Journal article

Publication year: 2015

Pages: 136-143

Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Volume number: 1853

Issue number: 1

ISSN: 0167-4889

eISSN: 1879-2596

Open access status: Bronze

DOI Link: https://doi.org/10.1016/j.bbamcr.2014.10.008

Publisher: Elsevier

Abstract: 

The non-canonical IKK kinase TBK1 serves as an important signal transmitter of the antiviral interferon response, but is also involved in the regulation of further processes such as autophagy. The activity of TBK1 is regulated by posttranslational modifications comprising phosphorylation and ubiquitination. This study identifies SUMOylation as a novel posttranslational TBK1 modification. TBK1 kinase activity is required to allow the attachment of SUMO1 or SUMO2/3 proteins. Since TBK1 does not bind to the E2 enzyme Ubc9, this modification most likely proceeds via trans-SUMOylation. Mass spectrometry allowed identifying 1(694 as the SUMO acceptor site, a residue located in the C-terminal coiled-coil domain which is exclusively responsible for the association with the adaptor proteins NAP1, Sintbad and TANK. SUMO modification at 1(694 contributes to the antiviral function of TBK1 and accordingly the viral protein Gam1 antagonizes this posttranslational modification.

Harvard Citation style: Saul, V., Niedenthal, R., Pich, A., Weber, F. and Schmitz, M. (2015) SUMO modification of TBK1 at the adaptor-binding C-terminal coiled-coil domain contributes to its antiviral activity, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1853(1), pp. 136-143. https://doi.org/10.1016/j.bbamcr.2014.10.008

APA Citation style: Saul, V., Niedenthal, R., Pich, A., Weber, F., & Schmitz, M. (2015). SUMO modification of TBK1 at the adaptor-binding C-terminal coiled-coil domain contributes to its antiviral activity. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853(1), 136-143. https://doi.org/10.1016/j.bbamcr.2014.10.008