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Human AGO2 Protein expressed in Baculovirus infected Insect Cells - ABIN2003923
Rand, Petersen, Du, Wang: Argonaute2 cleaves the anti-guide strand of siRNA during RISC activation. in Cell 2005
Show all 6 Pubmed References
Human AGO2 Protein expressed in Wheat germ - ABIN1352524
Rawlings, Krishnan, Walter: Viral RNAi suppressor reversibly binds siRNA to outcompete Dicer and RISC via multiple turnover. in Journal of molecular biology 2011
Mouse (Murine) AGO2 Protein expressed in Baculovirus infected Insect Cells - ABIN2008152
Qi, Ongusaha, Myllyharju, Cheng, Pakkanen, Shi, Lee, Peng, Shi: Prolyl 4-hydroxylation regulates Argonaute 2 stability. in Nature 2008
Show all 5 Pubmed References
Data show that Argonaute family protein AGO2 and AGO3 (show EIF2C3 Proteins) were important for abscisic acid (ABA)-mediated resistance.
AGO1, AGO2 and AGO10 promoted anti-TuMV defense in a modular way in various organs, with AGO2 providing a prominent antiviral role in leaves. AGO5, AGO7 and AGO10 had minor effects in leaves.
Base pairing at the 15th nucleotide of a miRNA duplex is important for miRNA sorting in both Arabidopsis AGO1 (show EIF2C1 Proteins) and AGO2. AGO2 favours miRNA duplexes with no middle mismatches.
Complementation analyses in ago mutant plants revealed that the catalytic residues of AGO1, AGO2, and AGO7 are required to restore the defects of Arabidopsis ago1-25, ago2-1, and zip-1 (AGO7-defective) mutants, respectively.
AGO2 and HEN1 (show HENMT1 Proteins) participate in the DCL2-mediated antiviral defense to ensure the survival of Turnip crinkle virus-infected plants at high temperature.
This study reveals that miR408, which has a 5'A, regulates its target Plantacyanin through either AGO1 (show EIF2C1 Proteins) or AGO2.
AGO1 (show EIF2C1 Proteins) and AGO2 are involved in defense against mutant of Cucumber mosaic virus, which act downstream the biogenesis of viral secondary siRNAs in a nonredundant and cooperative manner.
Results show that AGO2-bound small RNA miR393b( *) targets a Golgi-localized SNARE (show NAPA Proteins) gene, MEMB12.
second layer is activated when the first layer is suppressed because AGO2 is repressed by AGO1 (show EIF2C1 Proteins) via miR403
Here we show that biotin-labelled miR (show MLXIP Proteins)-34a can be loaded to AGO2, and AGO2 immunoprecipitation can pulldown biotinylated miR (show MLXIP Proteins)-34a (Bio-miR (show MLXIP Proteins) pulldown). RNA-sequencing (RNA-seq) of the Bio-miR (show MLXIP Proteins) pulldown RNAs efficiently identified miR (show MLXIP Proteins)-34a mRNA targets, which could be verified with luciferase assays
extracellular vesicles are efficiently internalized by endothelial cells, where the miRNA-Argonaute 2 complexes modulate target gene expression and barrier properties.
CASC7 expression was significantly decreased in colorectal cancer (CRC (show CALR Proteins)) tissues and CRC (show CALR Proteins) cell lines; CASC7 overexpression could inhibit cell viability, migration and invasion, and promote apoptosis in CRC (show CALR Proteins) cells
A dual role of the association between AGO2 and ERbeta (show ESR2 Proteins) in luminal-like breast cancer cells in the nucleus and the cytoplasm, for the regulation of gene expression at both the transcriptional and post-transcriptional level.
Decreased argonaute 2 and dicer1 (show DICER1 Proteins) in peripheral blood mononuclear cells from War Veterans with post-traumatic stress disorder leads to diminished miRNA resulting in elevated inflammation.
Phosphorylation of AGO2 at Ser (show SIGLEC1 Proteins) 387 by Akt3 (show AKT3 Proteins) induces LIMD1 (show LIMD1 Proteins) binding, which in turn enables AGO2 to interact with TNRC6A and downstream effector DDX6 (show DDX6 Proteins).
AGO2-mediated cleavage of targets is more common than previously thought. This may explain the vital role of endonuclease activity in controlling miRNA-mediated gene regulation.
Data show that neuropilin 1 (NRP1 (show NRP1 Proteins)) binds extracellular AGO2 (carrying miRNA or not), and internalizes AGO2/miRNA complexes.
We found a much larger number of microparticles (MPs) results demonstrate that normal RBCs (show SSU1 Proteins) display an innate ability to resist infection by P. falciparum parasite by releasing Ago2-miRNA complexes via microparticles (MPs)into infected RBCs (show SSU1 Proteins); data suggest that, through release of MPs, mature RBCs (show SSU1 Proteins) present an innate resistance to malaria infection
we describe these two methodologies that we recently used to select a specific compound able to interfere with the AGO2 functional activity and able to improve the retinoic acid-dependent myeloid differentiation of leukemic cells.
Here, we show that partial loss of either APOBEC1 complementation factor (A1CF (show A1CF Proteins)), the RNA-binding cofactor of APOBEC1 (show APOBEC1 Proteins) in RNA editing, or Argonaute 2 (AGO2), a key factor in the biogenesis of certain noncoding RNAs, modulates risk for TGCTs and testicular abnormalities in both parent-of-origin and conventional genetic manners.
This identified Ago2 as a key determinant of quiescence exit in Hematopoietic stem cells.
miR (show MLXIP Proteins)-9, along with Argonaute proteins (Agos), is localized to the nucleus of quiescent neural stem cells, and manipulating their nuclear/cytoplasmic ratio impacts quiescence.
We propose that RISC-mediated inhibition of specific sets of chromatin regulators is a primary mechanism for preserving embryonic stem cell pluripotency while inhibiting the onset of embryonic developmental programs
Increased AGO2 was detected in autophagy-deficient ATG5 (show ATG5 Proteins)-/- and ATG16 (show ATG16L1 Proteins)-/- mouse embryonic fibroblast cells. Chemical agents and VacA toxin, which disrupt autophagy, increased AGO2 expression in MEFs, epithelial cells lines, and human monocytes.
DIS3L2 (show DIS3L2 Proteins) interacts with Ago2 and governs target RNA-directed miRNA degradation.
Results from the liver show that, siRNA targets 3'UTR and the coding sequence (CDs (show ABHD5 Proteins)) of endogenous genes in the presence Ago2 but in its absence, only 3'UTR-targeted siRNA-mediated knockdown are active with the help of Ago1 (show EIF2C1 Proteins) and Ago3 (show EIF2C3 Proteins).
Roquin (show RC3H1 Proteins) also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR (show MLXIP Proteins)-146a, a microRNA that targets Icos (show ICOS Proteins) mRNA.
Target mRNAs induce tailing and trimming on Ago2-loaded miRNAs.
Results provide evidence for an Ago2-interaction network participating in dosage compensation in drosophila.
findings reveal coordination of AGO2 and LaminB function to dictate genome architecture and thereby regulate gene expression
Molecular evolution of AGO2 glutamine-rich repeat region
Mutation of T1149 or R1158 in the conserved PIWI (show PIWIL1 Proteins) domain causes AGO2 protein instability, but only T1149 affects RNAi activity. Mass spec analysis shows that several proteasome components co-purify with both wildtype and mutant AGO2, and knockdown of two proteasome pathway components results in AGO2 protein accumulation.
We speculate that the repeated evolution of testis specificity in obscura group Ago2 genes, combined with their dynamic turnover and strong signatures of adaptive evolution, may be associated with highly derived roles in the suppression of transposable elements or meiotic drive
We find there are large differences in evolutionary rates and gene turnover between pathways, and that paralogs of Ago2, Ago3, and Piwi/Aub show contrasting rates of evolution after duplication.
Study shows that the Cricket Paralysis virus suppressor of RNA silencing, CrPV-1A but not B2 strongly interfere with the Ago-2-dependent miRNA silencing in Drosophila.
siRNA biogenesis does not stabilize AGO2 in Drosophila.
The results of this study found that mutations in Drosophila Argonaute 2 (Ago2) resulted in exacerbated transposon expression in the brain, progressive and age-dependent memory impairment, and shortened lifespan
analysis of regulation of Argonaute (show EIF2C1 Proteins) slicer activity by guide RNA 3' end interactions with the N-terminal lobe
This gene encodes a member of the Argonaute family of proteins which play a role in RNA interference. The encoded protein is highly basic, and contains a PAZ domain and a PIWI domain. It may interact with dicer1 and play a role in short-interfering-RNA-mediated gene silencing. Multiple transcript variants encoding different isoforms have been found for this gene.
eukaryotic translation initiation factor 2C, 2
, protein argonaute-2-like
, PAZ Piwi domain protein
, argonaute 2
, eIF-2C 2
, eIF2C 2
, protein argonaute-2
, protein slicer
, golgi ER protein 95 kDa
, Protein slicer
, eukaryotic translation initiation factor 2C, 1
, Piwi/Argonaute family protein meIF2C2
, argonaute RISC catalytic component 2
, eukaryotic translation initiation factor 2C 2
, Eukaryotic translation initiation factor 2C 2
, translation initiation factor eIF2C