Tankyrase (TRF1-interacting ankyrin-related ADP-ribose polymerase, Tankyase 1, TANK1, TNKS1) is a protein with homology to ankyrins as well as to the catalytic domain of poly (adenosine diphosphate-ribose) polymerase (PARP) (1).
Tankyrase localizes to telomeres by binding to the telomeric repeat binding factor 1 (TRF1) through its ankyrin repeats.
TRF1 is a negative regulator of telomere length maintenance.
Tankyrase exhibits PARP activity functioning as acceptors for adenosine diphosphate (ADP)-ribosylation.
Since ADP-ribosylation of TRF1 diminishes its ability to bind to telomeric DNA, this suggests that telomere function in human cells is regulated by poly (ADP)-ribosylation.
Both the cell cycle and TRF1 may regulate the subcellular localization of tankyrase.
During interphase tankyrase colocalizes with TRF1 to telomeres plus nuclear pore complexes whereas during mitosis tankyrase localizes around the pericentriolar matrix of mitotic chromosomes.
Tankyrase 2 (TRF1-interacting akyrin-related ADP-ribose polymerase 2, TANK2, TNKS2) is a closely related homolog of tankyrase 1.
Tankyrase 2 lacks the N-terminus HPS domain (containing homo-polymeric runs of histidine, proline, and serine) found in tankyrase 1.
Applications:Suitable for use in Peptide ELISA and Western Blot.
