Golgins

Golgins are a family of coiled-coil proteins that reside on the membranes of the Golgi apparatus in eukaryotic cells. They extend into the cytosol and act as vesicle tethering factors, capturing transport carriers as they approach or leave the Golgi.

Most golgins function by recognizing Rab GTPases on vesicles and interacting with other tethering factors and SNAREs to promote tethering and subsequent membrane fusion. In this way, they contribute to the specificity and efficiency of vesicle trafficking between the endoplasmic reticulum and the Golgi, as well as within Golgi compartments.

Golgins are distributed across the Golgi cisternae, with different family members localizing to cis, medial, or trans regions and sometimes to the Golgi periphery. The family is diverse and conserved across many eukaryotes, reflecting a long-standing role in maintaining Golgi architecture and facilitating cargo sorting.

Localization and regulation vary: some golgins are anchored to the Golgi membrane by transmembrane domains, while others are peripherally associated through protein interactions. Golgins can be rearranged during cell cycle progression, such as during mitosis when the Golgi fragments and reassembles after cell division.

Functional disruption of golgins can lead to Golgi fragmentation, trafficking defects, and altered organelle homeostasis. Although most studies focus on cellular phenotypes, perturbations of golgin function have been linked to disease-relevant processes in some contexts.