[Induced degradation of proteins by PROTACs and other strategies: towards promising drugs].
Dégradation induite des protéines par des molécules PROTAC et stratégies apparentées : développements à visée thérapeutique.
Antineoplastic Agents
/ chemistry
Autophagy
Catalysis
Drug Design
Humans
Lysosomes
/ metabolism
Molecular Targeted Therapy
/ methods
Neoplasm Proteins
/ antagonists & inhibitors
Neoplasms
/ drug therapy
Proteasome Endopeptidase Complex
/ metabolism
Protein Conformation
Protein Processing, Post-Translational
/ drug effects
Protein Stability
Proteolysis
/ drug effects
RNA
/ drug effects
RNA-Binding Proteins
/ antagonists & inhibitors
Recombinant Fusion Proteins
/ chemistry
SARS-CoV-2
/ drug effects
Structure-Activity Relationship
Ubiquitin-Protein Ligases
/ metabolism
Ubiquitination
COVID-19 Drug Treatment
PROTAC
PROTACs
colles moléculaires
drugs
dégradation induite de protéines
hydrophobic tagging
molecular glues
médicaments
protéasome
targeted protein degradation
Journal
Biologie aujourd'hui
ISSN: 2105-0686
Titre abrégé: Biol Aujourdhui
Pays: France
ID NLM: 101544020
Informations de publication
Date de publication:
2021
2021
Historique:
received:
18
06
2021
entrez:
16
8
2021
pubmed:
17
8
2021
medline:
21
8
2021
Statut:
ppublish
Résumé
Targeted protein degradation (TPD), discovered twenty years ago through the PROTAC technology, is rapidly developing thanks to the implication of many scientists from industry and academia. PROTAC chimeras are heterobifunctional molecules able to link simultaneously a protein to be degraded and an E3 ubiquitin ligase. This allows the protein ubiquitination and its degradation by 26S proteasome. PROTACs have evolved from small peptide molecules to small non-peptide and orally available molecules. It was shown that PROTACs are capable to degrade proteins considered as "undruggable" i.e. devoid of well-defined pockets and deep grooves possibly occupied by small molecules. Among these "hard to drug" proteins, several can be degraded by PROTACs: scaffold proteins, BAF complex, transcription factors, Ras family proteins. Two PROTACs are clinically tested for breast (ARV471) and prostate (ARV110) cancers. The protein degradation by proteasome is also induced by other types of molecules: molecular glues, hydrophobic tagging (HyT), HaloPROTACs and homo-PROTACs. Other cellular constituents are eligible to induced degradation: RNA-PROTACs for RNA binding proteins and RIBOTACs for degradation of RNA itself (SARS-CoV-2 RNA). TPD has recently moved beyond the proteasome with LYTACs (lysosome targeting chimeras) and MADTACs (macroautophagy degradation targeting chimeras). Several techniques such as screening platforms together with mathematical modeling and computational design are now used to improve the discovery of new efficient PROTACs. Dégradation induite des protéines par des molécules PROTAC et stratégies apparentées : développements à visée thérapeutique. Alors que, pour la plupart, les médicaments actuels sont de petites molécules inhibant l’action d’une protéine en bloquant un site d’interaction, la dégradation ciblée des protéines, découverte il y a une vingtaine d’années via les petites molécules PROTAC, connaît aujourd’hui un très grand développement, aussi bien au niveau universitaire qu’industriel. Cette dégradation ciblée permet de contrôler la concentration intracellulaire d’une protéine spécifique comme peuvent le faire les techniques basées sur les acides nucléiques (oligonucléotides antisens, ARNsi, CRISPR-Cas9). Les molécules PROTAC sont des chimères hétéro-bifonctionnelles capables de lier simultanément une protéine spécifique devant être dégradée et une E3 ubiquitine ligase. Les PROTAC sont donc capables de provoquer l’ubiquitinylation de la protéine ciblée et sa dégradation par le protéasome 26S. De nature peptidique, puis non peptidique, les PROTAC sont maintenant administrables par voie orale. Ce détournement du système ubiquitine protéasome permet aux molécules PROTAC d’élargir considérablement le champ des applications thérapeutiques puisque l’élimination de protéines dépourvues de poches ou de crevasses bien définies, dites difficiles à cibler, devient possible. Cette technologie versatile a conduit à la dégradation d’une grande variété de protéines comme des facteurs de transcription, des sérine/thréonine/tyrosine kinases, des protéines de structure, des protéines cytosoliques, des lecteurs épigénétiques. Certaines ligases telles que VHL, MDM2, cereblon et IAP sont couramment utilisées pour être recrutées par les PROTAC. Actuellement, le nombre de ligases pouvant être utilisées ainsi que la nature des protéines dégradées sont en constante augmentation. Deux PROTAC sont en étude clinique pour les cancers du sein (ARV471) et de la prostate (ARV110). La dégradation spécifique d’une protéine par le protéasome peut aussi être induite par d’autres types de molécules synthétiques : colles moléculaires, marqueurs hydrophobes, HaloPROTAC, homo-PROTAC. D’autres constituants cellulaires sont aussi éligibles à une dégradation induite : ARN-PROTAC pour les protéines se liant à l’ARN et RIBOTAC pour la dégradation de l’ARN lui-même comme celui du SARS-CoV-2. Des dégradations induites en dehors du protéasome sont aussi connues : LYTAC, pour des chimères détournant la dégradation de protéines extracellulaires vers les lysosomes, et MADTAC, pour des chimères détournant la dégradation par macroautophagie. Plusieurs techniques, en particulier des plates-formes de criblage, la modélisation mathématique et la conception computationnelle sont utilisées pour le développement de nouveaux PROTAC efficaces.
Autres résumés
Type: Publisher
(fre)
Dégradation induite des protéines par des molécules PROTAC et stratégies apparentées : développements à visée thérapeutique.
Identifiants
pubmed: 34397373
doi: 10.1051/jbio/2021007
pii: jbio210007
doi:
Substances chimiques
Antineoplastic Agents
0
Neoplasm Proteins
0
RNA-Binding Proteins
0
Recombinant Fusion Proteins
0
RNA
63231-63-0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Proteasome Endopeptidase Complex
EC 3.4.25.1
Types de publication
Journal Article
Langues
fre
Sous-ensembles de citation
IM
Pagination
25-43Commentaires et corrections
Type : ErratumIn
Informations de copyright
© Société de Biologie, 2021.
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