Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane
SH Park, J Han, BC Jeong, JH Song, SH Jang… - Nature Structural & …, 2023 - nature.com
Defects in plasma membrane repair can lead to muscle and heart diseases in humans.
Tripartite motif-containing protein (TRIM) 72 (mitsugumin 53; MG53) has been determined to …
Tripartite motif-containing protein (TRIM) 72 (mitsugumin 53; MG53) has been determined to …
Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase
DM Dawidziak, JG Sanchez, JM Wagner… - Proteins: Structure …, 2017 - Wiley Online Library
Tripartite motif (TRIM) proteins comprise a large family of RING‐type ubiquitin E3 ligases
that regulate important biological processes. An emerging general model is that TRIMs form …
that regulate important biological processes. An emerging general model is that TRIMs form …
Structural insights into the TRIM family of ubiquitin E3 ligases
TRIM proteins play important roles in a wide range of biological processes, including cell
proliferation, differentiation, development, apoptosis, oncogenesis and innate immunity [1 …
proliferation, differentiation, development, apoptosis, oncogenesis and innate immunity [1 …
Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity
MG Koliopoulos, D Esposito, E Christodoulou… - The EMBO …, 2016 - embopress.org
TRIM E3 ubiquitin ligases regulate a wide variety of cellular processes and are particularly
important during innate immune signalling events. They are characterized by a conserved …
important during innate immune signalling events. They are characterized by a conserved …
Does it take two to tango? RING domain self-association and activity in TRIM E3 ubiquitin ligases
F Fiorentini, D Esposito… - Biochemical Society …, 2020 - portlandpress.com
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 …
domain comprising a RING domain, one or two B-box domains and a coiled-coil region …
Structural basis for TRIM72 oligomerization during membrane damage repair
Y Ma, L Ding, Z Li, C Zhou - Nature Communications, 2023 - nature.com
Abstract Tripartite Motif Protein 72 (TRIM72, also named MG53) mediates membrane
damage repair through membrane fusion and exocytosis. During injury, TRIM72 molecules …
damage repair through membrane fusion and exocytosis. During injury, TRIM72 molecules …
Structural determinants of TRIM protein function
D Esposito, MG Koliopoulos… - Biochemical Society …, 2017 - portlandpress.com
Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of Really Interesting
New Gene (RING) E3 ubiquitin ligases and contribute to the regulation of numerous cellular …
New Gene (RING) E3 ubiquitin ligases and contribute to the regulation of numerous cellular …
Ubiquitination of E3 ubiquitin ligase TRIM5α and its potential role
K Yamauchi, K Wada, K Tanji, M Tanaka… - The FEBS …, 2008 - Wiley Online Library
HIV‐1 efficiently infects susceptible cells and causes AIDS in humans. Although HIV can
also enter the cells of Old World monkeys, it encounters a block before reverse transcription …
also enter the cells of Old World monkeys, it encounters a block before reverse transcription …
Functional interactions between ubiquitin E2 enzymes and TRIM proteins
LM Napolitano, EG Jaffray, RT Hay… - Biochemical …, 2011 - portlandpress.com
The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite
motif module, composed of a RING domain, one or two B-box domains and a coiled-coil …
motif module, composed of a RING domain, one or two B-box domains and a coiled-coil …
Trim-Away ubiquitinates and degrades lysine-less and N-terminally acetylated substrates
TRIM proteins are the largest family of E3 ligases in mammals. They include the intracellular
antibody receptor TRIM21, which is responsible for mediating targeted protein degradation …
antibody receptor TRIM21, which is responsible for mediating targeted protein degradation …