Histone propionylation is a mark of active chromatin

Autor: Raphaël Margueron, Robert H. Schneider, Aaron Taudt, Anna Nieborak, Florian Richter, Marijke P. Baltissen, Helena de Fatima Magliarelli, Gergö Meszaros, Maria Colomé-Tatché, Sylvain Daujat, Michiel Vermeulen, Lara Zorro Shahidian, Stéphanie Le Gras, Gerhard Mittler, Diana Aguilar Gómez, Adam Fiseha Kebede, Romeo Ricci

Publikováno v: Nature Structural & Molecular Biology, 24, 12, pp. 1048-1062
Nature Structural & Molecular Biology, 24(12), 1048-1056. Nature Publishing Group
Nature Structural & Molecular Biology, 24, 1048-1062

Histones are highly covalently modified, but the functions of many of these modifications remain unknown. In particular, it is unclear how histone marks are coupled to cellular metabolism and how this coupling affects chromatin architecture. We ident

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6776958a02e47f0e3f4215a2e9338aa
https://hdl.handle.net/2066/207705

Protein kinase D at the Golgi controls NLRP3 inflammasome activation

Autor: Zhirong, Zhang, Gergö, Meszaros, Wan-Ting, He, Yanfang, Xu, Helena, de Fatima Magliarelli, Laurent, Mailly, Michael, Mihlan, Yansheng, Liu, Marta, Puig Gámez, Alexander, Goginashvili, Adrien, Pasquier, Olga, Bielska, Bénédicte, Neven, Pierre, Quartier, Rudolf, Aebersold, Thomas F, Baumert, Philippe, Georgel, Jiahuai, Han, Romeo, Ricci

Publikováno v: The Journal of Experimental Medicine

Zhang et al. show that Golgi-mediated protein kinase D (PKD) signaling is required and sufficient for NLRP3 inflammasome activation. PKD at the Golgi phosphorylates NLRP3 to release it from mitochondria-associated endoplasmic reticulum membranes, all

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bdd5f053c22872a5d4a8ac13d557ebef
https://pubmed.ncbi.nlm.nih.gov/28716882