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Structure paper

TitleStructure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 11, Page 1695-1706, Year 2023
Publish dateSep 28, 2023
AuthorsSi Hoon Park / Juhyun Han / Byung-Cheon Jeong / Ju Han Song / Se Hwan Jang / Hyeongseop Jeong / Bong Heon Kim / Young-Gyu Ko / Zee-Yong Park / Kyung Eun Lee / Jaekyung Hyun / Hyun Kyu Song /
PubMed AbstractDefects 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 rapidly nucleate vesicles ...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 rapidly nucleate vesicles at the site of membrane damage, but the underlying molecular mechanisms remain poorly understood. Here we present the structure of Mus musculus TRIM72, a complete model of a TRIM E3 ubiquitin ligase. We demonstrated that the interaction between TRIM72 and phosphatidylserine-enriched membranes is necessary for its oligomeric assembly and ubiquitination activity. Using cryogenic electron tomography and subtomogram averaging, we elucidated a higher-order model of TRIM72 assembly on the phospholipid bilayer. Combining structural and biochemical techniques, we developed a working molecular model of TRIM72, providing insights into the regulation of RING-type E3 ligases through the cooperation of multiple domains in higher-order assemblies. Our findings establish a fundamental basis for the study of TRIM E3 ligases and have therapeutic implications for diseases associated with membrane repair.
External linksNat Struct Mol Biol / PubMed:37770719 / PubMed Central
MethodsEM (tomography) / EM (subtomogram averaging) / X-ray diffraction
Resolution2.75 - 26.0 Å
Structure data

EMDB-31139: Reconstituted proteoliposomes of TRIM72 in negative curvature #1
Method: EM (tomography)

EMDB-31150: Reconstituted proteoliposomes of TRIM72 in negative curvature #2
Method: EM (tomography)

EMDB-31151: Reconstituted proteoliposomes of TRIM72 in positive curvature #1
Method: EM (tomography)

EMDB-31152: Reconstituted proteoliposomes of TRIM72 in positive curvature #2
Method: EM (tomography)

EMDB-33569: Higher-ordered assembly of mouse TRIM72 WT on the Phosphatidylserine/Cholesterol liposome bilayer
Method: EM (subtomogram averaging) / Resolution: 25.0 Å

EMDB-33582: Higher-ordered assembly of mouse TRIM72 M138R on the Phosphatidylserine/Cholesterol liposome bilayer
Method: EM (subtomogram averaging) / Resolution: 26.0 Å

PDB-7xv2:
TRIM E3 ubiquitin ligase
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-7xyy:
TRIM E3 ubiquitin ligase WT
Method: X-RAY DIFFRACTION / Resolution: 7.1 Å

PDB-7xyz:
TRIM E3 ubiquitin ligase
Method: X-RAY DIFFRACTION / Resolution: 4.62 Å

PDB-7xz0:
TRIM E3 ubiquitin ligase
Method: X-RAY DIFFRACTION / Resolution: 3.28 Å

PDB-7xz1:
TRIM E3 ubiquitin ligase
Method: X-RAY DIFFRACTION / Resolution: 5.2 Å

PDB-7xz2:
TRIM E3 ubiquitin ligase
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / TRIM / Tripartite motif / Ubiquitin ligase / Coiled coil / B-box / PRY-SPRY / LIGASE / METAL BINDING PROTEIN / TRIM72 / MG53

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