TRIM72

TRIM72 (Tripartite Motif Containing 72) is a Protein Coding gene. Among its related pathways are Cardiac conduction and Smooth Muscle Contraction. Gene Ontology (GO) annotations related to TRIM72 include phosphatidylserine binding. An important paralog of TRIM72 is TRIM50.

Tripartite Motif Containing 72

Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca2+-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).

Biological Process exocytosis Source:UniProtKB-KW
Biological Process muscle organ development Source:UniProtKB
Biological Process muscle system process Source:UniProtKB
Biological Process negative regulation of insulin receptor signaling pathway Source:Ensembl
Biological Process negative regulation of insulin-like growth factor receptor signaling pathway Source:Ensembl
Biological Process negative regulation of myotube differentiation Source:Ensembl
Biological Process plasma membrane repair Source:UniProtKB
Biological Process proteasome-mediated ubiquitin-dependent protein catabolic process Source:GO_Central1 Publication
Biological Process protein homooligomerization Source:UniProtKB
Biological Process protein ubiquitination Source:GO_Central1 Publication

Cell membrane, sarcolemma
Cytoplasmic vesicle membrane
Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.

Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.
S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.