Biology:Tankyrase
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Short description: Enzyme
Tankyrase, also known as tankyrase 1, is an enzyme that in humans is encoded by the TNKS gene.[1][2][3] It inhibits the binding of TERF1 to telomeric DNA.[4] Tankyrase attracts substantial interest in cancer research through its interaction with AXIN1 and AXIN2, which are negative regulators of pro-oncogenic β-catenin signaling. Importantly, activity in the β-catenin destruction complex can be increased by tankyrase inhibitors and thus such inhibitors are a potential therapeutic option to reduce the growth of β-catenin-dependent cancers.[5]
Description[6]
Tankyrase-1 is a 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 (PARylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity.[7]
Protein interactions
TNKS has been shown to interact with:
References
- ↑ 1.0 1.1 "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres". Science 282 (5393): 1484–7. Dec 1998. doi:10.1126/science.282.5393.1484. PMID 9822378.
- ↑ "Chromosomal mapping of the tankyrase gene in human and mouse". Genomics 57 (2): 320–1. May 1999. doi:10.1006/geno.1999.5771. PMID 10198177.
- ↑ "Entrez Gene: TNKS tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8658.
- ↑ Cook, B. D.; Dynek, J. N.; Chang, W.; Shostak, G.; Smith, S. (1 January 2002). "Role for the Related Poly(ADP-Ribose) Polymerases Tankyrase 1 and 2 at Human Telomeres". Molecular and Cellular Biology 22 (1): 332–342. doi:10.1128/MCB.22.1.332-342.2002. PMID 11739745.
- ↑ "Evaluation of AXIN1 and AXIN2 as targets of tankyrase inhibition in hepatocellular carcinoma cell lines". Scientific Reports 11 (1): 7470. April 2021. doi:10.1038/s41598-021-87091-4. PMID 33811251. Bibcode: 2021NatSR..11.7470W.
- ↑ "TNKS - Poly [ADP-ribose] polymerase tankyrase-1 - Homo sapiens (Human) - TNKS gene & protein". https://www.uniprot.org/uniprot/O95271.
- ↑ "The 26S proteasome: a molecular machine designed for controlled proteolysis". Annu. Rev. Biochem. 68: 1015–68. 1999. doi:10.1146/annurev.biochem.68.1.1015. PMID 10872471.
- ↑ "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. Nov 2003. doi:10.1016/s0014-5793(03)01063-9. PMID 14596906.
- ↑ "Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis". J. Biol. Chem. 278 (7): 5195–204. Feb 2003. doi:10.1074/jbc.M201988200. PMID 12475993.
- ↑ 10.0 10.1 "The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)". J. Biol. Chem. 277 (16): 14116–26. Apr 2002. doi:10.1074/jbc.M112266200. PMID 11854288.
- ↑ 11.0 11.1 "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner". J. Biol. Chem. 277 (35): 31887–92. Aug 2002. doi:10.1074/jbc.M203916200. PMID 12080061.
- ↑ "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres". Mol. Cell. Biol. 22 (1): 332–42. Jan 2002. doi:10.1128/mcb.22.1.332-342.2002. PMID 11739745.
- ↑ "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)". Biochem. J. 361 (Pt 3): 451–9. Feb 2002. doi:10.1042/0264-6021:3610451. PMID 11802774.
Further reading
- "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes". J. Cell Sci. 112 (21): 3649–56. 1999. doi:10.1242/jcs.112.21.3649. PMID 10523501.
- "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles". J. Biol. Chem. 275 (49): 38437–44. 2001. doi:10.1074/jbc.M007635200. PMID 10988299.
- "Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14". J. Biol. Chem. 276 (20): 17172–80. 2001. doi:10.1074/jbc.M009756200. PMID 11278563.
- "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7". J. Biol. Chem. 276 (31): 29393–402. 2001. doi:10.1074/jbc.M101778200. PMID 11382755.
- "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres". Mol. Cell. Biol. 22 (1): 332–42. 2002. doi:10.1128/MCB.22.1.332-342.2002. PMID 11739745.
- "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)". Biochem. J. 361 (Pt 3): 451–9. 2002. doi:10.1042/0264-6021:3610451. PMID 11802774.
- "The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)". J. Biol. Chem. 277 (16): 14116–26. 2002. doi:10.1074/jbc.M112266200. PMID 11854288.
- "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner". J. Biol. Chem. 277 (35): 31887–92. 2002. doi:10.1074/jbc.M203916200. PMID 12080061.
- "Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length". J. Mol. Biol. 323 (2): 217–24. 2002. doi:10.1016/S0022-2836(02)00946-4. PMID 12381316.
- "Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis". J. Biol. Chem. 278 (7): 5195–204. 2003. doi:10.1074/jbc.M201988200. PMID 12475993.
- "POT1 as a terminal transducer of TRF1 telomere length control". Nature 423 (6943): 1013–8. 2003. doi:10.1038/nature01688. PMID 12768206. Bibcode: 2003Natur.423.1013L.
- "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. 2003. doi:10.1016/S0014-5793(03)01063-9. PMID 14596906.
- "Functional subdomain in the ankyrin domain of tankyrase 1 required for poly(ADP-ribosyl)ation of TRF1 and telomere elongation". Mol. Cell. Biol. 24 (5): 1944–55. 2004. doi:10.1128/MCB.24.5.1944-1955.2004. PMID 14966275.
- "Resolution of sister telomere association is required for progression through mitosis". Science 304 (5667): 97–100. 2004. doi:10.1126/science.1094754. PMID 15064417. Bibcode: 2004Sci...304...97D.
- "TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex". Nat. Genet. 36 (6): 618–23. 2004. doi:10.1038/ng1360. PMID 15133513.
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