase PPM1A regulates the nuclear export of Smad2/3 through targeting nuclear exporter RanBP3.
Pegylated interferon alpha targets Wnt signaling by inducing nuclear export of β-catenin.
Monga et al., Pittsburgh, United States. In J Hepatol, 2011
Peg-IFN treatment led to increased mRNA and protein expression of RanBP3, a known β-catenin nuclear export factor, in all hepatoma cells.
Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.
GeneRIF
Petosa et al., Heidelberg, Germany. In Plos One, 2010
Crystal structure of the Ran-binding domain (RBD) from RanBP3 and compare it to RBD structures from RanBP1 and RanBP2 in complex with Ran and CRM1.
Coupling of dephosphorylation and nuclear export of Smads in TGF-beta signaling.
Feng et al., Houston, United States. In Methods Mol Biol, 2009
The second step involves nuclear export of dephosphorylated Smad2/3 with the aid of nuclear protein RanBP3 to terminate Smad signaling.
Perturbation of host nuclear membrane component RanBP2 impairs the nuclear import of human immunodeficiency virus -1 preintegration complex (DNA).
Chauhan et al., Columbia, United States. In Plos One, 2009
More precisely, there was a profound decline in 2-LTR DNA copies (marker for nuclear entry of HIV DNA) and an unchanged level of viral reverse transcription in RanBP2-ablated HIV-infected cells compared to RanBP3-depleted or non-specific siRNA controls.
Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling.
GeneRIF
Feng et al., Houston, United States. In Dev Cell, 2009
RanBP3 directly recognizes dephosphorylated Smad2/3, which results from the activity of nuclear Smad phosphatases, and mediates nuclear export of Smad2/3 in a Ran-dependent manner.
Ran-binding protein 3 phosphorylation links the Ras and PI3-kinase pathways to nucleocytoplasmic transport.
GeneRIF
Blenis et al., Boston, United States. In Mol Cell, 2008
RANBP3 phosphorylation links the Ras and PI3-kinase pathways to nucleocytoplasmic transport.
A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein.
GeneRIF
Shida et al., Sapporo, Japan. In Mol Cell Biol, 2003
A multifunctional domain in CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein.
Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor.
GeneRIF
Macara et al., Charlottesville, United States. In J Biol Chem, 2002
RanBP3 stimulates export by enhancing the affinity of Crm1 for Ran-GTP and cargo.
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