GOLGA5 (golgin A5) is a coiled-coil protein localized to the Golgi apparatus that functions primarily in maintaining Golgi structural organization and facilitating intra-Golgi retrograde vesicle transport 1. The protein acts as a tethering factor for vesicle docking between the endoplasmic reticulum and Golgi apparatus 2, and stimulates formation of Golgi stacks and ribbons through protein homodimerization and small GTPase binding activities. Mechanistically, GOLGA5 is essential for extracellular matrix (ECM) protein production and secretion, particularly type I collagen and fibronectin 2. Its depletion causes Golgi fragmentation in the perinuclear region and downregulation of fibroblastic differentiation markers 2. GOLGA5 transcription is suppressed during persistent Chlamydia trachomatis infection, correlating with reduced Golgi fragmentation 3. Despite in vitro evidence of functional importance, GOLGA5 knockout mice develop normally without compromised embryonic development, postnatal survival, or fertility, suggesting functional redundancy in vivo 1. However, disease relevance exists: GOLGA5 variants associate with myelin oligodendrocyte glycoprotein-IgG-positive acute disseminated encephalomyelitis in pediatric patients 4, and GOLGA5 expression predicts survival outcomes in colorectal adenocarcinoma metastases 5. Additionally, GOLGA5 participates in RET fusion oncogenes in radiation-induced thyroid carcinoma 6.