MICAL-like protein 2 (MICALL2)

MICAL-like protein 2 (MICALL2) is a cytoskeletal regulatory protein belonging to the MICAL family, characterized by the presence of a calponin homology domain, a LIM domain, and a coiled-coil C-terminal domain[1][2][6]. MICALL2 functions primarily as a key regulator of actin cytoskeleton organization, linking Rab GTPase signaling (notably Rab13) to both cytoskeletal dynamics and membrane trafficking[1][2][4][5][6]. It facilitates the endocytic recycling of cell adhesion molecules (such as occludin, claudin, E-cadherin), thus playing a major role in the formation and maintenance of tight and adherens junctions in epithelial cells[4][5]. By interacting with actin and actin-associated proteins (filamin, actinin), MICALL2 directly stabilizes and bundles F-actin fibers, while its association with Rab13 mediates conformational activation, leading to actin remodeling and ruffle formation at the cell periphery[6]. MICALL2 is highly expressed in various cancers, where it promotes cell migration, invasion, and proliferation, and may influence oncogenic signaling pathways such as Wnt/β-catenin and c-Myc stabilization[1]. The gene is also implicated in rare genetic disorders including Joubert syndrome 1 and dyschromatosis universalis hereditaria based on gene association data[5]. While crucial for multiple physiological processes related to cell structure and adhesion, MICALL2 does not currently constitute a direct therapeutic target (for small molecules, biologics, or approved drugs), nor are there known drugs, mechanisms of actions, or established safety concerns relating to direct modulation of this protein.

Other names

MICAL-L2JRABJunctional Rab13-binding proteinMolecule interacting with CasL-like 2MGC46023FLJ23471