The Golgi apparatus is a complex and dynamic organelle that functions in protein sorting and modification. Numerous structural and regulatory proteins are involved in the budding, docking, and fusion of Golgi-directed vesicles. Golgin-84 is an integral membrane protein associated with the Golgi. Sequence analysis of the C-terminal region of Golgin-84 demonstrates a 14 residue region extending into the lumen of the Golgi, a membrane insertion sequence, and a Golgi retention signal. The large N-terminal cytoplasmic region contains a coiled-coil domain that is required for dimerization and two leucine zipper domains. Golgin-84 is ubiquitously expressed, but is abundant in testis. Golgin-84 has sequence homology to coiled-coil containing myosin family members and to several other Golgi proteins, including trans-Golgi p230 and gigantin. Trans-Golgi p230 has been implicated in the biogenesis of specific Golgi vesicles, while gigantin is implicated in the tethering of non-clathrin coated vesicles and in the anchoring of adjacent Golgi cisternae. Thus, Golgin-84 may have similar roles in vesicle biogenesis, docking, and fusion at the Golgi interface.
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