conesin

Conesin is a protein complex that plays a crucial role in the transport of vesicles along microtubules in eukaryotic cells. It is named for its conical shape when visualized by electron microscopy. The conesin complex is composed of three major subunits: α, β, and γ. The α subunit is the motor protein that drives the movement of the vesicle, while the β and γ subunits form the neck of the cone and are involved in binding to the vesicle membrane and the microtubule.

Conesin is primarily involved in retrograde transport, the movement of vesicles from the cell periphery back towards the cell center. This process is essential for various cellular functions, including the maintenance of the microtubule network, the transport of organelles, and the regulation of gene expression. Conesin-mediated transport is also important in the development and maintenance of the nervous system, as it is involved in the transport of synaptic vesicles and other organelles along axons.

The conesin complex is regulated by a variety of factors, including phosphorylation, GTP binding, and interactions with other proteins. These regulatory mechanisms allow the complex to adapt to different cellular conditions and ensure the proper functioning of retrograde transport. Mutations in the conesin complex have been linked to several human diseases, including Charcot-Marie-Tooth disease and spinocerebellar ataxia. These diseases are characterized by progressive degeneration of the peripheral and central nervous systems, respectively.