This article explores the vesicle-mediated protein transport pathways in Yarrowia lipolytica, a dimorphic yeast with strong protein secretion capabilities. The study compares Y. lipolytica with other yeasts, including Saccharomyces cerevisiae, to identify conserved and unique proteins involved in secretion. Key findings include the expansion of the Rab protein family in Y. lipolytica, which may reflect its more complex secretion pathway. The Rab4-related protein is highlighted as potentially involved in membrane recycling, with a deletion of the RAB4 gene leading to changes in colony morphology, dimorphic transition, and membrane permeability. Y. lipolytica also has three copies of the SSO gene, which may contribute to its secretion capacity. Comparative analysis shows that Y. lipolytica proteins are more similar to animal homologues than S. cerevisiae proteins, suggesting a closer evolutionary relationship to animal secretion pathways. The study also identifies several unique proteins in Y. lipolytica, including SNARE proteins and other components of the secretory pathway, which may be related to its dimorphic nature and ability to secrete proteins. Overall, the results support the idea that Y. lipolytica is more representative of vesicular secretion in animals and other fungi than S. cerevisiae. The study provides insights into the molecular mechanisms underlying protein secretion in Y. lipolytica and highlights its potential as a model organism for studying secretion pathways.This article explores the vesicle-mediated protein transport pathways in Yarrowia lipolytica, a dimorphic yeast with strong protein secretion capabilities. The study compares Y. lipolytica with other yeasts, including Saccharomyces cerevisiae, to identify conserved and unique proteins involved in secretion. Key findings include the expansion of the Rab protein family in Y. lipolytica, which may reflect its more complex secretion pathway. The Rab4-related protein is highlighted as potentially involved in membrane recycling, with a deletion of the RAB4 gene leading to changes in colony morphology, dimorphic transition, and membrane permeability. Y. lipolytica also has three copies of the SSO gene, which may contribute to its secretion capacity. Comparative analysis shows that Y. lipolytica proteins are more similar to animal homologues than S. cerevisiae proteins, suggesting a closer evolutionary relationship to animal secretion pathways. The study also identifies several unique proteins in Y. lipolytica, including SNARE proteins and other components of the secretory pathway, which may be related to its dimorphic nature and ability to secrete proteins. Overall, the results support the idea that Y. lipolytica is more representative of vesicular secretion in animals and other fungi than S. cerevisiae. The study provides insights into the molecular mechanisms underlying protein secretion in Y. lipolytica and highlights its potential as a model organism for studying secretion pathways.