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  Decoding the messaging of the ubiquitin system using chemical and protein probes

Henneberg, L. T., & Schulman, B. A. (2021). Decoding the messaging of the ubiquitin system using chemical and protein probes. Cell Chemical Biology, 28(7), 889-902. doi:10.1016/j.chembiol.2021.03.009.

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 Creators:
Henneberg, Lukas T.1, Author           
Schulman, Brenda A.1, Author           
Affiliations:
1Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466699              

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Free keywords: E3 LIGASE; ACTIVATING ENZYME; COMPLEX REVEALS; SELECTIVE DEGRADATION; ALLOSTERIC INHIBITOR; MECHANISM; E1; DISCOVERY; SUBSTRATE; CANCERBiochemistry & Molecular Biology;
 Abstract: Post-translational modification of proteins by ubiquitin is required for nearly all aspects of eukaryotic cell function. The numerous targets of ubiquitylation, and variety of ubiquitin modifications, are often likened to a code, where the ultimate messages are diverse responses to target ubiquitylation. E1, E2, and E3 multi-protein enzymatic assemblies modify specific targets and thus function as messengers. Recent advances in chemical and protein tools have revolutionized our ability to explore the ubiquitin system, through enabling new high-throughput screening methods, matching ubiquitylation enzymes with their cellular targets, revealing intricate allosteric mechanisms regulating ubiquitylating enzymes, facilitating structural revelation of transient assemblies determined by multivalent interactions, and providing new paradigms for inhibiting and redirecting ubiquitylation in vivo as new therapeutics. Here we discuss the development of methods that control, disrupt, and extract the flow of information across the ubiquitin system and have enabled elucidation of the underlying molecular and cellular biology.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Issued
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Cell Chemical Biology
Source Genre: Journal
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Publ. Info: Cell Press
Pages: - Volume / Issue: 28 (7) Sequence Number: - Start / End Page: 889 - 902 Identifier: ISSN: 2451-9456
CoNE: https://pure.mpg.de/cone/journals/resource/2451-9456