Highlights from The FEBS Journal - August 2017

The highlights from issue 15 include research that sheds light on DNA damage response signalling, and a Viewpoint on the roles of the inflammasome during nucleic-acid- and histone-driven ‘sterile inflammation’.

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Aug 07, 2017
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The heat shock protein 90 (Hsp90α) modulates the stability of several DNA damage response (DDR) proteins including MRE11/RAD50/NBN (MRN trimer). di Masi and colleagues now reveal that NBN and the ataxia-telangiectasia-mutated (ATM) kinase are Hsp90α clients and that Hsp90α facilitates NBN–ATM crosstalk in response to DNA damage. Upon IR-induced DNA double-strand breaks (DSBs), ATM phosphorylates NBN and Hsp90α. NBN then dissociates from Hsp90α and relocalises to the DSBs together with MRE11 and RAD50 to promote the DDR.

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The inflammasome is a protein complex that forms in the cytoplasm in response to cellular damage or the presence of pathogen-associated molecules resulting from infection. Undegraded self-DNA and histones can also induce inflammasome formation and drive ‘sterile inflammation’. In this Viewpoint, Kanneganti and colleagues discuss the roles of the inflammasome during nucleic-acid- and histone-driven ‘sterile inflammation’ and highlight emerging roles of pathogens and commensal microbes in the development of ‘sterile inflammation’.

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The FEBS Journal

The FEBS Journal is an international journal devoted to the rapid publication of full-length papers covering a wide range of topics in any area of the molecular life sciences.

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