| First Author | Kaminker PG | Year | 2001 |
| Journal | J Biol Chem | Volume | 276 |
| Issue | 38 | Pages | 35891-9 |
| PubMed ID | 11454873 | Mgi Jnum | J:71663 |
| Mgi Id | MGI:2150540 | Doi | 10.1074/jbc.M105968200 |
| Citation | Kaminker PG, et al. (2001) Tank2, a new trf1-associated poly(adp-ribose) polymerase, causes rapid induction of cell death upon overexpression. J Biol Chem 276(38):35891-9 |
| abstractText | Tankyrase (TANK1) is a human telomere-associated poly(ADP-ribose) polymerase (PARP) that binds the telomere-binding protein TRF1 and increases telomere length when overexpressed. Here we report characterization of a second human tankyrase, tankyrase 2 (TANK2), which can also interact with TRF1 but has properties distinct from those of TANK1. TANK2 is encoded by a 66-kilobase pair gene (TNKS2) containing 28 exons, which express a 6.7-kilobase pair mRNA and a 1166-amino acid protein. The protein shares 85% amino acid identity with TANK1 in the ankyrin repeat, sterile alpha-motif, and PARP catalytic domains but has a unique N-terminal domain, which is conserved in the murine TNKS2 gene. TANK2 interacted with TRF1 in yeast and in vitro and localized predominantly to a perinuclear region, similar to the properties of TANK1. In contrast to TANK1, however, TANK2 caused rapid cell death when highly overexpressed. TANK2-induced death featured loss of mitochondrial membrane potential, but not PARP1 cleavage, suggesting that TANK2 kills cells by necrosis. The cell death was prevented by the PARP inhibitor 3-aminobenzamide. In vivo, TANK2 may differ from TANK1 in its intrinsic or regulated PARP activity or its substrate specificity. |
