E3 ubiquitin-protein ligase TRIM36 (TRIM36)

E3 ubiquitin-protein ligase TRIM36 is a cytoskeletal-associated enzyme of the tripartite motif (TRIM) family, characterized by a RING finger, B-box type 1 and 2, and coiled-coil domains, with prominent roles in ubiquitinating target proteins and regulating their degradation via the proteasome[1][2][3]. TRIM36 is notably involved in cell cycle regulation, chromosome segregation, and organization of the microtubule cytoskeleton, as well as being essential for embryonic dorso–ventral axis formation and neural tube closure in early development[1]. It is also highly expressed in testis, participating in the acrosome reaction during spermatogenesis[1]. Loss-of-function mutations result in neural tube defects such as anencephaly, and disruptions in its activity are linked to cellular proliferation and apoptotic changes, hinting at possible tumor suppressor or oncogenic functions depending on context[1][2][3]. There are no known drugs directly targeting TRIM36 as of current knowledge.

Other names

Tripartite motif-containing protein 36HaprinRING finger protein 98RNF98Zinc-binding protein Rbcc728ANPHANPH1RBCC728

For hypothetical drugs: Inhibition or modulation of E3 ligase activity (would affect substrate ubiquitination and degradation)