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RAN binding protein 1

RanBP1, Ran-binding protein 1, YRB1, CST20, Yrb1p
Ran/TC4-binding protein, RanBP1, interacts specifically with GTP-charged RAN. RANBP1 encodes a 23-kD protein that binds to RAN complexed with GTP but not GDP. RANBP1 does not activate GTPase activity of RAN but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). The RANBP1 cDNA encodes a 201-amino acid protein that is 92% similar to its mouse homolog. In both mammalian cells and in yeast, RANBP1 acts as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: RAN, CAN, RCC1, importin, RanGAP1
Papers on RanBP1
The Role of mGluR Copy Number Variation in Genetic and Environmental Forms of Syndromic Autism Spectrum Disorder.
Hakonarson et al., Seattle, United States. In Sci Rep, Dec 2015
A comparison cohort with 22q11DS (n = 25 with ASD, n = 50 without ASD), all haploinsufficient for mGluR network gene RANBP1, were evaluated for "second mGluR hits".
Ethanol Attenuates Histiotrophic Nutrition Pathways and Alters the Intracellular Redox Environment and Thiol Proteome during Rat Organogenesis.
Harris et al., Ann Arbor, United States. In Toxicol Sci, Oct 2015
Decreased concentrations for specific proteins from cytoskeletal dynamics and endocytosis pathways (α-actinin, α-tubulin, cubilin, and actin-related protein 2); nuclear translocation (Ran and RanBP1); and maintenance of receptor-mediated endocytosis (cubilin) were observed.
Increased cathepsin D protein expression is a biomarker for osteosarcomas, pulmonary metastases and other bone malignancies.
Habermann et al., Lübeck, Germany. In Oncotarget, Jul 2015
Ran/TC4-binding protein (RANBP1) and Cathepsin D (CTSD) were further validated by Western Blot in cell lines while the latter one showed higher expression differences also in cytospins and in clinical samples using tissue microarrays comprising osteosarcomas, metastases, other bone malignancies, and control tissues.
Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport.
Rogelj et al., Ljubljana, Slovenia. In Neuroscience, Jun 2015
We show that Ran-binding protein 1 (RanBP1), DNA methyltransferase 3 alpha (Dnmt3a) and chromogranin B (CgB) are downregulated upon TDP-43 knockdown.
Novel reversible selective inhibitor of CRM1 for targeted therapy in ovarian cancer.
Niu et al., Xuzhou, China. In J Ovarian Res, 2014
The subcellular localization of RanBP1 was analyzed by immunofluorescence microscopy assay.
Identification and Evaluation of Reference Genes for Accurate Transcription Normalization in Safflower under Different Experimental Conditions.
Wu et al., Chengdu, China. In Plos One, 2014
These genes were ABCS, 60SRPL10, RANBP1, UBCL, MFC, UBCE2, EIF5A, COA, EF1-β, EF1, GAPDH, ATPS, MBF1, GTPB and GST.
Atomic basis of CRM1-cargo recognition, release and inhibition.
Chook et al., Dallas, United States. In Semin Cancer Biol, 2014
Numerous atomic resolution CRM1 structures are now available, explaining how the exporter recognizes nuclear export signals in its cargos, how RanGTP and cargo bind with positive cooperativity, how RanBP1 causes release of export cargos in the cytoplasm and how diverse inhibitors such as Leptomycin B and the new KPT-SINE compounds block nuclear export.
Phosphorylation of Ran-binding protein-1 by Polo-like kinase-1 is required for interaction with Ran and early mitotic progression.
Jang et al., Ch'ŏnan, South Korea. In J Biol Chem, 2011
in vitro and in vivo phosphorylation of RanBP1 by Plk1 as well as the importance of phosphorylation of RanBP1 in the interaction between Plk1 and Ran during early mitosis, is demonstrated.
Mice lacking Ran binding protein 1 are viable and show male infertility.
Yoneda et al., Suita, Japan. In Febs Lett, 2011
The dramatic decrease in "RanBP" activity impairs germ cell viability and affects spermatogenesis decisively in RanBP1-knockout mice.
Association of RANBP1 haplotype with smooth pursuit eye movement abnormality.
Woo et al., Seoul, South Korea. In Am J Med Genet B Neuropsychiatr Genet, 2011
RANBP1 on 22q11.21 locus might be causally related to the smooth pursuit eye movement abnormality rather than the development of schizophrenia.
Nuclear reformation after mitosis requires downregulation of the Ran GTPase effector RanBP1 in mammalian cells.
Lavia et al., Roma, Italy. In Chromosoma, 2010
Downregulation of the Ran GTPase effector RanBP1 is required for nuclear reorganisation.
An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1.
Matsuura et al., Nagoya, Japan. In Embo J, 2010
The structure shows that on association of Ran-binding domain (RanBD) of RanBP1 with CRM1:NES-cargo:RanGTP complex, RanBD and the C-terminal acidic tail of Ran induce a large movement of the intra-HEAT9 loop of CRM1.
The design of Förster (fluorescence) resonance energy transfer (FRET)-based molecular sensors for Ran GTPase.
Soderholm et al., Bethesda, United States. In Methods, 2010
Finally, we review the design and optimization of monomolecular FRET sensors that monitor the RanGTP-RanBP1 interaction, and of sensors detecting the RanGTP-regulated importin beta cargo release.
Ran on tracks--cytoplasmic roles for a nuclear regulator.
Fainzilber et al., Israel. In J Cell Sci, 2009
Striking findings suggest that the guanine-nucleotide state of Ran can be regulated by local translation of the Ran-binding protein RanBP1 in axons, and that an additional Ran-binding protein, RanBP10, can act as a microtubule-binding cytoplasmic guanine-nucleotide exchange factor for Ran (RanGEF) in megakaryocytes.
Temporal and spatial control of nucleophosmin by the Ran-Crm1 complex in centrosome duplication.
Wang et al., Bethesda, United States. In Nat Cell Biol, 2005
NPM contains a functional nuclear export signal (NES) that is responsible for both its nucleocytoplasmic shuttling and its association with centrosomes, which are Ran-Crm1-dependent as they are sensitive to Crm1-specific nuclear export inhibition, either by leptomycin B (LMB) or by the expression of a Ran-binding protein, RanBP1.
RanGAP mediates GTP hydrolysis without an arginine finger.
Vetter et al., Dortmund, Germany. In Nature, 2002
Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic.
A Ran-independent pathway for export of spliced mRNA.
Reed et al., Boston, United States. In Nat Cell Biol, 2001
The activity of RanGAP is increased by RanBP1, which also promotes disassembly of RanGTP-cargo-transporter complexes.
Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp.
Blobel et al., New York City, United States. In Nature, 1999
This provides a structural basis for the specificity of the karyopherin-beta family for the GTP-bound state of Ran, as well as a rationale for interactions of the karyopherin-Ran complex with the regulatory proteins ranGAP, ranGEF and ranBP1.
Distinct nuclear import and export pathways mediated by members of the karyopherin beta family.
Moroianu, Boston, United States. In J Cell Biochem, 1998
The GTPase Ran; the RanGDP binding protein, p10; and the RanGTP binding protein, RanBP1 are involved in translocation of the docked NLS-protein into the nucleus.
Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor.
Görlich et al., Heidelberg, Germany. In Cell, 1997
Importin alpha is released from this complex in the cytoplasm by the combined action of RanBP1 and RanGAP1.
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