A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases.
AUX/IAAs
Duet expression system
auto-ubiquitination of TIR1
co-expression recombinant proteins
detection of ubiquitination
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
25 Sep 2024
25 Sep 2024
Historique:
received:
28
05
2024
revised:
20
09
2024
accepted:
23
09
2024
medline:
26
10
2024
pubmed:
26
10
2024
entrez:
26
10
2024
Statut:
epublish
Résumé
Ubiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible for substrate recognition, are the most abundant and varied proteins in the cascade and the most studied. SKP1-CUL1-F-Box (SCF)-type E3 ubiquitin ligases are multi-subunit RING (Really Interesting New Gene) E3 ubiquitin ligases, composed of CUL1 (Cullin 1), RBX1 (RING BOX 1), SKP1 (S-phase Kinase-associated Protein 1), and F-box proteins. In vitro ubiquitination assays, used for studying the specific recognition of substrate proteins by E3 ubiquitin ligases, require the purification of all components involved in the cascade, and for assays with SCF-type E3 ligases, additional proteins (several SCF complex subunits). Here, the
Identifiants
pubmed: 39456142
pii: biom14101209
doi: 10.3390/biom14101209
pii:
doi:
Substances chimiques
SKP Cullin F-Box Protein Ligases
EC 2.3.2.27
Ubiquitin-Protein Ligases
EC 2.3.2.27
Cullin Proteins
0
Cullin 1
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Natural Science Foundation of Gansu Province
ID : 22JR5RA462, 23JRRA1141
Organisme : Fundamental Research Funds for the Central Universities
ID : lzujbky-2023-22, lzujbky-2023-it20