dyneinin

Dynein is a family of ATP-dependent motor proteins that move along microtubules toward the minus end, converting chemical energy into mechanical work. The dynein family includes cytoplasmic dynein, which transports vesicles, organelles, and protein complexes within the cell, and axonemal dynein, which powers the beating of cilia and flagella. Both classes are large multi-subunit complexes; the motor activity resides in the heavy chains that form an AAA+ ATPase motor domain, while intermediate and light chains, along with accessory proteins such as dynactin, mediate cargo binding, regulatory interactions, and complex assembly.

In cells, cytoplasmic dynein supports retrograde transport in neurons, Golgi apparatus positioning, and spindle dynamics during mitosis. Axonemal dyneins generate ciliary and flagellar motility by producing sliding forces between adjacent microtubule doublets. Regulation of dynein activity involves multiple factors, including dynein adaptors and regulators such as LIS1 and the dynactin complex, which influence cargo binding and processivity.

Genetic defects in dynein components and regulators underlie human disease. Axonemal dynein arm defects cause primary ciliary dyskinesia, a disorder characterized by chronic respiratory infections, situs abnormalities, and infertility in some cases. Mutations in cytoplasmic dynein heavy chain genes (for example DYNC1H1) and in regulators like LIS1 are associated with neurodevelopmental disorders, including cortical malformations and intellectual disability. Research into dynein function continues to illuminate fundamental cellular logistics and the pathogenesis of ciliopathies and neurodevelopmental diseases.