GOLGA7B is a Golgi-localized accessory protein that regulates protein S-acylation (palmitoylation) and cell adhesion. Functionally, GOLGA7B acts as a stabilizing factor for the palmitoyltransferase DHHC5 at the plasma membrane 1. GOLGA7B itself is S-acylated by DHHC5, and this modification prevents clathrin-mediated endocytosis of DHHC5, maintaining its membrane localization 1. The DHHC5/GOLGA7B complex preferentially associates with adhesion proteins, particularly desmosomal components, and is required for palmitoylation of adhesion substrates such as desmoglein-2 and plakophilin-3, which are necessary for proper desmosomal organization 1. Additionally, GOLGA7B shares functional similarity with the related accessory protein GCP16, both stabilizing DHHC acyltransferases through conserved C-terminal cysteine motifs; GOLGA7B specifically enhances stability of DHHC5 and DHHC8 but not other DHHC9 subfamily members 2. Disease relevance includes associations with clear cell renal cell carcinoma, where GOLGA7B is coregulated with sphingolipid metabolism genes and tumor suppressors 3, and with acne vulgaris through nutrigenomic pathways linking high glycemic index diets 4. These findings position GOLGA7B as an essential regulator of protein acylation dynamics and cell adhesion.