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Transportin 3

TRN-SR2, TNPO3, transportin-SR, imp-12, TRN-SR, transportin 3, A TRN-SR2
The protein encoded by this gene is a nuclear import receptor for serine/arginine-rich (SR) proteins such as the splicing factors SFRS1 and SFRS2. The encoded protein has also been shown to be involved in HIV-1 infection, apparently through interaction with the HIV-1 capsid protein. Two transcript variants encoding different isoforms as well as a noncoding transcript have been found for this gene.[provided by RefSeq, Jul 2010] (from NCBI)
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Top mentioned proteins: MIP, importin, CAN, IRF5, STEP
Papers using TRN-SR2 antibodies
Characterization of the forward and reverse integration reactions of the Moloney murine leukemia virus integrase protein purified from Escherichia coli
Debyser Zeger et al., In Retrovirology, 1992
... The siRNA siTRN-SR_2 targeting the TRN-SR2 mRNA (5' UCGGCGCACAGAAAUUAUAdTdT 3') (Qiagen, The Netherlands) was previously ...
Papers on TRN-SR2
GWAS in an Amerindian ancestry population reveals novel systemic lupus erythematosus risk loci and the role of European admixture.
Jacob et al., Irapuato, Mexico. In Arthritis Rheumatol, Dec 2015
RESULTS: The IRF5-TNPO3 region showed the strongest association and largest odds ratio (OR) (rs10488631, Pgcadj = 2.61x10(-29) , OR = 2.12, 95% CI: 1.88-2.39)
HIV-1 Resistance to the Capsid-Targeting Inhibitor PF74 Results in Altered Dependence on Host Factors Required for Virus Nuclear Entry.
Aiken et al., Nashville, United States. In J Virol, Sep 2015
The mutant capsid structure was not significantly perturbed by binding of PF74; rather, the mutations inhibited capsid interactions with CPSF6 and Nup153 and altered HIV-1 dependence on these host factors and on TNPO3.
Nuclear localization signals for four distinct karyopherin-β nuclear import systems.
Chook et al., Dallas, United States. In Biochem J, Jul 2015
The present paper briefly describes the classical NLS, reviews recent literature on the PY-NLS and provides in-depth reviews of the two newly discovered classes of NLSs that bind Kap121p and Transportin-SR respectively.
A trojan horse for human immunodeficiency virus.
de Franciscis et al., Napoli, Italy. In Chem Biol, Apr 2015
In this issue of Chemistry & Biology, Zhou et al. demonstrate the possibility of effective multiple targeting of HIV infection by using a multifunctional molecule in which an anti-CCR5 receptor aptamer (G-3) is conjugated to an anti-TNPO3 siRNA.
Knockdown of the host cellular protein transportin 3 attenuates prototype foamy virus infection.
Shin et al., South Korea. In Biosci Biotechnol Biochem, 2014
Transportin 3 (TNPO3) is a member of the importin-ß superfamily proteins.
Genetic basis of limb-girdle muscular dystrophies: the 2014 update.
Savarese et al., Napoli, Italy. In Acta Myol, 2014
The dominant forms (LGMD1) are: LGMD1A (myotilin), LGMD1B (lamin A/C), LGMD1C (caveolin 3), LGMD1D (DNAJB6), LGMD1E (desmin), LGMD1F (transportin 3), LGMD1G (HNRPDL), LGMD1H (chr.
A model for cofactor use during HIV-1 reverse transcription and nuclear entry.
Towers et al., London, United Kingdom. In Curr Opin Virol, 2014
We present a model that may explain how the capsid protein has a fundamental role in the early part of the viral lifecycle by utilising cyclophilin A (CypA), cleavage and polyadenylation specificity factor-6 (CPSF6), Nup358 and TNPO3 to orchestrate a coordinated process of DNA synthesis, capsid uncoating and integration targeting that evades innate responses and promotes integration into preferred areas of chromatin.
Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant.
Serguera et al., Fontenay-aux-Roses, France. In Mol Ther Nucleic Acids, 2013
Here, we compared six HIV vectors carrying different integrases, either wild type or with different mutations (D64V, D167H, Q168A, K186Q+Q214L+Q216L, and RRK262-264AAH) shown to modify integrase enzymatic activity, oligomerization, or interaction with key cellular cofactor of HIV DNA integration as LEDGF/p75 or TNPO3.
Host and viral determinants for MxB restriction of HIV-1 infection.
Engelman et al., Boston, United States. In Retrovirology, 2013
MxB expression suppressed integration into gene-enriched regions of chromosomes, similar to affects observed previously when cells were depleted for nuclear transport factors such as transportin 3. MxB activity did not require predicted GTPase active site residues or a series of unstructured loops within the stalk domain that confer functional oligomerization to related dynamin family proteins.
Variants at multiple loci implicated in both innate and adaptive immune responses are associated with Sjögren's syndrome.
Sivils et al., Oklahoma City, United States. In Nat Genet, 2013
In addition to strong association within the human leukocyte antigen (HLA) region at 6p21 (Pmeta = 7.65 × 10(-114)), we establish associations with IRF5-TNPO3 (Pmeta = 2.73 × 10(-19)), STAT4 (Pmeta = 6.80 × 10(-15)), IL12A (Pmeta = 1.17 × 10(-10)), FAM167A-BLK (Pmeta = 4.97 × 10(-10)), DDX6-CXCR5 (Pmeta = 1.10 × 10(-8)) and TNIP1 (Pmeta = 3.30 × 10(-8)).
Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.
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.
TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core.
Diaz-Griffero et al., New York City, United States. In J Virol, 2012
TNPO3 interacts with HIV-1 gag in the cytoplasm to assist HIV-1 infection after nuclear import.
Replication of GWAS-identified systemic lupus erythematosus susceptibility genes affirms B-cell receptor pathway signalling and strengthens the role of IRF5 in disease susceptibility in a Northern European population.
Kere et al., Huddinge, Sweden. In Rheumatology (oxford), 2012
RESULTS: The strongest evidence of association was found at the IRF5-TNPO3 locus, with the most significant P-value being 2.0 × 10(-7) and an odds ratio of 1.95 (95% CI 1.51, 2.50).
The cargo-binding domain of transportin 3 is required for lentivirus nuclear import.
Landau et al., New York City, United States. In J Virol, 2011
The authors demonstrated that TNPO3 was required by several lentiviruses for nuclear import.
Pigment epithelium-derived factor (PEDF) interacts with transportin SR2, and active nuclear import is facilitated by a novel nuclear localization motif.
Worrall et al., Dublin, Ireland. In Plos One, 2010
a novel nuclear localization signal and mechanism for serpinF1 nuclear import
Inhibition of HIV-1 infection by TNPO3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus.
Luban et al., Genève, Switzerland. In Retrovirology, 2010
TNPO3 promotes HIV-1 infectivity at a step in the virus life cycle that is detectable after the preintegration complex arrives in the nucleus and capsid is the viral determinant for TNPO3 dependence.
Mutations affecting interaction of integrase with TNPO3 do not prevent HIV-1 cDNA nuclear import.
Emiliani et al., Paris, France. In Retrovirology, 2010
TNPO3 binds to a surface of monomeric HIV-1 integrase that remains exposed after tetramerization.
Variants at IRF5-TNPO3, 17q12-21 and MMEL1 are associated with primary biliary cirrhosis.
Siminovitch et al., Toronto, Canada. In Nat Genet, 2010
Combined analysis of the genome-wide association and replication datasets identified IRF5-TNPO3 (combined P = 8.66 x 10(-13)), 17q12-21 (combined P = 3.50 x 10(-13)) and MMEL1 (combined P = 3.15 x 10(-8)) as new primary biliary cirrhosis susceptibility loci.
Genome-wide meta-analyses identify three loci associated with primary biliary cirrhosis.
Seldin et al., Toronto, Canada. In Nat Genet, 2010
IRF5-TNPO3 (P = 2.8 x 10(-10), OR = 1.63) and 17q12-21 (P = 1.7 x 10(-10), OR = 1.38).
Identification of host proteins required for HIV infection through a functional genomic screen.
Elledge et al., Boston, United States. In Science, 2008
Further analysis revealed previously unknown roles for retrograde Golgi transport proteins (Rab6 and Vps53) in viral entry, a karyopherin (TNPO3) in viral integration, and the Mediator complex (Med28) in viral transcription.
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