BMC Biology | Article collections | Ubiquitin signals and beyond

Submit a manuscript Register Contact us Follow us on Twitter

Explore BMC Biology

Advertisement

Articles

Ubiquitin signals and beyond

Collection published: 15 March 2012

Last updated: 25 June 2013

Ubiquitin signals and beyond Consulting Editor: Ivan Dikic

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.

		Review Macromolecular juggling by ubiquitylation enzymes Sonja Lorenz, Aaron J Cantor, Michael Rape, John Kuriyan BMC Biology 2013, 11:65 (25 June 2013) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Post-translational modification with ubiquitin requires several distinct catalytic steps three of which must be performed serially by a single enzyme. Lorenz, Kuriyan and colleagues review the macromolecular juggling involved, with an animation set to music performed by the first author
		Review The pupylation pathway and its role in mycobacteria Jonas Barandun, Cyrille L Delley, Eilika Weber-Ban BMC Biology 2012, 10:95 (30 November 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Small-molecule post-translational modification of proteins, long thought to be exclusive to eukaryotes, has recently turned up in Actinobacteria, including the pathogen M .tuberculosis, in which the structurally unrelated pupylation pathway seems functionally analogous to eukaryotic ubiquitination. Eilika Weber-Ban and colleagues review what is known of its mechanisms and meaning.
		Commentary p97 complexes as signal integration hubs Hemmo Meyer BMC Biology 2012, 10:48 (13 June 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary The AAA+ ATPase p97 is known to extract proteins from membranes or complexes for routing to the proteasome for degradation, but Hemmo Meyer, commenting on a recent article from Alexandru and colleagues in BMC Biology, draws attention to increasing evidence that it is a versatile hub for the formation of complexes with distinct functions in cell physiology.
		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 Céline Castanier, Naima Zemirli, Alain Portier, Dominique Garcin, Nicolas Bidère, Aimé Vazquez, Damien Arnoult BMC Biology 2012, 10:44 (24 May 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary A number of proteins are now known to sense viral infection in cells and signal antiviral responses. Studies by Damien Arnoult and colleagues suggest that the interferon response involves the sequential assembly and proteasomal dissolution of a signalling complex at the mitochondrial surface.
		Research article UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1α accumulation Susanne Bandau, Axel Knebel, Zoe O Gage, Nicola T Wood, Gabriela Alexandru BMC Biology 2012, 10:36 (26 April 2012) Abstract \| Full text \| PDF \| PubMed \| Cited on BioMed Central \| Editor’s summary p97 is a AAA+ ATPase that extracts proteins from membranes and protein complexes for ubiquitin-dependent degradation. Gabriela Alexandru and colleagues suggest how its interaction with the ubiquitinating complex CUL2 may regulate HIF1alpha degradation in normoxia.
		Review Signaling-mediated control of ubiquitin ligases in endocytosis Simona Polo BMC Biology 2012, 10:25 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Simona Polo reviews the role of ubiquitination in the regulation of signaling by endocytosis, drawing parallels with the regulation of signalling pathways by phoshorylation.
		Review Following Ariadne's thread: a new perspective on RBR ubiquitin ligases Dawn M Wenzel, Rachel E Klevit BMC Biology 2012, 10:24 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Cited on BioMed Central \| Editor’s summary The RING-between-RING (RBR) ubiquitin ligases were assumed on the basis of their homologous RING domains to assemble ubiquitin chains by the same mechanism.
		Review Generation and physiological roles of linear ubiquitin chains Henning Walczak, Kazuhiro Iwai, Ivan Dikic BMC Biology 2012, 10:23 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Henning Walczak, Kazuhiro Iwai and Ivan Dikic explain what is known of the assembly of linear ubiquitin chains, and discuss the evidence for their role in the regulation of inflammatory immune responses.
		Editorial Ubiquitin ligases and beyond Ivan Dikic, Miranda Robertson BMC Biology 2012, 10:22 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Ivan Dikic and Miranda Robertson introduce a new series on the assembly and many functions of ubiquitin chains.

		Review Macromolecular juggling by ubiquitylation enzymes Sonja Lorenz, Aaron J Cantor, Michael Rape, John Kuriyan BMC Biology 2013, 11:65 (25 June 2013) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Post-translational modification with ubiquitin requires several distinct catalytic steps three of which must be performed serially by a single enzyme. Lorenz, Kuriyan and colleagues review the macromolecular juggling involved, with an animation set to music performed by the first author
		Review The pupylation pathway and its role in mycobacteria Jonas Barandun, Cyrille L Delley, Eilika Weber-Ban BMC Biology 2012, 10:95 (30 November 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Small-molecule post-translational modification of proteins, long thought to be exclusive to eukaryotes, has recently turned up in Actinobacteria, including the pathogen M .tuberculosis, in which the structurally unrelated pupylation pathway seems functionally analogous to eukaryotic ubiquitination. Eilika Weber-Ban and colleagues review what is known of its mechanisms and meaning.
		Commentary p97 complexes as signal integration hubs Hemmo Meyer BMC Biology 2012, 10:48 (13 June 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary The AAA+ ATPase p97 is known to extract proteins from membranes or complexes for routing to the proteasome for degradation, but Hemmo Meyer, commenting on a recent article from Alexandru and colleagues in BMC Biology, draws attention to increasing evidence that it is a versatile hub for the formation of complexes with distinct functions in cell physiology.
		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 Céline Castanier, Naima Zemirli, Alain Portier, Dominique Garcin, Nicolas Bidère, Aimé Vazquez, Damien Arnoult BMC Biology 2012, 10:44 (24 May 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary A number of proteins are now known to sense viral infection in cells and signal antiviral responses. Studies by Damien Arnoult and colleagues suggest that the interferon response involves the sequential assembly and proteasomal dissolution of a signalling complex at the mitochondrial surface.
		Research article UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1α accumulation Susanne Bandau, Axel Knebel, Zoe O Gage, Nicola T Wood, Gabriela Alexandru BMC Biology 2012, 10:36 (26 April 2012) Abstract \| Full text \| PDF \| PubMed \| Cited on BioMed Central \| Editor’s summary p97 is a AAA+ ATPase that extracts proteins from membranes and protein complexes for ubiquitin-dependent degradation. Gabriela Alexandru and colleagues suggest how its interaction with the ubiquitinating complex CUL2 may regulate HIF1alpha degradation in normoxia.
		Review Signaling-mediated control of ubiquitin ligases in endocytosis Simona Polo BMC Biology 2012, 10:25 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Simona Polo reviews the role of ubiquitination in the regulation of signaling by endocytosis, drawing parallels with the regulation of signalling pathways by phoshorylation.
		Review Following Ariadne's thread: a new perspective on RBR ubiquitin ligases Dawn M Wenzel, Rachel E Klevit BMC Biology 2012, 10:24 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Cited on BioMed Central \| Editor’s summary The RING-between-RING (RBR) ubiquitin ligases were assumed on the basis of their homologous RING domains to assemble ubiquitin chains by the same mechanism.
		Review Generation and physiological roles of linear ubiquitin chains Henning Walczak, Kazuhiro Iwai, Ivan Dikic BMC Biology 2012, 10:23 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Henning Walczak, Kazuhiro Iwai and Ivan Dikic explain what is known of the assembly of linear ubiquitin chains, and discuss the evidence for their role in the regulation of inflammatory immune responses.
		Editorial Ubiquitin ligases and beyond Ivan Dikic, Miranda Robertson BMC Biology 2012, 10:22 (15 March 2012) Abstract \| Full text \| PDF \| PubMed \| Editor’s summary Ivan Dikic and Miranda Robertson introduce a new series on the assembly and many functions of ubiquitin chains.