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Regulation of tankyrase activity by a catalytic domain dimer interface.

Abstract：

:Tankyrases (TNKS and TNKS2) are enzymes that catalyze poly-ADP-ribosylation (PARsylation) of their target proteins. Tankyrase-mediated PARsylation plays critical regulatory roles in cell signaling, particularly in the Wnt/β-catenin pathway. The sterile alpha motif (SAM) domain in tankyrases mediates their oligomerization, which is essential for tankyrase function. The oligomerization regulates the catalytic activity of tankyrases, but the underlying mechanism is unclear. Our analyses of crystal structures of the tankyrase catalytic domain suggest that formation of a head-to-head dimer regulates the catalytic activity. Our activity assays show that residues in the catalytic domain dimer interface are important for the PARsylation activity of tankyrases both in solution and cells. The dimer is weak and may only form in the context of the SAM domain-mediated oligomers of tankyrases, consistent with the dependence of the tankyrase activity on the SAM domain.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Fan C,Yarravarapu N,Chen H,Kulak O,Dasari P,Herbert J,Yamaguchi K,Lum L,Zhang X

doi

10.1016/j.bbrc.2018.07.113

subject

Has Abstract

pub_date

2018-09-10 00:00:00

pages

1780-1785

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)31615-2

journal_volume

503

pub_type

杂志文章

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