Publications
2020
Goto Akira, Okado Kiyoshi, Martins Nelson, Cai Hua, Barbier Vincent, Lamiable Olivier, Troxler Laurent, Santiago Estelle, Kuhn Lauriane, Paik Donggi, Silverman Neal, Holleufer Andreas, Hartmann Rune, Liu Jiyong, Peng Tao, Hoffmann Jules A, Meignin Carine, Daeffler Laurent, Imler Jean-Luc
The Kinase IKKβ Regulates a STING-and NF-κB-Dependent Antiviral Response Pathway in Drosophila Journal Article
In: Immunity, vol. 52, no. 1, pp. 200, 2020.
Abstract | Links | BibTeX | Tags: antiviral, Drosophila, hoffmann, imler, Kinase, M3i, meignin, STING
@article{goto2020,
title = {The Kinase IKKβ Regulates a STING-and NF-κB-Dependent Antiviral Response Pathway in Drosophila},
author = {Akira Goto and Kiyoshi Okado and Nelson Martins and Hua Cai and Vincent Barbier and Olivier Lamiable and Laurent Troxler and Estelle Santiago and Lauriane Kuhn and Donggi Paik and Neal Silverman and Andreas Holleufer and Rune Hartmann and Jiyong Liu and Tao Peng and Jules A Hoffmann and Carine Meignin and Laurent Daeffler and Jean-Luc Imler
},
url = {https://www-sciencedirect-com.insb.bib.cnrs.fr/science/article/pii/S107476131930528X},
doi = {10.1016/j.immuni.2019.12.009 },
year = {2020},
date = {2020-01-14},
journal = {Immunity},
volume = {52},
number = {1},
pages = {200},
abstract = {Antiviral immunity inDrosophilainvolves RNA inter-ference and poorly characterized inducible re-sponses. Here, we showed that two components ofthe IMD pathway, the kinase dIKKband the tran-scription factor Relish, were required to controlinfection by two picorna-like viruses. We identifieda set of genes induced by viral infection and regu-lated by dIKKband Relish, which included an ortho-log of STING. We showed that dSTING participatedin the control of infection by picorna-like viruses,acting upstream of dIKKbto regulate expression ofNazo, an antiviral factor. Our data reveal an antiviralfunction for STING in an animal model devoid of inter-ferons and suggest an evolutionarily ancient role forthis molecule in antiviral immunity.},
keywords = {antiviral, Drosophila, hoffmann, imler, Kinase, M3i, meignin, STING},
pubstate = {published},
tppubtype = {article}
}
2016
Harashima Hirofumi, Dissmeyer Nico, Hammann Philippe, Nomura Yuko, Kramer Katharina, Nakagami Hirofumi, Schnittger Arp
Modulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1. Journal Article
In: BMC plant biology, vol. 16, no. 1, pp. 209, 2016, ISSN: 1471-2229 1471-2229.
Abstract | Links | BibTeX | Tags: Arabidopsis, Cell cycle, Kinase, Mitosis, Phosphorylation, PPSE, Substrate
@article{harashima_modulation_2016,
title = {Modulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1.},
author = {Hirofumi Harashima and Nico Dissmeyer and Philippe Hammann and Yuko Nomura and Katharina Kramer and Hirofumi Nakagami and Arp Schnittger},
doi = {10.1186/s12870-016-0900-7},
issn = {1471-2229 1471-2229},
year = {2016},
date = {2016-01-01},
journal = {BMC plant biology},
volume = {16},
number = {1},
pages = {209},
abstract = {BACKGROUND: Modulation of protein activity by phosphorylation through kinases and subsequent de-phosphorylation by phosphatases is one of the most prominent cellular control mechanisms. Thus, identification of kinase substrates is pivotal for the understanding of many - if not all - molecular biological processes. Equally, the possibility to deliberately tune kinase activity is of great value to analyze the biological process controlled by a particular kinase. RESULTS: Here we have applied a chemical genetic approach and generated an analog-sensitive version of CDKA;1, the central cell-cycle regulator in Arabidopsis and homolog of the yeast Cdc2/CDC28 kinases. This variant could largely rescue a cdka;1 mutant and is biochemically active, albeit less than the wild type. Applying bulky kinase inhibitors allowed the reduction of kinase activity in an organismic context in vivo and the modulation of plant growth. To isolate CDK substrates, we have adopted a two-dimensional differential gel electrophoresis strategy, and searched for proteins that showed mobility changes in fluorescently labeled extracts from plants expressing the analog-sensitive version of CDKA;1 with and without adding a bulky ATP variant. A pilot set of five proteins involved in a range of different processes could be confirmed in independent kinase assays to be phosphorylated by CDKA;1 approving the applicability of the here-developed method to identify substrates. CONCLUSION: The here presented generation of an analog-sensitive CDKA;1 version is functional and represent a novel tool to modulate kinase activity in vivo and identify kinase substrates. Our here performed pilot screen led to the identification of CDK targets that link cell proliferation control to sugar metabolism, proline proteolysis, and glucosinolate production providing a hint how cell proliferation and growth are integrated with plant development and physiology.},
keywords = {Arabidopsis, Cell cycle, Kinase, Mitosis, Phosphorylation, PPSE, Substrate},
pubstate = {published},
tppubtype = {article}
}