Microtubule associated monooxygenase, calponin and LIM domain containing 1 (MICAL1)

Microtubule associated monooxygenase, calponin and LIM domain containing 1 (MICAL1) is a **flavin-monooxygenase enzyme** that oxidizes specific methionine residues on actin filaments, leading to **actin depolymerization** and preventing their repolymerization[1][4]. MICAL1 acts as a cytoskeletal regulator and connects signaling proteins such as NEDD9/CasL to intermediate filaments, impacting vesicle trafficking and neuronal connectivity[1]. It has roles in negative regulation of apoptosis, redox control of protein function (including CaMKII in cardiac cells), and may contribute to cellular responses under oxidative stress[2][8]. MICAL1 is implicated in various diseases, notably cancer, epilepsy, and cardiac arrhythmias, as well as in redox-dependent signaling pathways. It is part of a larger family of MICAL proteins characterized by actin-binding and FAD-dependent monooxygenase domains, making it unique as a redox-dependent F-actin disassembling factor[4]. Knockout or malfunction of MICAL1 can lead to disease, particularly due to disrupted actin regulation, abnormal redox signaling, and altered cellular connectivity[1][2][8].

Other names

MICAL1MICALNICALMICAL-1Molecule interacting with CasL protein 1NEDD9-interacting protein with calponin homology and LIM domains[F-actin]-monooxygenase MICAL1Protein-methionine sulfoxide oxidase MICAL1DKFZp434B1517FLJ11937FLJ21739

Drugs that inhibit MICAL1 would likely inhibit the enzyme’s methionine monooxygenase activity and thus stabilize actin filaments. Drugs that activate or mimic MICAL1 function may promote actin depolymerization and redox signaling.