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Ubiquitin signals and beyond

Ubiquitination has been progressively recognized over the past quarter of a century or so as a post-translational regulatory mechanism operating in almost all the fundamental processes of cells. Mono-ubiquitination and poly-ubiquitination of proteins play a part in the regulation of transcription, translation, DNA repair, endocytosis, cell signaling, the cell cycle, and both lysosomal and proteasomal protein degradation. Yet fundamental questions about its mechanism remain unanswered. This series will explore what is currently known about the mechanisms of assembly of the diverse known ubiquitin signals, their disassembly and recognition, and their functions in cells. Relevant research papers published in BMC Biology will be added to the series, with commentary to explain their significance, or put them in context for nonspecialist readers, and submissions will be welcomed.

Ivan Dikic

  1. Review

    Macromolecular juggling by ubiquitylation enzymes

    The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. Members of the E1 and E3 enzyme families can...

    Sonja Lorenz, Aaron J Cantor, Michael Rape and John Kuriyan

    BMC Biology 2013 11:65

    Published on: 25 June 2013

  2. Review

    The pupylation pathway and its role in mycobacteria

    Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is conjugated to lysine re...

    Jonas Barandun, Cyrille L Delley and Eilika Weber-Ban

    BMC Biology 2012 10:95

    Published on: 30 November 2012

  3. Commentary

    p97 complexes as signal integration hubs

    In the ubiquitin-proteasome system, a subset of ubiquitylated proteins requires the AAA+ ATPase p97 (also known as VCP or Cdc48) for extraction from membranes or protein complexes before delivery to the protea...

    Hemmo Meyer

    BMC Biology 2012 10:48

    Published on: 13 June 2012

  4. Research article

    MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors

    During a viral infection, the intracellular RIG-I-like receptors (RLRs) sense viral RNA and signal through the mitochondrial antiviral signaling adaptor MAVS (also known as IPS-1, Cardif and VISA) whose activa...

    Céline Castanier, Naima Zemirli, Alain Portier, Dominique Garcin, Nicolas Bidère, Aimé Vazquez and Damien Arnoult

    BMC Biology 2012 10:44

    Published on: 24 May 2012

  5. Review

    Generation and physiological roles of linear ubiquitin chains

    Ubiquitination now ranks with phosphorylation as one of the best-studied post-translational modifications of proteins with broad regulatory roles across all of biology. Ubiquitination usually involves the addi...

    Henning Walczak, Kazuhiro Iwai and Ivan Dikic

    BMC Biology 2012 10:23

    Published on: 15 March 2012