Recognition of substrate degrons by E3 ubiquitin ligases and modulation by small-molecule mimicry strategies

[Display omitted] •E3 ligases recruit substrates for proteasomal degradation by recognition of degrons.•Crystal structures reveal the structural basis and mechanism of degron recognition.•Small-molecule degron mimetics can prevent or re-direct substrate recognition.•Small-molecule inducible degrons...

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Published inCurrent opinion in structural biology Vol. 44; pp. 101 - 110
Main Authors Lucas, Xavier, Ciulli, Alessio
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.06.2017
Subjects
Amino Acid Sequence
Animals
Humans
Protein Binding - drug effects
Proteolysis - drug effects
Small Molecule Libraries - pharmacology
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - metabolism
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Abstract [Display omitted] •E3 ligases recruit substrates for proteasomal degradation by recognition of degrons.•Crystal structures reveal the structural basis and mechanism of degron recognition.•Small-molecule degron mimetics can prevent or re-direct substrate recognition.•Small-molecule inducible degrons and PROTACs enable targeted protein degradation. The ubiquitin–proteasome system is a master regulator of protein homeostasis, by which proteins are initially targeted for poly-ubiquitination by E3 ligases and then degraded into short peptides by the proteasome. Nature evolved diverse peptidic motifs, termed degrons, to signal substrates for degradation. We discuss degrons of the N-end rule pathway and also degrons characterized by post-translational modifications, including phosphorylation and hydroxylation. In each case we detail the structural basis of E3 ligase:degron recognition and small-molecule mimicry approaches that disrupt those protein–protein interactions. We present as well genetic and chemical technologies that enable targeted degradation of proteins of interest, namely small-molecule dependent inducible degrons and chemical degraders, for example, proteolysis-targeting chimeras (PROTACs).
AbstractList The ubiquitin-proteasome system is a master regulator of protein homeostasis, by which proteins are initially targeted for poly-ubiquitination by E3 ligases and then degraded into short peptides by the proteasome. Nature evolved diverse peptidic motifs, termed degrons, to signal substrates for degradation. We discuss degrons of the N-end rule pathway and also degrons characterized by post-translational modifications, including phosphorylation and hydroxylation. In each case we detail the structural basis of E3 ligase:degron recognition and small-molecule mimicry approaches that disrupt those protein-protein interactions. We present as well genetic and chemical technologies that enable targeted degradation of proteins of interest, namely small-molecule dependent inducible degrons and chemical degraders, for example, proteolysis-targeting chimeras (PROTACs).
[Display omitted] •E3 ligases recruit substrates for proteasomal degradation by recognition of degrons.•Crystal structures reveal the structural basis and mechanism of degron recognition.•Small-molecule degron mimetics can prevent or re-direct substrate recognition.•Small-molecule inducible degrons and PROTACs enable targeted protein degradation. The ubiquitin–proteasome system is a master regulator of protein homeostasis, by which proteins are initially targeted for poly-ubiquitination by E3 ligases and then degraded into short peptides by the proteasome. Nature evolved diverse peptidic motifs, termed degrons, to signal substrates for degradation. We discuss degrons of the N-end rule pathway and also degrons characterized by post-translational modifications, including phosphorylation and hydroxylation. In each case we detail the structural basis of E3 ligase:degron recognition and small-molecule mimicry approaches that disrupt those protein–protein interactions. We present as well genetic and chemical technologies that enable targeted degradation of proteins of interest, namely small-molecule dependent inducible degrons and chemical degraders, for example, proteolysis-targeting chimeras (PROTACs).
Author Lucas, Xavier
Ciulli, Alessio
Author_xml – sequence: 1
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  surname: Ciulli
  fullname: Ciulli, Alessio
  email: a.ciulli@dundee.ac.uk
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28130986$$D View this record in MEDLINE/PubMed
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Snippet [Display omitted] •E3 ligases recruit substrates for proteasomal degradation by recognition of degrons.•Crystal structures reveal the structural basis and...
The ubiquitin-proteasome system is a master regulator of protein homeostasis, by which proteins are initially targeted for poly-ubiquitination by E3 ligases...
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StartPage 101
SubjectTerms Amino Acid Sequence
Animals
Humans
Protein Binding - drug effects
Proteolysis - drug effects
Small Molecule Libraries - pharmacology
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - metabolism
Title Recognition of substrate degrons by E3 ubiquitin ligases and modulation by small-molecule mimicry strategies
URI https://dx.doi.org/10.1016/j.sbi.2016.12.015
https://www.ncbi.nlm.nih.gov/pubmed/28130986
https://search.proquest.com/docview/1862940069
Volume 44
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