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Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Additionally we are shipping Tankyrase, TRF1-Interacting Ankyrin-Related ADP-Ribose Polymerase Antibodies (82) and Tankyrase, TRF1-Interacting Ankyrin-Related ADP-Ribose Polymerase Kits (16) and many more products for this protein.
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Tank1/Tank2 (show TNKS2 Proteins) inhibition aggravates kidney injury in the absence of CD2AP (show Cd2ap Proteins).
Finally, through functional validation, we uncovered a role for TNKS/2 (show TNKS2 Proteins) in peroxisome homeostasis and determined that this function is independent of TNKS enzyme activities.
The data indicate that the sterile alpha motif domain polymerization is critical for TNKS1 catalytic activity and allows TNKS1 to efficiently access cytoplasmic signaling complexes.
Polymerization is required for Tankyrase to drive beta-catenin (show CTNNB1 Proteins)-dependent transcription. The polymeric state supports PARP activity and allows Tankyrase to effectively access destruction complexes through enabling avidity-dependent AXIN (show AXIN1 Proteins) binding.
In late S/G2 (show STRN3 Proteins) phase, the DNA damage-responsive E3 ligase RNF8 (show RNF8 Proteins) conjugates K63-linked ubiquitin chains to tankyrase 1, while in G1 phase such ubiquitin chains are removed by BRISC, an ABRO1 (show FAM175B Proteins)/BRCC36 (show BRCC3 Proteins)-containing deubiquitinase complex.
These structural insights will be invaluable for the functional and biophysical characterization of TNKS1/2, including the role of TNKS oligomerization in protein poly(ADP-ribosyl)ation (PARylation) and PARylation-dependent ubiquitylation.
Results describe the structure of three consecutive TNKS- ankyrin repeat clusters (ARCs). Binding analysis indicates specific ARC (show NOL3 Proteins) pairs engage bivalent binding partner Axin1 (show AXIN1 Proteins), and that both rigid and flexible ARC (show NOL3 Proteins) connections form an adaptable TNKS binding platform.
we show for the first time that Tankyrase 1 inhibitior XAV939 was able to significantly increase the apoptosis induced by 5-FU/DDP, accompanied by the protein expression level alternation of b-catenin, Axin and CSC markers in colon cancer cells.
Data show that poly(ADP-ribose) polymerase (PARP (show PARP1 Proteins)) enzyme Tankyrase (TNKS) inhibition in colon cancer cells decreases beta-catenin (show CTNNB1 Proteins) signaling at the level of both Axin (show AXIN1 Proteins) and APC2.
HCMV modulates the activity of TNKS to induce Axin1 (show AXIN1 Proteins), resulting in inhibition of the beta-catenin (show CTNNB1 Proteins) pathway.
Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1 (show PARP1 Proteins)/2 and tankyrase 1/2 inhibitor which has the advantage of targeting Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling addicted tumors.
analyses also reveal the structural basis for TNKS substrate recruitment, and shed light on the overall structure of TNKS that should help in developing specific inhibitors of Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling
Data show that Tnks1 and 2 are broadly expressed during mouse development and are essential during kidney and lung development. In the kidney, blockage of tankyrase activity phenocopies the effect of blocking production of all Wnt (show WNT2 Proteins) ligands.
Collectively, our data suggest that GSK3 contributes to mitotic tankyrase phosphorylation.
insulin (show INS Proteins)-stimulated insulin-responsive aminopeptidase (show LNPEP Proteins) translocation remained intact despite substantial GLUT4 (show SLC2A4 Proteins) knockdown
tankyrase1 is a poly(ADP-ribose) polymerase (show PARP1 Proteins) with roles in telomere length control by the TRF1 (show TERF1 Proteins) component of the shelterin complex
Tankyrase 1 is essential but redundant for mouse embryonic development
Tankyrase-deficient mice exhibit increases in energy expenditure, fatty acid oxidation, and insulin (show INS Proteins)-stimulated glucose utilization.
Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.
, tankyrase 1
, ADP-ribosyltransferase diphtheria toxin-like 5
, TRF1-interacting ankyrin-related ADP-ribose polymerase
, poly [ADP-ribose] polymerase 5A
, tankyrase I
, TRF1-interacting ankyrin-related ADP-ribose polymerase 1