Bacterial pathogens have evolved innumerable tactics to enhance their survival in eukaryotic hosts by evading host cell defenses. Notably, the secretion of proteins to modulate host cell membrane dynamics through unique means is one broad method that aids in bacterial survival, as seen in the case of each of the bacteria presented in this work: Wolbachia pipientis, Rhodococcus equi, and Vibrio parahaemolyticus. Through the use of the model eukaryotic host, Saccharomyces cerevisiae, the unique means by which a protein from each of the aforementioned bacteria manipulates host membrane dynamics for survival have been analyzed and include the modulation of actin dynamics (wBm0076), endosomal maturation and membrane trafficking (wBm0152, VapA, VopQ), and autophagic processes (VopQ). wBm0076 is an actin modulator that causes cell bloating and lysis in S. cerevisiae while wBm0152 modulates the vacuole protein sorting trafficking pathway. A ligand for VapA binding at the macrophage membrane has been identified and explored in greater detail through mutations in specific regions of VapA, however its activity as a modulator of endosome maturation remains unknown. Finally, VopQ is shown to bind specifically VO containing membranes through its interaction with Vma3p and block vacuole:vacuole fusion. The unique inhibitory behavior of VopQ has led to its utilization as a model protein inhibitor in fusion reactions and means to evaluate historically debated roles of the V-ATPase inyeast fusion events, specifically in regards to vacuolar acidification. Collectively, the function of each protein described presents the well-conserved target for bacterial invaders or symbionts of eukaryotic hosts as membrane dynamics. Through modulation of membrane dynamics in S. cerevisiae as a model host, such proteins demonstrate features necessary for successful bacterial invasion and/or intracellular survival and provide continued evidence for the effectivity of using S. cerevisiae to identify bacterial effector or virulence associated proteins.