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Cover Picture: Dissecting Ubiquitin Signaling with Linkage‐Defined and Protease Resistant Ubiquitin Chains (Angew. Chem. Int. Ed. 47/2014)
Author(s) -
Schneider Tatjana,
Schneider Daniel,
Rösner Daniel,
Malhotra Saurav,
Mortensen Franziska,
Mayer Thomas U.,
Scheffner Martin,
Marx Andreas
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201408957
Subject(s) - ubiquitin , chemistry , biochemistry , stereochemistry , gene
The fate of poly‐ubiquitylated proteins is determined by the linkage type of the ubiquitin chains attached. In their Communication on page 12925 ff., T. U. Mayer, M. Scheffner, A. Marx et al. report a straightforward method that relies on codon expansion and bioorthogonal polymerization to generate linkage‐defined and protease‐resistant ubiquitin chains. These chains can be used to analyze ubiquitin signaling in cell extracts, as demonstrated by a study of linkage‐dependent effects on cell‐cycle progression.