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  How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini

Sherpa, D., Chrustowicz, J., & Schulman, B. (2022). How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini. Molecular Cell, 82(8), 1424-1438. doi:10.1016/j.molcel.2022.02.004.

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 Creators:
Sherpa, D.1, Author           
Chrustowicz, J.1, Author           
Schulman, Brenda1, Author           
Affiliations:
1Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466699              

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Free keywords: rule pathway structural basis molecular-basis recognition component substrate recognition cellular-proteins cohesin subunit gid complex n-degron ubr box Biochemistry & Molecular Biology Cell Biology
 Abstract: Specificity of eukaryotic protein degradation is determined by E3 ubiquitin ligases and their selective binding to protein motifs, termed ???degrons,???in substrates for ubiquitin-mediated proteolysis. From the discovery of the first substrate degron and the corresponding E3 to a flurry of recent studies enabled by modern systems and structural methods, it is clear that many regulatory pathways depend on E3s recognizing protein termini. Here, we review the structural basis for recognition of protein termini by E3s and how this recognition underlies biological regulation. Diverse E3s evolved to harness a substrate???s N and/or C terminus (and often adjacent residues as well) in a sequence-specific manner. Regulation is achieved through selective activation of E3s and also through generation of degrons at ribosomes or by posttranslational means. Collectively, many E3 interactions with protein N and C termini enable intricate control of protein quality and responses to cellular signals.

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Language(s): eng - English
 Dates: 2022-04-21
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000804371300009
DOI: 10.1016/j.molcel.2022.02.004
ISSN: 1097-2765
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 82 (8) Sequence Number: - Start / End Page: 1424 - 1438 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929