golgin

Golgin is a family of coiled-coil proteins that localize to the Golgi apparatus and function as vesicle tethering factors in the secretory pathway. These proteins are characterized by long coiled-coil domains that extend into the cytosol, enabling them to reach and capture transport carriers that are arriving at or moving within the Golgi network. Most golgins associate with Golgi membranes through specific targeting domains or interactions with other Golgi residents, placing them in strategic positions to influence trafficking.

Functionally, golgins act as initial tethers that capture vesicles from sources such as the endoplasmic reticulum or endosomes and help deliver them to the appropriate Golgi subcompartment. They work in concert with Rab GTPases and SNARE proteins to promote vesicle docking and fusion, and they contribute to the maintenance of Golgi ribbon structure and cisternal organization. Disruption of golgin function can impair trafficking pathways and alter Golgi morphology, underscoring their role in organelle integrity and secretion.

Notable members of the golgin family include GM130 (also known as GOLGA2), giantin (GOLGB1), GMAP210, Golgin-97, Golgin-84, and Golgin-245 (p230). The family is evolutionarily conserved across eukaryotes, with varying repertoires among species. In addition to their basic trafficking roles, golgins have been implicated in developmental processes and cellular organization, reflecting their importance for proper secretory pathway function.

See also: Golgi apparatus, vesicle trafficking, Rab GTPases, SNAREs.