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TitleStructural basis of tankyrase activation by polymerization.
Journal, issue, pagesNature, Vol. 612, Issue 7938, Page 162-169, Year 2022
Publish dateNov 23, 2022
AuthorsNisha Pillay / Laura Mariotti / Mariola Zaleska / Oviya Inian / Matthew Jessop / Sam Hibbs / Ambroise Desfosses / Paul C R Hopkins / Catherine M Templeton / Fabienne Beuron / Edward P Morris / Sebastian Guettler /
PubMed AbstractThe poly-ADP-ribosyltransferase tankyrase (TNKS, TNKS2) controls a wide range of disease-relevant cellular processes, including WNT-β-catenin signalling, telomere length maintenance, Hippo ...The poly-ADP-ribosyltransferase tankyrase (TNKS, TNKS2) controls a wide range of disease-relevant cellular processes, including WNT-β-catenin signalling, telomere length maintenance, Hippo signalling, DNA damage repair and glucose homeostasis. This has incentivized the development of tankyrase inhibitors. Notwithstanding, our knowledge of the mechanisms that control tankyrase activity has remained limited. Both catalytic and non-catalytic functions of tankyrase depend on its filamentous polymerization. Here we report the cryo-electron microscopy reconstruction of a filament formed by a minimal active unit of tankyrase, comprising the polymerizing sterile alpha motif (SAM) domain and its adjacent catalytic domain. The SAM domain forms a novel antiparallel double helix, positioning the protruding catalytic domains for recurring head-to-head and tail-to-tail interactions. The head interactions are highly conserved among tankyrases and induce an allosteric switch in the active site within the catalytic domain to promote catalysis. Although the tail interactions have a limited effect on catalysis, they are essential to tankyrase function in WNT-β-catenin signalling. This work reveals a novel SAM domain polymerization mode, illustrates how supramolecular assembly controls catalytic and non-catalytic functions, provides important structural insights into the regulation of a non-DNA-dependent poly-ADP-ribosyltransferase and will guide future efforts to modulate tankyrase and decipher its contribution to disease mechanisms.
External linksNature / PubMed:36418402 / PubMed Central
MethodsEM (helical sym.)
Resolution2.98 Å
Structure data

15520

8aly

EMDB-15520, PDB-8aly:
Cryo-EM structure of human tankyrase 2 SAM-PARP filament (G1032W mutant)
Method: EM (helical sym.) / Resolution: 2.98 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Poly-ADP-ribosyltransferase / Enzyme / Polymer

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