SUMO and ubiquitin are related eukaryotic protein ‘tags’ that covalently modify substrate proteins to alter their stability, their intracellular localization or their interactions with other proteins. Although they have distinct functions and use independent enzymatic machineries to control their conjugation to substrate proteins, recent studies have revealed several direct and indirect functional interactions of the two protein tags, as Praefcke et al. describe on pages 23–31 of this issue. Among others, these interactions include alternative tagging of a protein substrate by sumoylation or ubiquitylation, proteolytic targeting of SUMO-modified proteins by addition of ubiquitin tags, and modifying the activity of enzymes controlling one modifier by their conjugation to the other. Cover design by Ana Fuejo.
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SUMO playing tag with ubiquitin
SUMO and ubiquitin are related eukaryotic protein ‘tags’ that covalently modify substrate proteins to alter their stability, their intracellular localization or their interactions with other proteins. In this Review, Gerrit Praefcke, Kay Hofmann and Jürgen Dohmen describe functional interactions between the two tag systems that influence genome stability and cell growth.
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The ATM protein kinase and cellular redox signaling: beyond the DNA damage response
The ataxia–telangiectasia mutated (ATM) protein kinase has a key role in the DNA damage response and also functions as a redox sensor. Here, Scott Ditch and Tanya Paull describe how ATM can be directly activated by oxidation and review the importance of this protein in oxidative stress responses, ATM-deficient patients and in cancer cells.
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Also in this issue:
Is there a twist in the Escherichia coli signal recognition particle pathway?
The enzymes of bacterial census and censorship
The complexity of cardiolipin in health and disease
![]() | When proteins do not fold properly, or fail to interact in the right manner with other proteins, cells either refold them or degrade them. However, sometimes this protein quality control fails, which can lead to cell death and human disease. Here, we highlight recent reviews that discuss these mechanisms and how they are controlled, as well as their importance in cell biology and human health.
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TiBS publishes papers online ahead of the print issue. Here are some of the latest:
| Zhou Intrinsic disorder: signaling via highly specific but short-lived association | Bieniossek et al. MultiBac: expanding the research toolbox for multiprotein complexes | |
| Grasby et al. Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases | Silverman et al. SCF ubiquitin ligases in the maintenance of genome stability |
These are the five most downloaded papers for the 30 days preceding February 4, 2012. See full list of most read articles