Microtubule associated monooxygenase, calponin and LIM domain containing 3 (MICAL3)

Microtubule associated monooxygenase, calponin and LIM domain containing 3 (MICAL3) is an FAD-dependent monooxygenase enzyme, functioning as a key regulator of the actin cytoskeleton and vesicle trafficking. It catalyzes the oxidation of specific methionine residues on F-actin, promoting actin filament depolymerization and thus modulating cytoskeletal dynamics. MICAL3 also acts as a molecular adaptor and scaffold in several cellular processes: it is essential for vesicle docking and fusion (especially through interactions with Rab8A and the cortical factor ELKS), plays a critical role in ciliogenesis by targeting vesicles to the ciliary base, and regulates cytokinesis by organizing midbody-associated protein complexes to promote cell division. Genetic changes in MICAL3 have been associated with certain ciliopathies and developmental syndromes. MICAL3 shares high structural similarity with other MICAL family members, using conserved mechanisms of autoinhibition and activation involving interactions with Rab GTPases

Other names

MICAL-3KIAA0819KIAA1364Molecule interacting with CasL protein 3[F-actin]-monooxygenase MICAL3[F-actin]-methionine sulfoxide oxidase MICAL3flavoprotein oxidoreductase MICAL3protein-methionine sulfoxide oxidase MICAL3MICA3_HUMAN

Catalytic oxidation of F-actin methionine residues, leading to actin disassembly; Modulation of vesicle docking and fusion by acting as an effector for Rab8A and other Rab GTPases; Scaffold for tethering vesicles via protein-protein interactions