Does it take two to tango? RING domain self-association and activity in TRIM E3 ubiquitin ligases.
Amino Acid Motifs
Animals
Apoptosis
Catalysis
Catalytic Domain
Dimerization
Humans
Models, Molecular
Protein Conformation
Protein Domains
Protein Multimerization
Protein Structure, Secondary
Signal Transduction
Tripartite Motif Proteins
/ chemistry
Ubiquitin-Protein Ligases
/ metabolism
Ubiquitination
TRIM proteins
protein structure
ring ligases
ubiquitin ligases
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
18 12 2020
18 12 2020
Historique:
received:
12
09
2020
revised:
16
10
2020
accepted:
19
10
2020
pubmed:
11
11
2020
medline:
10
8
2021
entrez:
10
11
2020
Statut:
ppublish
Résumé
TRIM proteins form a protein family that is characterized by a conserved tripartite motif domain comprising a RING domain, one or two B-box domains and a coiled-coil region. Members of this large protein family are important regulators of numerous cellular functions including innate immune responses, transcriptional regulation and apoptosis. Key to their cellular role is their E3 ligase activity which is conferred by the RING domain. Self-association is an important characteristic of TRIM protein activity and is mediated by homodimerization via the coiled-coil region, and in some cases higher order association via additional domains of the tripartite motif. In many of the TRIM family proteins studied thus far, RING dimerization is an important prerequisite for E3 ligase enzymatic activity though the propensity of RING domains to dimerize differs significantly between different TRIMs and can be influenced by other regions of the protein.
Identifiants
pubmed: 33170204
pii: 226927
doi: 10.1042/BST20200383
pmc: PMC7752041
doi:
Substances chimiques
Tripartite Motif Proteins
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2615-2624Informations de copyright
© 2020 The Author(s).