Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.
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Cover Image
Cover Image
The cover shows a metaphorical representation of the anti-CRISPR AcrIIA6, represented as handcuffs, sequestering two Streptococcus thermophilus CRISPR1-Cas9 (St1Cas9) molecules at a time and preventing conformational changes associated with DNA recognition and binding. In the absence of AcrIIA6, St1Cas9 tightly binds to its target DNA, and can proceed to target cleavage. For further information, see the article by Hardouin and Goulet in this issue (pp. 507–516). This cover artwork has been made by Beata Edyta Mierzwa (www.BeataScienceArt.com).
Signal-regulated oxidation of proteins via MICAL
Clara Ortegón Salas, Katharina Schneider, Christopher Horst Lillig, Manuela Gellert; Signal-regulated oxidation of proteins via MICAL. Biochem Soc Trans 29 April 2020; 48 (2): 613–620. doi: https://doi.org/10.1042/BST20190866
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