MOK (MAPK/MAK/MRK overlapping kinase) is a serine/threonine protein kinase localized to the ciliary base, cytoplasm, and nucleus that functions as a negative regulator of cilium length through cAMP and mTORC1 signaling pathways. Beyond its ciliary role, MOK exhibits previously uncharacterized immune functions in microglia. Specifically, MOK phosphorylates bromodomain-containing protein 4 (Brd4) at serine 492, promoting its binding to cytokine gene promoters and thereby controlling inflammatory and type-I interferon responses 1. This immune regulatory function has significant disease relevance: MOK expression is elevated in amyotrophic lateral sclerosis (ALS) spinal cord tissue, particularly in microglial cells, and contributes to microglia-mediated neurotoxic inflammation that damages motor neurons 1. Clinically, MOK inhibition shows therapeutic promise—chemical MOK inhibitors administered to ALS model mice effectively modulate phospho-Brd4 levels, suppress microglial activation, and modify disease progression 1. These findings establish MOK as a dual-function kinase with roles in both ciliary homeostasis and neuroinflammatory regulation, positioning it as a potential therapeutic target for ALS and related neuroinflammatory conditions.