NDLI: Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling.

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Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sims, Joshua J. Scavone, Francesco Cooper, Eric M. Kane, Lesley A. Youle, Richard J. Boeke, Jef D. Cohen, Robert E.
Description	Country affiliation: United States Author Affiliation: Sims JJ ( Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA.)
Abstract	Polyubiquitin chain topology is thought to direct modified substrates to specific fates, but this function-topology relationship is poorly understood, as are the dynamics and subcellular locations of specific polyubiquitin signals. Experimental access to these questions has been limited because linkage-specific inhibitors and in vivo sensors have been unavailable. Here we present a general strategy to track linkage-specific polyubiquitin signals in yeast and mammalian cells, and to probe their functions. We designed several high-affinity Lys63 polyubiquitin-binding proteins and demonstrate their specificity in vitro and in cells. We apply these tools as competitive inhibitors to dissect the polyubiquitin-linkage dependence of NF-κB activation in several cell types, inferring the essential role of Lys63 polyubiquitin for signaling via the IL-1ß and TNF-related weak inducer of apoptosis (TWEAK) but not TNF- receptors. We anticipate live-cell imaging, proteomic and biochemical applications for these tools and extension of the design strategy to other polymeric ubiquitin-like protein modifications.
File Format	HTM / HTML
ISSN	15487091
e-ISSN	15487105
DOI	10.1038/nmeth.1888
Journal	Nature Methods
Issue Number	3
Volume Number	9
Language	English
Publisher	Nature Publishing Group
Publisher Date	2012-02-05
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Clinical Laboratory Techniques Molecular Probe Techniques Protein Interaction Mapping Signal Transduction Physiology Ubiquitin Metabolism Animals Binding Sites Protein Binding Research Support, N.i.h., Extramural Research Support, N.i.h., Intramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology Biotechnology

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Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling

E6AP/UBE3A ubiquitin ligase harbors two E2~ubiquitin binding sites.

Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture.

Structural insights into interactions between ubiquitin specific protease 5 and its polyubiquitin substrates by mass spectrometry and ion mobility spectrometry.

Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T.

Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.

Exploring functional roles of multibinding protein interfaces.

Protein interaction data curation: the International Molecular Exchange (IMEx) consortium.

An integrated suite of fast docking algorithms.

Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling.

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Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling

E6AP/UBE3A ubiquitin ligase harbors two E2~ubiquitin binding sites.

Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture.

Structural insights into interactions between ubiquitin specific protease 5 and its polyubiquitin substrates by mass spectrometry and ion mobility spectrometry.

Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T.

Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.

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Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling.